Abstract
Chromogranin A (CHGA), a member of the granin family of proteins, has been an attractive therapeutic target and candidate biomarker for several cardiovascular, neurological, and inflammatory disorders. The prominence of CHGA stems from the pleiotropic roles of several bioactive peptides (e.g., catestatin, pancreastatin, vasostatins) generated by its proteolytic cleavage and by their wide anatomical distribution. These peptides are emerging as novel modulators of cardiometabolic diseases that are often linked to high blood cholesterol levels. However, their impact on cholesterol homeostasis is poorly understood. The dynamic nature of cholesterol and its multitudinous roles in almost every aspect of normal body function makes it an integral component of metabolic physiology. A tightly regulated coordination of cholesterol homeostasis is imperative for proper functioning of cellular and metabolic processes. The deregulation of cholesterol levels can result in several pathophysiological states. Although studies till date suggest regulatory roles for CHGA and its derived peptides on cholesterol levels, the mechanisms by which this is achieved still remain unclear. This review aims to aggregate and consolidate the available evidence linking CHGA with cholesterol homeostasis in health and disease. In addition, we also look at common molecular regulatory factors (viz., transcription factors and microRNAs) which could govern the expression of CHGA and genes involved in cholesterol homeostasis under basal and pathological conditions. In order to gain further insights into the pathways mediating cholesterol regulation by CHGA/its derived peptides, a few prospective signaling pathways are explored, which could act as primers for future studies.
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Availability of data and material
The datasets analyzed during the current study are available from the corresponding author on reasonable request.
Change history
12 October 2023
Error in the Table 1 has been updated.
06 November 2023
A Correction to this paper has been published: https://doi.org/10.1007/s00018-023-04990-7
References
Taupenot L, Harper KL, O’Connor DT (2003) The chromogranin-secretogranin family. N Engl J Med 348(12):1134–1149
Winkler H, Fischer-Colbrie R (1992) The chromogranins A and B: the first 25 years and future perspectives. Neuroscience 49(3):497–528
Bartolomucci A et al (2011) The extended granin family: structure, function, and biomedical implications. Endocr Rev 32(6):755–797
Wiedenmann B, Huttner WB (1989) Synaptophysin and chromogranins/secretogranins–widespread constituents of distinct types of neuroendocrine vesicles and new tools in tumor diagnosis. Virchows Arch B Cell Pathol Incl Mol Pathol 58(2):95–121
Montero-Hadjadje M et al (2008) Chromogranins A and B and secretogranin II: evolutionary and functional aspects. Acta Physiol (Oxf) 192(2):309–324
Kim T et al (2001) Chromogranin A, an “on/off” switch controlling dense-core secretory granule biogenesis. Cell 106(4):499–509
Taupenot L et al (2002) Identification of a novel sorting determinant for the regulated pathway in the secretory protein chromogranin A. J Cell Sci 115(Pt 24):4827–4841
Tooze SA, Martens GJ, Huttner WB (2001) Secretory granule biogenesis: rafting to the SNARE. Trends Cell Biol 11(3):116–122
Videen JS et al (1992) Calcium and catecholamine interactions with adrenal chromogranins. comparison of driving forces in binding and aggregation. J Biol Chem 267(5):3066–3073
Yoo SH (1992) Identification of the Ca(2+)-dependent calmodulin-binding region of chromogranin A. Biochemistry 31(26):6134–6140
Mahapatra NR et al (2004) A dynamic pool of calcium in catecholamine storage vesicles. exploration in living cells by a novel vesicle-targeted chromogranin A-aequorin chimeric photoprotein. J Biol Chem 279(49):51107–51121
Borges R et al (2010) Chromogranins as regulators of exocytosis. J Neurochem 114(2):335–343
Pasqua T et al (2016) Impact of Chromogranin A deficiency on catecholamine storage, catecholamine granule morphology and chromaffin cell energy metabolism in vivo. Cell Tissue Res 363(3):693–712
Díaz-Vera J et al (2012) Chromogranins A and B are key proteins in amine accumulation, but the catecholamine secretory pathway is conserved without them. FASEB J 26(1):430–438
Mahata SK, Corti A (2019) Chromogranin A and its fragments in cardiovascular, immunometabolic, and cancer regulation. Ann N Y Acad Sci 1455(1):34–58
Pasqua T et al (2019) Modulation of the coronary tone in the expanding scenario of Chromogranin-A and its derived peptides. Future Med Chem 11(12):1501–1511
Muntjewerff EM et al (2018) Catestatin as a target for treatment of inflammatory diseases. Front Immunol 9:2199
Garg R et al (2023) Chromogranin A-derived peptides pancreastatin and catestatin: emerging therapeutic target for diabetes. Amino Acids 54(5):549
Bozic J et al (2021) Catestatin as a biomarker of cardiovascular diseases: a clinical perspective. Biomedicines 9(12):1757
Bourebaba Y et al (2021) Catestatin peptide of chromogranin A as a potential new target for several risk factors management in the course of metabolic syndrome. Biomed Pharmacother 134:111113
Watanabe T (2021) The emerging roles of chromogranins and derived polypeptides in atherosclerosis, diabetes, and coronary heart disease. Int J Mol Sci 22(11):6118
Jati S et al (2023) Catestatin: antimicrobial functions and potential therapeutics. Pharmaceutics 15(5):1550
Mahata SK et al (1997) Novel autocrine feedback control of catecholamine release A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest 100(6):1623–1633
Mahapatra NR (2008) Catestatin is a novel endogenous peptide that regulates cardiac function and blood pressure. Cardiovasc Res 80(3):330–338
Mahata SK et al (2003) Catecholamine secretory vesicle stimulus-transcription coupling in vivo. demonstration by a novel transgenic promoter/photoprotein reporter and inhibition of secretion and transcription by the chromogranin A fragment catestatin. J Biol Chem 278(34):32058–32067
Mahata SK et al (2010) Catestatin: a multifunctional peptide from chromogranin A. Regul Pept 162(1–3):33–43
Tatemoto K et al (1986) Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature 324(6096):476–478
O’Connor DT et al (2005) Pancreastatin: multiple actions on human intermediary metabolism in vivo, variation in disease, and naturally occurring functional genetic polymorphism. J Clin Endocrinol Metab 90(9):5414–5425
Sánchez-Margalet V et al (2010) Reprint of: Metabolic effects and mechanism of action of the chromogranin A-derived peptide pancreastatin. Regul Pept 165(1):71–77
Gayen JR et al (2009) A novel pathway of insulin sensitivity in chromogranin A null mice: a crucial role for pancreastatin in glucose homeostasis. J Biol Chem 284(42):28498–28509
Tota B et al (2008) The chromogranin A-derived vasostatins: new players in the endocrine heart. Curr Med Chem 15(14):1444–1451
Aardal S, Helle KB (1992) The vasoinhibitory activity of bovine chromogranin A fragment (vasostatin) and its independence of extracellular calcium in isolated segments of human blood vessels. Regul Pept 41(1):9–18
Helle KB (2010) The chromogranin A-derived peptides vasostatin-I and catestatin as regulatory peptides for cardiovascular functions. Cardiovasc Res 85(1):9–16
Fleming I (2023) Vasostatin-2, angiogenesis and collateral function. Eur Heart J 44(19):1745
Brown MS, Goldstein JL (1986) A receptor-mediated pathway for cholesterol homeostasis. Science 232(4746):34–47
Rezen T et al (2011) Interplay between cholesterol and drug metabolism. Biochim Biophys Acta 1814(1):146–160
Lippincott-Schwartz J, Phair RD (2010) Lipids and cholesterol as regulators of traffic in the endomembrane system. Annu Rev Biophys 39:559–578
Bretscher MS, Munro S (1993) Cholesterol and the Golgi apparatus. Science 261(5126):1280–1281
Mesmin B, Antonny B (2016) The counterflow transport of sterols and PI4P. Biochim Biophys Acta 1861(8(8 Pt B)):940–951
Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387(6633):569–572
Sezgin E et al (2017) The mystery of membrane organization: composition, regulation and roles of lipid rafts. Nat Rev Mol Cell Biol 18(6):361–374
Byfield FJ et al (2004) Cholesterol depletion increases membrane stiffness of aortic endothelial cells. Biophys J 87(5):3336–3343
Gondre-Lewis MC et al (2006) Abnormal sterols in cholesterol-deficiency diseases cause secretory granule malformation and decreased membrane curvature. J Cell Sci 119(Pt 9):1876–1885
Burger K, Gimpl G, Fahrenholz F (2000) Regulation of receptor function by cholesterol. Cell Mol Life Sci 57(11):1577–1592
Pucadyil TJ, Chattopadhyay A (2006) Role of cholesterol in the function and organization of G-protein coupled receptors. Prog Lipid Res 45(4):295–333
Incardona JP, Eaton S (2000) Cholesterol in signal transduction. Curr Opin Cell Biol 12(2):193–203
Burgess TL, Kelly RB (1987) Constitutive and regulated secretion of proteins. Annu Rev Cell Biol 3:243–293
Braakman I, Bulleid NJ (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem 80:71–99
Halban PA, Irminger JC (1994) Sorting and processing of secretory proteins. Biochem J 299(Pt 1):1–18
Tooze SA (1998) Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells. Biochim Biophys Acta 1404(1–2):231–244
Arvan P, Castle D (1998) Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem J 332(Pt 3):593–610
Tanguy E et al (2016) Lipids implicated in the journey of a secretory granule: from biogenesis to fusion. J Neurochem 137(6):904–912
Westhead EW (1987) Lipid composition and orientation in secretory vesicles. Ann N Y Acad Sci 493:92–100
Dhanvantari S, Loh YP (2000) Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. J Biol Chem 275(38):29887–29893
Orci L et al (1981) Topology of morphologically detectable protein and cholesterol in membranes of polypeptide-secreting cells. Philos Trans R Soc Lond B Biol Sci 296(1080):47–54
Wang R et al (2006) Molecular probes for sensing the cholesterol composition of subcellular organelle membranes. Biochim Biophys Acta 1761(10):1169–1181
Wang Y, Thiele C, Huttner WB (2000) Cholesterol is required for the formation of regulated and constitutive secretory vesicles from the trans-Golgi Network. Traffic 1(12):952–962
Lang T et al (2001) SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J 20(9):2202–2213
Zhang J et al (2009) Roles of cholesterol in vesicle fusion and motion. Biophys J 97(5):1371–1380
Ammar MR et al (2013) Lipids in regulated exocytosis: what are they doing? Front Endocrinol (Lausanne) 4:125
Hosaka M et al (2002) Identification of a chromogranin A domain that mediates binding to secretogranin III and targeting to secretory granules in pituitary cells and pancreatic beta-cells. Mol Biol Cell 13(10):3388–3399
Hosaka M et al (2004) Secretogranin III binds to cholesterol in the secretory granule membrane as an adapter for chromogranin A. J Biol Chem 279(5):3627–3634
Hosaka M, Watanabe T (2010) Secretogranin III: a bridge between core hormone aggregates and the secretory granule membrane. Endocr J 57(4):275–286
Baumstark D et al (2019) (1)H NMR spectroscopy quantifies visibility of lipoproteins, subclasses, and lipids at varied temperatures and pressures. J Lipid Res 60(9):1516–1534
Daniels TF et al (2009) Lipoproteins, cholesterol homeostasis and cardiac health. Int J Biol Sci 5(5):474–488
Feingold KR (2021) Introduction to Lipids and Lipoproteins, in Endotext, K.R. Feingold, et al., Editors. MDText.com, Inc., South Dartmouth, MA
Soliman GA (2018) Dietary cholesterol and the lack of evidence in cardiovascular disease. Nutrients 10(6):780
Afonso MS et al (2018) Molecular pathways underlying cholesterol homeostasis. Nutrients 10(6):760
Luo J, Yang H, Song BL (2020) Mechanisms and regulation of cholesterol homeostasis. Nat Rev Mol Cell Biol 21(4):225–245
Ge L et al (2008) The cholesterol absorption inhibitor ezetimibe acts by blocking the sterol-induced internalization of NPC1L1. Cell Metab 7(6):508–519
Garcia CK et al (2001) Autosomal recessive hypercholesterolemia caused by mutations in a putative LDL receptor adaptor protein. Science 292(5520):1394–1398
Morris SM, Cooper JA (2001) Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2(2):111–123
Poirier S et al (2009) Dissection of the endogenous cellular pathways of PCSK9-induced low density lipoprotein receptor degradation: evidence for an intracellular route. J Biol Chem 284(42):28856–28864
Ahamad S, Bhat SA (2022) Recent update on the development of PCSK9 inhibitors for hypercholesterolemia treatment. J Med Chem 65(23):15513–15539
Tabas I (2002) Consequences of cellular cholesterol accumulation: basic concepts and physiological implications. J Clin Invest 110(7):905–911
Ikonen E (2006) Mechanisms for cellular cholesterol transport: defects and human disease. Physiol Rev 86(4):1237–1261
Chang TY et al (2001) Roles of acyl-coenzyme A: cholesterol acyltransferase-1 and -2. Curr Opin Lipidol 12(3):289–296
Arenas F, Garcia-Ruiz C, Fernandez-Checa JC (2017) Intracellular cholesterol trafficking and impact in neurodegeneration. Front Mol Neurosci 10:382
Litvinov DY, Savushkin EV, Dergunov AD (2018) Intracellular and plasma membrane events in cholesterol transport and homeostasis. J Lipids 2018:3965054
Raychaudhuri S, Prinz WA (2010) The diverse functions of oxysterol-binding proteins. Annu Rev Cell Dev Biol 26:157–177
Ngo M, Ridgway ND (2009) Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function. Mol Biol Cell 20(5):1388–1399
Rader DJ et al (2009) The role of reverse cholesterol transport in animals and humans and relationship to atherosclerosis. J Lipid Res 50(Suppl):S189–S194
Soutar AK, Naoumova RP (2007) Mechanisms of disease: genetic causes of familial hypercholesterolemia. Nat Clin Pract Cardiovasc Med 4(4):214–225
Santos RD et al (2016) Defining severe familial hypercholesterolaemia and the implications for clinical management: a consensus statement from the International Atherosclerosis Society Severe Familial Hypercholesterolemia Panel. Lancet Diabetes Endocrinol 4(10):850–861
Benjamin EJ et al (2018) Heart disease and stroke statistics-2018 update: a report from the American Heart Association. Circulation 137(12):e67–e492
St-Pierre AC et al (2001) Comparison of various electrophoretic characteristics of LDL particles and their relationship to the risk of ischemic heart disease. Circulation 104(19):2295–2299
Walldius G et al (2001) High apolipoprotein B, low apolipoprotein A-I, and improvement in the prediction of fatal myocardial infarction (AMORIS study): a prospective study. Lancet 358(9298):2026–2033
Collaboration N.C.D.R.F (2020) Repositioning of the global epicentre of non-optimal cholesterol. Nature 582(7810):73–77
Taverne F et al (2013) Abdominal obesity, insulin resistance, metabolic syndrome and cholesterol homeostasis. PharmaNutrition 1(4):130–136
van der Harst P, Verweij N (2018) Identification of 64 novel genetic loci provides an expanded view on the genetic architecture of coronary artery disease. Circ Res 122(3):433–443
Schunkert H et al (2011) Large-scale association analysis identifies 13 new susceptibility loci for coronary artery disease. Nat Genet 43(4):333–338
Khera AV, Kathiresan S (2017) Genetics of coronary artery disease: discovery, biology and clinical translation. Nat Rev Genet 18(6):331–344
Do R et al (2015) Exome sequencing identifies rare LDLR and APOA5 alleles conferring risk for myocardial infarction. Nature 518(7537):102–106
Erdmann J et al (2009) New susceptibility locus for coronary artery disease on chromosome 3q22.3. Nat Genet 41(3):280–282
Myocardial Infarction Genetics et al (2009) Genome-wide association of early-onset myocardial infarction with single nucleotide polymorphisms and copy number variants. Nat Genet 41(3):334–341
Bergheanu SC, Bodde MC, Jukema JW (2017) Pathophysiology and treatment of atherosclerosis: current view and future perspective on lipoprotein modification treatment. Neth Heart J 25(4):231–242
Escola-Gil JC et al (2014) Sitosterolemia: diagnosis, investigation, and management. Curr Atheroscler Rep 16(7):424
Kolovou GD et al (2006) Tangier disease four decades of research: a reflection of the importance of HDL. Curr Med Chem 13(7):771–782
Bjorkhem I, Meaney S (2004) Brain cholesterol: long secret life behind a barrier. Arterioscler Thromb Vasc Biol 24(5):806–815
Anchisi L et al (2012) Cholesterol homeostasis: a key to prevent or slow down neurodegeneration. Front Physiol 3:486
Zhang J, Liu Q (2015) Cholesterol metabolism and homeostasis in the brain. Protein Cell 6(4):254–264
Vanier MT (2013) Niemann-Pick diseases. Handb Clin Neurol 113:1717–1721
Fiedorowicz JG, Haynes WG (2010) Cholesterol, mood, and vascular health: Untangling the relationship: does low cholesterol predispose to depression and suicide, or vice versa? Curr Psychiatr 9(7):17-A
Arguello G et al (2015) Recent insights on the role of cholesterol in non-alcoholic fatty liver disease. Biochim Biophys Acta 1852(9):1765–1778
Malhotra P et al (2020) Disturbances in cholesterol homeostasis and non-alcoholic fatty liver diseases. Front Med (Lausanne) 7:467
Bernstein DL et al (2013) Cholesteryl ester storage disease: review of the findings in 135 reported patients with an underdiagnosed disease. J Hepatol 58(6):1230–1243
Beaudet AL et al (1977) Cholesterol ester storage disease: clinical, biochemical, and pathological studies. J Pediatr 90(6):910–914
Dugail I, Amri EZ, Vitale N (2020) High prevalence for obesity in severe COVID-19: possible links and perspectives towards patient stratification. Biochimie 179:257–265
Wei X et al (2020) Hypolipidemia is associated with the severity of COVID-19. J Clin Lipidol 14(3):297–304
Marcello A et al (2020) The cholesterol metabolite 27-hydroxycholesterol inhibits SARS-CoV-2 and is markedly decreased in COVID-19 patients. Redox Biol 36:101682
Zhang XJ et al (2020) In-hospital use of statins is associated with a reduced risk of mortality among individuals with COVID-19. Cell Metab 32(2):176-187 e4
Schmidt NM et al (2020) Cholesterol-modifying drugs in COVID-19. Oxf Open Immunol 1(1):iqaa001
Lee W et al (2020) COVID-19-activated SREBP2 disturbs cholesterol biosynthesis and leads to cytokine storm. Signal Transduct Target Ther 5(1):186
Cervin M, Anderson R (1991) Modulation of coronavirus-mediated cell fusion by homeostatic control of cholesterol and fatty acid metabolism. J Med Virol 35(2):142–149
Wei C et al (2020) HDL-scavenger receptor B type 1 facilitates SARS-CoV-2 entry. Nat Metab 2(12):1391–1400
Alfred K., Das chromaffine Gewebe. 1902: Ergeb Anat Entwicklungsgesch. p. 253–348.
Carmon O et al (2020) Chromogranin A preferential interaction with Golgi phosphatidic acid induces membrane deformation and contributes to secretory granule biogenesis. FASEB J 34(5):6769–6790
Yoo SH, Huh YH, Hur YS (2010) Inositol 1,4,5-trisphosphate receptor in chromaffin secretory granules and its relation to chromogranins. Cell Mol Neurobiol 30(8):1155–1161
Mahapatra NR et al (2005) Hypertension from targeted ablation of chromogranin A can be rescued by the human ortholog. J Clin Invest 115(7):1942–1952
Simon JP, Aunis D (1989) Biochemistry of the chromogranin A protein family. Biochem J 262(1):1–13
Friese RS et al (2005) Common genetic mechanisms of blood pressure elevation in two independent rodent models of human essential hypertension. Am J Hypertens 18(5 Pt 1):633–652
Friese RS et al (2010) Global metabolic consequences of the chromogranin A-null model of hypertension: transcriptomic detection, pathway identification, and experimental verification. Physiol Genomics 40(3):195–207
Fantini J, Barrantes FJ (2013) How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains. Front Physiol 4:31
Fantini J et al (2016) Molecular mechanisms of protein-cholesterol interactions in plasma membranes: functional distinction between topological (tilted) and consensus (CARC/CRAC) domains. Chem Phys Lipids 199:52–60
Durakoglugil ME et al (2015) The relationship of plasma catestatin concentrations with metabolic and vascular parameters in untreated hypertensive patients: influence on high-density lipoprotein cholesterol. Anatol J Cardiol 15(7):577–585
Dopp JM, Reichmuth KJ, Morgan BJ (2007) Obstructive sleep apnea and hypertension: mechanisms, evaluation, and management. Curr Hypertens Rep 9(6):529–534
Borovac JA et al (2019) Catestatin serum levels are increased in male patients with obstructive sleep apnea. Sleep Breath 23(2):473–481
Kim J et al (2010) Leukocyte telomere length and plasma catestatin and myeloid-related protein 8/14 concentrations in children with obstructive sleep apnea. Chest 138(1):91–99
Subramanian L et al (2017) A haplotype variant of the human chromogranin A gene (CHGA) promoter increases CHGA expression and the risk for cardiometabolic disorders. J Biol Chem 292(34):13970–13985
Allu PK et al (2014) Naturally occurring variants of the dysglycemic peptide pancreastatin: differential potencies for multiple cellular functions and structure-function correlation. J Biol Chem 289(7):4455–4469
O’Connor DT (1985) Plasma chromogranin A initial studies in human hypertension. Hypertension 7(3 Pt 2):I76–I79
Takiyyuddin MA et al (1995) Chromogranin A in human hypertension influence of heredity. Hypertension 26(1):213–220
O’Connor DT et al (2002) Early decline in the catecholamine release-inhibitory peptide catestatin in humans at genetic risk of hypertension. J Hypertens 20(7):1335–1345
Sanchez-Margalet V et al (1995) Increased plasma pancreastatin-like immunoreactivity levels in non-obese patients with essential hypertension. J Hypertens 13(2):251–258
Funakoshi A et al (1990) Elevated plasma levels of pancreastatin (PST) in patients with non-insulin-dependent diabetes mellitus (NIDDM). Regul Pept 30(2):159–164
Sanchez-Margalet V et al (1998) Increased plasma pancreastatin-like levels in gestational diabetes: correlation with catecholamine levels. Diabetes Care 21(11):1951–1954
Allu PKR et al (2022) Functional Gly297Ser variant of the physiological dysglycemic peptide pancreastatin is a novel risk factor for cardiometabolic disorders. Diabetes 71(3):538–553
Kogawa EM et al (2016) Salivary function impairment in type 2 Diabetes patients associated with concentration and genetic polymorphisms of chromogranin A. Clin Oral Investig 20(8):2083–2095
Kojima M et al (2018) Catestatin prevents macrophage-driven atherosclerosis but not arterial injury-induced neointimal hyperplasia. Thromb Haemost 118(1):182–194
Chen Y et al (2019) Decreased circulating catestatin levels are associated with coronary artery disease: The emerging anti-inflammatory role. Atherosclerosis 281:78–88
Lu L et al (2012) Reduced serum levels of vasostatin-2, an anti-inflammatory peptide derived from chromogranin A, are associated with the presence and severity of coronary artery disease. Eur Heart J 33(18):2297–2306
Bachetti T et al (2017) Plasma levels of vasostatin-1, a chromogranin A fragment, are associated with carotid artery maximum stenosis: a pilot study. Int J Cardiol 236:438–443
Ottesen AH et al (2017) Glycosylated chromogranin A in heart failure: implications for processing and cardiomyocyte calcium homeostasis. Circ Heart Fail 10(2):e003675
Sato Y et al (2018) Inhibitory effects of vasostatin-1 against atherogenesis. Clin Sci (Lond) 132(23):2493–2507
Jansson AM et al (2009) Prognostic value of circulating chromogranin A levels in acute coronary syndromes. Eur Heart J 30(1):25–32
Estensen ME et al (2006) Prognostic value of plasma chromogranin A levels in patients with complicated myocardial infarction. Am Heart J 152(5):927 e1–6
Omland T, Dickstein K, Syversen U (2003) Association between plasma chromogranin a concentration and long-term mortality after myocardial infarction. Am J Med 114(1):25–30
Wang X et al (2011) Dramatic changes in catestatin are associated with hemodynamics in acute myocardial infarction. Biomarkers 16(4):372–377
Meng L et al (2013) Plasma catestatin level in patients with acute myocardial infarction and its correlation with ventricular remodelling. Postgrad Med J 89(1050):193–196
Liu L et al (2013) Plasma levels and potential roles of catestatin in patients with coronary heart disease. Scand Cardiovasc J 47(4):217–224
Xu W et al (2017) Plasma catestatin in patients with acute coronary syndrome. Cardiology 136(3):164–169
Zhu D et al (2017) Catestatin-a novel predictor of left ventricular remodeling after acute myocardial infarction. Sci Rep 7:44168
Zhu D et al (2015) Correlation of plasma catestatin level and the prognosis of patients with acute myocardial infarction. PLoS ONE 10(4):e0122993
Pan WQ et al (2016) Association of decreased serum vasostatin-2 level with ischemic chronic heart failure and with MACE in 3-year follow-up: Vasostatin-2 prevents heart failure in myocardial infarction rats. Int J Cardiol 221:1–11
Kannel WB, McGee DL (1979) Diabetes and cardiovascular risk factors: the Framingham study. Circulation 59(1):8–13
Tobin KA et al (2002) Liver X receptors as insulin-mediating factors in fatty acid and cholesterol biosynthesis. J Biol Chem 277(12):10691–10697
Tian J, Goldstein JL, Brown MS (2016) Insulin induction of SREBP-1c in rodent liver requires LXRalpha-C/EBPbeta complex. Proc Natl Acad Sci U S A 113(29):8182–8187
Penque BA et al (2013) Hexosamine biosynthesis impairs insulin action via a cholesterolgenic response. Mol Endocrinol 27(3):536–547
McNulty PH (2007) Hexosamine biosynthetic pathway flux and cardiomyopathy in type 2 diabetes mellitus focus on “impact of type 2 diabetes and aging on cardiomyocyte function and O-linked N-acetylglucosamine levels in the heart.” Am J Physiol Cell Physiol 292(4):C1243-4
Bhonagiri P et al (2011) Evidence coupling increased hexosamine biosynthesis pathway activity to membrane cholesterol toxicity and cortical filamentous actin derangement contributing to cellular insulin resistance. Endocrinology 152(9):3373–3384
Gonzalez-Yanes C, Sanchez-Margalet V (2000) Pancreastatin modulates insulin signaling in rat adipocytes: mechanisms of cross-talk. Diabetes 49(8):1288–1294
Gallo MP et al (2018) Catestatin induces glucose uptake and GLUT4 trafficking in adult rat cardiomyocytes. Biomed Res Int 2018:2086109
Wu H et al (1995) A functional cyclic AMP response element plays a crucial role in neuroendocrine cell type-specific expression of the secretory granule protein chromogranin A. J Clin Invest 96(1):568–578
Canaff L et al (1998) Analysis of molecular mechanisms controlling neuroendocrine cell specific transcription of the chromogranin A gene. Endocrinology 139(3):1184–1196
Tang K et al (1996) Stimulus-transcription coupling in pheochromocytoma cells. promoter region-specific activation of chromogranin a biosynthesis. J Biol Chem 271(45):28382–28390
Taupenot L et al (1998) Peptidergic activation of transcription and secretion in chromaffin cells. Cis and trans signaling determinants of pituitary adenylyl cyclase-activating polypeptide (PACAP). J Clin Invest 101(4):863–876
Mahapatra NR et al (2003) Secretin activation of chromogranin A gene transcription. identification of the signaling pathways in cis and in trans. J Biol Chem 278(22):19986–19994
Mahata SK et al (1999) Neurotrophin activation of catecholamine storage vesicle protein gene expression: signaling to chromogranin a biosynthesis. Neuroscience 88(2):405–424
Plath T et al (1999) Interferon-alpha inhibits chromogranin A promoter activity in neuroendocrine pancreatic cancer cells. FEBS Lett 458(3):378–382
Hocker M et al (1998) Sp1 and CREB mediate gastrin-dependent regulation of chromogranin A promoter activity in gastric carcinoma cells. J Biol Chem 273(51):34000–34007
Raychowdhury R et al (2002) Interaction of early growth response protein 1 (Egr-1), specificity protein 1 (Sp1), and cyclic adenosine 3’5’-monophosphate response element binding protein (CREB) at a proximal response element is critical for gastrin-dependent activation of the chromogranin A promoter. Mol Endocrinol 16(12):2802–2818
Persson P et al (2004) Olf/EBF proteins are expressed in neuroblastoma cells: potential regulators of the chromogranin A and SCG10 promoters. Int J Cancer 110(1):22–30
Rao F et al (2012) Genetic variation within a metabolic motif in the chromogranin a promoter: pleiotropic influence on cardiometabolic risk traits in twins. Am J Hypertens 25(1):29–40
Chiron S et al (2011) Proteomic analysis yields an unexpected trans-acting point in control of the human sympathochromaffin phenotype. Circ Cardiovasc Genet 4(4):437–445
Chen Y et al (2008) Common genetic variants in the chromogranin A promoter alter autonomic activity and blood pressure. Kidney Int 74(1):115–125
Bailey TL et al (2009) MEME SUITE: tools for motif discovery and searching. Nucleic Acids Res 37(Web Server issue):W202–W208
Fornes O et al (2020) JASPAR 2020: update of the open-access database of transcription factor binding profiles. Nucleic Acids Res 48(D1):D87–D92
Lee C, Huang CH (2013) LASAGNA-Search: an integrated web tool for transcription factor binding site search and visualization. Biotechniques 54(3):141–153
Messeguer X et al (2002) PROMO: detection of known transcription regulatory elements using species-tailored searches. Bioinformatics 18(2):333–334
Chekmenev DS, Haid C, Kel AE (2005) P-Match: transcription factor binding site search by combining patterns and weight matrices. Nucleic Acids Res 33(Web Server issue):W432-7
Zambelli F, Pesole G, Pavesi G (2009) Pscan: finding over-represented transcription factor binding site motifs in sequences from co-regulated or co-expressed genes. Nucleic Acids Res 37(6):W247–W252
Friese RS et al (2013) MicroRNA-22 and promoter motif polymorphisms at the Chga locus in genetic hypertension: functional and therapeutic implications for gene expression and the pathogenesis of hypertension. Hum Mol Genet 22(18):3624–3640
Zhang K et al (2015) Molecular mechanism for hypertensive renal disease: differential regulation of chromogranin A expression at 3′-untranslated region polymorphism C+87T by MicroRNA-107. J Am Soc Nephrol 26(8):1816–1825
Diniz GP et al (2017) Loss of microRNA-22 prevents high-fat diet induced dyslipidemia and increases energy expenditure without affecting cardiac hypertrophy. Clin Sci (Lond) 131(24):2885–2900
Vlachos IS et al (2015) DIANA-miRPath v30: deciphering microRNA function with experimental support. Nucleic Acids Res 43(W1):W460–W466
Dweep H et al (2011) miRWalk–database: prediction of possible miRNA binding sites by “walking” the genes of three genomes. J Biomed Inform 44(5):839–847
Kruger J, Rehmsmeier M (2006) RNAhybrid: microRNA target prediction easy, fast and flexible. Nucleic Acids Res 34(Web Server issue):W451–W454
Goedeke L et al (2015) MicroRNA-148a regulates LDL receptor and ABCA1 expression to control circulating lipoprotein levels. Nat Med 21(11):1280–1289
Wang D et al (2018) Apoptotic cell induction of miR-10b in macrophages contributes to advanced atherosclerosis progression in ApoE-/- mice. Cardiovasc Res 114(13):1794–1805
Rayner KJ et al (2010) MiR-33 contributes to the regulation of cholesterol homeostasis. Science 328(5985):1570–1573
Najafi-Shoushtari SH (2011) MicroRNAs in cardiometabolic disease. Curr Atheroscler Rep 13(3):202–207
Marquart TJ et al (2010) miR-33 links SREBP-2 induction to repression of sterol transporters. Proc Natl Acad Sci U S A 107(27):12228–12232
Price NL et al (2017) Genetic dissection of the impact of miR-33a and miR-33b during the progression of atherosclerosis. Cell Rep 21(5):1317–1330
Li T et al (2013) Regulation of cholesterol and bile acid homeostasis by the cholesterol 7alpha-hydroxylase/steroid response element-binding protein 2/microRNA-33a axis in mice. Hepatology 58(3):1111–1121
Allen RM et al (2012) miR-33 controls the expression of biliary transporters, and mediates statin- and diet-induced hepatotoxicity. EMBO Mol Med 4(9):882–895
Davalos A et al (2011) miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling. Proc Natl Acad Sci U S A 108(22):9232–9237
Strub JM et al (1997) Phosphorylation and O-glycosylation sites of bovine chromogranin A from adrenal medullary chromaffin granules and their relationship with biological activities. J Biol Chem 272(18):11928–11936
Gadroy P et al (1998) Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors. J Biol Chem 273(51):34087–34097
Motoshima H et al (2006) AMPK and cell proliferation–AMPK as a therapeutic target for atherosclerosis and cancer. J Physiol 574(Pt 1):63–71
Viollet B et al (2009) AMP-activated protein kinase in the regulation of hepatic energy metabolism: from physiology to therapeutic perspectives. Acta Physiol (Oxf) 196(1):81–98
Ke R et al (2018) Mechanisms of AMPK in the maintenance of ATP balance during energy metabolism. Cell Biol Int 42(4):384–392
Steinberg GR, Kemp BE (2009) AMPK in health and disease. Physiol Rev 89(3):1025–1078
Clarke PR, Hardie DG (1990) Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. EMBO J 9(8):2439–2446
Omkumar RV, Darnay BG, Rodwell VW (1994) Modulation of Syrian hamster 3-hydroxy-3-methylglutaryl-CoA reductase activity by phosphorylation. role of serine 871. J Biol Chem 269(9):6810–6814
Henin N et al (1995) Inhibition of fatty acid and cholesterol synthesis by stimulation of AMP-activated protein kinase. FASEB J 9(7):541–546
Bandyopadhyay GK et al (2012) Catestatin (chromogranin A(352–372)) and novel effects on mobilization of fat from adipose tissue through regulation of adrenergic and leptin signaling. J Biol Chem 287(27):23141–23151
Prieur X et al (2008) Leptin regulates peripheral lipid metabolism primarily through central effects on food intake. Endocrinology 149(11):5432–5439
Kosztaczky B et al (2007) Leptin stimulates endogenous cholesterol synthesis in human monocytes: new role of an old player in atherosclerotic plaque formation. leptin-induced increase in cholesterol synthesis. Int J Biochem Cell Biol 39(9):1637–1645
Iqbal J et al (2020) Leptin-mediated differential regulation of microsomal triglyceride transfer protein in the intestine and liver affects plasma lipids. J Biol Chem 295(13):4101–4113
Bandyopadhyay GK et al (2015) Pancreastatin-dependent inflammatory signaling mediates obesity-induced insulin resistance. Diabetes 64(1):104–116
Gupta AP et al (2019) Pancreastatin inhibitor activates AMPK pathway via GRP78 and ameliorates dexamethasone induced fatty liver disease in C57BL/6 mice. Biomed Pharmacother 116:108959
Cook KL, Clarke R (2012) Heat shock 70 kDa protein 5/glucose-regulated protein 78 “AMP”ing up autophagy. Autophagy 8(12):1827–1829
Biswas N et al (2014) Discovery of a novel target for the dysglycemic chromogranin A fragment pancreastatin: interaction with the chaperone GRP78 to influence metabolism. PLoS ONE 9(1):e84132
Hossain Z et al (2018) Discovery of pancreastatin inhibitor PSTi8 for the treatment of insulin resistance and diabetes: studies in rodent models of diabetes mellitus. Sci Rep 8(1):8715
Casas C (2017) GRP78 at the centre of the stage in cancer and neuroprotection. Front Neurosci 11:177
Werstuck GH et al (2001) Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest 107(10):1263–1273
Lee JN, Ye J (2004) Proteolytic activation of sterol regulatory element-binding protein induced by cellular stress through depletion of Insig-1. J Biol Chem 279(43):45257–45265
Wang Y et al (2015) GRP78 rescues the ABCG5 ABCG8 sterol transporter in db/db mice. Metabolism 64(11):1435–1443
Liao F et al (2015) Catestatin attenuates endoplasmic reticulum induced cell apoptosis by activation type 2 muscarinic acetylcholine receptor in cardiac ischemia/reperfusion. Sci Rep 5:16590
Chinetti G, Fruchart JC, Staels B (2000) Peroxisome proliferator-activated receptors (PPARs): nuclear receptors at the crossroads between lipid metabolism and inflammation. Inflamm Res 49(10):497–505
Desvergne B, Wahli W (1999) Peroxisome proliferator-activated receptors: nuclear control of metabolism. Endocr Rev 20(5):649–688
Smith U (1983) Adrenergic control of lipid metabolism. Acta Med Scand Suppl 672:41–44
Krone W, Muller-Wieland D, Greten H (1985) Effects of adrenergic antihypertensive drugs on sterol synthesis in freshly isolated human mononuclear leukocytes. J Cardiovasc Pharmacol 7(6):1134–1137
Krone W et al (1984) Stimulation of beta 2-adrenergic receptors suppresses sterol synthesis in human mononuclear leukocytes. Biochim Biophys Acta 804(1):137–140
Petrone A et al (2006) Association of beta2 adrenergic receptor polymorphisms and related haplotypes with triglyceride and LDL-cholesterol levels. Eur J Hum Genet 14(1):94–100
Davidson MH (2015) Beta-2 Agonism: a potential therapeutic target for dyslipidemia. EBioMedicine 2(4):284
Holmes C, Middleton B (1997) Cyclic AMP-mediated control of LDL receptor gene expression in human skin fibroblasts. Biochem Soc Trans 25(2):179S
Martin G et al (1999) Comparison of expression and regulation of the high-density lipoprotein receptor SR-BI and the low-density lipoprotein receptor in human adrenocortical carcinoma NCI-H295 cells. Eur J Biochem 261(2):481–491
Smith JD et al (1996) Cyclic AMP induces apolipoprotein E binding activity and promotes cholesterol efflux from a macrophage cell line to apolipoprotein acceptors. J Biol Chem 271(48):30647–30655
Oram JF et al (2000) ABCA1 is the cAMP-inducible apolipoprotein receptor that mediates cholesterol secretion from macrophages. J Biol Chem 275(44):34508–34511
Bernard DW et al (1991) cAMP stimulates cholesteryl ester clearance to high density lipoproteins in J7774 macrophages. J Biol Chem 266(2):710–716
Sacks FM, Dzau VJ (1986) Adrenergic effects on plasma lipoprotein metabolism. speculation on mechanisms of action. Am J Med 80(2A):71–81
Mazza R et al (2008) Catestatin (chromogranin A344–364) is a novel cardiosuppressive agent: inhibition of isoproterenol and endothelin signaling in the frog heart. Am J Physiol Heart Circ Physiol 295(1):H113–H122
Bassino E et al (2011) A novel catestatin-induced antiadrenergic mechanism triggered by the endothelial PI3K-eNOS pathway in the myocardium. Cardiovasc Res 91(4):617–624
Kiranmayi M et al (2016) Catestatin Gly364Ser variant alters systemic blood pressure and the risk for hypertension in human populations via endothelial nitric oxide pathway. Hypertension 68(2):334–347
Chu SY et al (2020) Catestatin in defense of oxidative-stress-induced apoptosis: a novel mechanism by activating the beta2 adrenergic receptor and PKB/Akt pathway in ischemic-reperfused myocardium. Peptides 123:170200
Cerra MC et al (2006) Recombinant N-terminal fragments of chromogranin-A modulate cardiac function of the Langendorff-perfused rat heart. Basic Res Cardiol 101(1):43–52
Gallo MP et al (2007) Endothelium-derived nitric oxide mediates the antiadrenergic effect of human vasostatin-1 in rat ventricular myocardium. Am J Physiol Heart Circ Physiol 292(6):H2906–H2912
Tota B et al (2012) The novel chromogranin A-derived serpinin and pyroglutaminated serpinin peptides are positive cardiac beta-adrenergic-like inotropes. FASEB J 26(7):2888–2898
Di Scala C et al (2017) Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic acetylcholine receptor and other membrane-bound receptors. Curr Top Membr 80:3–23
Borroni V, Barrantes FJ (2011) Cholesterol modulates the rate and mechanism of acetylcholine receptor internalization. J Biol Chem 286(19):17122–17132
Zhang G et al (2018) Placental mechanism of prenatal nicotine exposure-reduced blood cholesterol levels in female fetal rats. Toxicol Lett 296:31–38
Song W et al (2015) The implication of cigarette smoking and cessation on macrophage cholesterol efflux in coronary artery disease patients. J Lipid Res 56(3):682–691
Sahu BS et al (2012) Molecular interactions of the physiological anti-hypertensive peptide catestatin with the neuronal nicotinic acetylcholine receptor. J Cell Sci 125(9):2323–2337
Wang C et al (2017) Nicotine accelerates atherosclerosis in apolipoprotein E-deficient mice by activating alpha7 nicotinic acetylcholine receptor on mast cells. Arterioscler Thromb Vasc Biol 37(1):53–65
Wu Y et al (2015) Activation of AMPKalpha2 in adipocytes is essential for nicotine-induced insulin resistance in vivo. Nat Med 21(4):373–382
Dong F et al (2014) Akt inhibition promotes ABCA1-mediated cholesterol efflux to ApoA-I through suppressing mTORC1. PLoS ONE 9(11):e113789
Du X et al (2006) Involvement of Akt in ER-to-Golgi transport of SCAP/SREBP: a link between a key cell proliferative pathway and membrane synthesis. Mol Biol Cell 17(6):2735–2745
Penna C et al (2011) Ischemia/reperfusion injury is increased and cardioprotection by a postconditioning protocol is lost as cardiac hypertrophy develops in nandrolone treated rats. Basic Res Cardiol 106(3):409–420
Bi X et al (2018) Endoplasmic reticulum chaperone GRP78 protects heart from ischemia/reperfusion injury through Akt activation. Circ Res 122(11):1545–1554
Bassino E et al (2015) Catestatin exerts direct protective effects on rat cardiomyocytes undergoing ischemia/reperfusion by stimulating PI3K-Akt-GSK3beta pathway and preserving mitochondrial membrane potential. PLoS ONE 10(3):e0119790
Caron A, Richard D, Laplante M (2015) The roles of mTOR complexes in lipid metabolism. Annu Rev Nutr 35:321–348
Lu XY et al (2020) Feeding induces cholesterol biosynthesis via the mTORC1-USP20-HMGCR axis. Nature 588(7838):479–484
Esteve E, Ricart W, Fernandez-Real JM (2005) Dyslipidemia and inflammation: an evolutionary conserved mechanism. Clin Nutr 24(1):16–31
Kim MS et al (2007) Tumor necrosis factor and interleukin 1 decrease RXRalpha, PPARalpha, PPARgamma, LXRalpha, and the coactivators SRC-1, PGC-1alpha, and PGC-1beta in liver cells. Metabolism 56(2):267–279
Zimetti F et al (2017) Plasma cholesterol homeostasis, HDL remodeling and function during the acute phase reaction. J Lipid Res 58(10):2051–2060
Tang ZH et al (2017) New role of PCSK9 in atherosclerotic inflammation promotion involving the TLR4/NF-kappaB pathway. Atherosclerosis 262:113–122
Edfeldt K et al (2002) Expression of toll-like receptors in human atherosclerotic lesions: a possible pathway for plaque activation. Circulation 105(10):1158–1161
Zhou Y et al (2020) The role of toll-like receptors in atherothrombotic cardiovascular disease. ACS Pharmacol Transl Sci 3(3):457–471
Chen H et al (2019) Catestatin prevents endothelial inflammation and promotes thrombus resolution in acute pulmonary embolism in mice. Biosci Rep 39(11):BSR20192236
Fessler MB (2008) Liver X receptor: crosstalk node for the signaling of lipid metabolism, carbohydrate metabolism, and innate immunity. Curr Signal Transduct Ther 3(2):75–81
Ito A et al (2015) LXRs link metabolism to inflammation through Abca1-dependent regulation of membrane composition and TLR signaling. Elife 4:e08009
Manandhar B, Cochran BJ, Rye KA (2020) Role of high-density lipoproteins in cholesterol homeostasis and glycemic control. J Am Heart Assoc 9(1):e013531
Huang X et al (2018) The PI3K/AKT pathway in obesity and type 2 diabetes. Int J Biol Sci 14(11):1483–1496
Stephens JM, Lee J, Pilch PF (1997) Tumor necrosis factor-alpha-induced insulin resistance in 3T3-L1 adipocytes is accompanied by a loss of insulin receptor substrate-1 and GLUT4 expression without a loss of insulin receptor-mediated signal transduction. J Biol Chem 272(2):971–976
Valicherla GR et al (2013) Pancreastatin is an endogenous peptide that regulates glucose homeostasis. Physiol Genom 45(22):1060–1071
Ying W et al (2018) Catestatin inhibits obesity-induced macrophage infiltration and inflammation in the liver and suppresses hepatic glucose production leading to improved insulin sensitivity. Diabetes 67(5):841–848
Kanuri BN et al (2017) Altered glucose and lipid homeostasis in liver and adipose tissue pre-dispose inducible NOS knockout mice to insulin resistance. Sci Rep 7:41009
Strehlow K et al (2000) Angiotensin AT1 receptor over-expression in hypercholesterolaemia. Ann Med 32(6):386–389
Singh BM, Mehta JL (2003) Interactions between the renin-angiotensin system and dyslipidemia: relevance in the therapy of hypertension and coronary heart disease. Arch Intern Med 163(11):1296–1304
Daugherty A et al (2008) Augmentation of the renin-angiotensin system by hypercholesterolemia promotes vascular diseases. Future Lipidol 3(6):625–636
Daugherty A et al (2004) Hypercholesterolemia stimulates angiotensin peptide synthesis and contributes to atherosclerosis through the AT1A receptor. Circulation 110(25):3849–3857
Keidar S et al (1999) Angiotensin II atherogenicity in apolipoprotein E deficient mice is associated with increased cellular cholesterol biosynthesis. Atherosclerosis 146(2):249–257
Keidar S et al (1995) Angiotensin II stimulates macrophage-mediated oxidation of low density lipoproteins. Atherosclerosis 115(2):201–215
Keidar S, Kaplan M, Aviram M (1996) Angiotensin II-modified LDL is taken up by macrophages via the scavenger receptor, leading to cellular cholesterol accumulation. Arterioscler Thromb Vasc Biol 16(1):97–105
Keidar S, Attias J (1997) Angiotensin II injection into mice increases the uptake of oxidized LDL by their macrophages via a proteoglycan-mediated pathway. Biochem Biophys Res Commun 239(1):63–67
Li D et al (1999) Proapoptotic effects of ANG II in human coronary artery endothelial cells: role of AT1 receptor and PKC activation. Am J Physiol 276(3):H786–H792
Phelps T et al (2019) The influence of biological sex and sex hormones on bile acid synthesis and cholesterol homeostasis. Biol Sex Differ 10(1):52
Chinetti G et al (2001) PPAR-alpha and PPAR-gamma activators induce cholesterol removal from human macrophage foam cells through stimulation of the ABCA1 pathway. Nat Med 7(1):53–58
Claudel T et al (2002) Bile acid-activated nuclear receptor FXR suppresses apolipoprotein A-I transcription via a negative FXR response element. J Clin Invest 109(7):961–971
Tao R et al (2013) FoxO3 transcription factor and Sirt6 deacetylase regulate low density lipoprotein (LDL)-cholesterol homeostasis via control of the proprotein convertase subtilisin/kexin type 9 (Pcsk9) gene expression. J Biol Chem 288(41):29252–29259
Friesen JA, Rodwell VW (2004) The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases. Genome Biol 5(11):248
Sanchez-Margalet V, Gonzalez-Yanes C (1998) Pancreastatin inhibits insulin action in rat adipocytes. Am J Physiol 275(6):E1055–E1060
Sanchez V, Calvo JR, Goberna R (1990) Glycogenolytic effect of pancreastatin in the rat. Biosci Rep 10(1):87–91
Mahata SK et al (1998) A novel, catecholamine release-inhibitory peptide from chromogranin A: autocrine control of nicotinic cholinergic-stimulated exocytosis. Adv Pharmacol 42:260–264
Angelone T et al (2015) The NO stimulator, catestatin, improves the frank-starling response in normotensive and hypertensive rat hearts. Nitric Oxide 50:10–19
Penna C et al (2010) Catestatin improves post-ischemic left ventricular function and decreases ischemia/reperfusion injury in heart. Cell Mol Neurobiol 30(8):1171–1179
Fung MM et al (2010) Direct vasoactive effects of the chromogranin A (CHGA) peptide catestatin in humans in vivo. Clin Exp Hypertens 32(5):278–287
Radek KA et al (2008) The neuroendocrine peptide catestatin is a cutaneous antimicrobial and induced in the skin after injury. J Invest Dermatol 128(6):1525–1534
Akaddar A et al (2010) Catestatin, an endogenous chromogranin A-derived peptide, inhibits in vitro growth of Plasmodium falciparum. Cell Mol Life Sci 67(6):1005–1015
Briolat J et al (2005) New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A. Cell Mol Life Sci 62(3):377–385
Cappello S et al (2007) Human recombinant chromogranin A-derived vasostatin-1 mimics preconditioning via an adenosine/nitric oxide signaling mechanism. Am J Physiol Heart Circ Physiol 293(1):H719–H727
Lugardon K et al (2000) Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. J Biol Chem 275(15):10745–10753
Gasparri A et al (1997) Chromogranin A fragments modulate cell adhesion. Identification and characterization of a pro-adhesive domain. J Biol Chem 272(33):20835–20843
Fasciotto BH et al (1993) Parastatin (porcine chromogranin A347–419), a novel chromogranin A-derived peptide, inhibits parathyroid cell secretion. Endocrinology 133(2):461–466
Pasqua T et al (2015) pGlu-serpinin protects the normotensive and hypertensive heart from ischemic injury. J Endocrinol 227(3):167–178
Lugardon K et al (2001) Structural and biological characterization of chromofungin, the antifungal chromogranin A-(47–66)-derived peptide. J Biol Chem 276(38):35875–35882
Filice E et al (2015) Chromofungin, CgA47-66-derived peptide, produces basal cardiac effects and postconditioning cardioprotective action during ischemia/reperfusion injury. Peptides 71:40–48
Strub JM et al (1996) Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173–194 from bovine adrenal medullary chromaffin granules. J Biol Chem 271(45):28533–28540
Curry WJ et al (2002) WE-14, a chromogranin a-derived neuropeptide. Ann N Y Acad Sci 971:311–316
Stadinski BD et al (2010) Chromogranin A is an autoantigen in type 1 diabetes. Nat Immunol 11(3):225–231
Dooley KA, Bennett MK, Osborne TF (1999) A critical role for cAMP response element-binding protein (CREB) as a Co-activator in sterol-regulated transcription of 3-hydroxy-3-methylglutaryl coenzyme A synthase promoter. J Biol Chem 274(9):5285–5291
Lemberger T et al (2008) CREB has a context-dependent role in activity-regulated transcription and maintains neuronal cholesterol homeostasis. FASEB J 22(8):2872–2879
Liu J et al (2000) Identification of a novel sterol-independent regulatory element in the human low density lipoprotein receptor promoter. J Biol Chem 275(7):5214–5221
Yieh L, Sanchez HB, Osborne TF (1995) Domains of transcription factor Sp1 required for synergistic activation with sterol regulatory element binding protein 1 of low density lipoprotein receptor promoter. Proc Natl Acad Sci U S A 92(13):6102–6106
Sanchez HB, Yieh L, Osborne TF (1995) Cooperation by sterol regulatory element-binding protein and Sp1 in sterol regulation of low density lipoprotein receptor gene. J Biol Chem 270(3):1161–1169
Herzig S et al (2003) CREB controls hepatic lipid metabolism through nuclear hormone receptor PPAR-gamma. Nature 426(6963):190–193
Zhang F et al (2003) Specific interaction of Egr1 and c/EBPbeta leads to the transcriptional activation of the human low density lipoprotein receptor gene. J Biol Chem 278(45):44246–44254
Gokey NG et al (2011) Early growth response 1 (Egr1) regulates cholesterol biosynthetic gene expression. J Biol Chem 286(34):29501–29510
Alvarez V et al (2008) The Sp1/Egr1-tandem repeat polymorphism in the 5-lipoxygenase gene promoter is not associated with late onset Alzheimer disease. Alzheimer Dis Assoc Disord 22(2):177–180
Hoppe KL, Francone OL (1998) Binding and functional effects of transcription factors Sp1 and Sp3 on the proximal human lecithin:cholesterol acyltransferase promoter. J Lipid Res 39(5):969–977
Wu N et al (2013) Activation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase during high fat diet feeding. Biochim Biophys Acta 1832(10):1560–1568
Zhang C et al (2019) OSBPL2 deficiency upregulate SQLE expression increasing intracellular cholesterol and cholesteryl ester by AMPK/SP1 and SREBF2 signalling pathway. Exp Cell Res 383(2):111512
Kim JH, Lee JN, Paik YK (2001) Cholesterol biosynthesis from lanosterol A concerted role for Sp1 and NF-Y-binding sites for sterol-mediated regulation of rat 7-dehydrocholesterol reductase gene expression. J Biol Chem 276(21):18153–18160
Cagen LM et al (2005) Insulin activates the rat sterol-regulatory-element-binding protein 1c (SREBP-1c) promoter through the combinatorial actions of SREBP, LXR, Sp-1 and NF-Y cis-acting elements. Biochem J 385(Pt 1):207–216
Stroup D, Chiang JY (2000) HNF4 and COUP-TFII interact to modulate transcription of the cholesterol 7alpha-hydroxylase gene (CYP7A1). J Lipid Res 41(1):1–11
Yamazaki T et al (2013) The COUP-TFII variant lacking a DNA-binding domain inhibits the activation of the Cyp7a1 promoter through physical interaction with COUP-TFII. Biochem J 452(2):345–357
Myers SA, Wang SC, Muscat GE (2006) The chicken ovalbumin upstream promoter-transcription factors modulate genes and pathways involved in skeletal muscle cell metabolism. J Biol Chem 281(34):24149–24160
Robinson CE et al (1999) A corepressor and chicken ovalbumin upstream promoter transcriptional factor proteins modulate peroxisome proliferator-activated receptor-gamma2/retinoid X receptor alpha-activated transcription from the murine lipoprotein lipase promoter. Endocrinology 140(4):1586–1593
Buniello A et al (2019) The NHGRI-EBI GWAS Catalog of published genome-wide association studies, targeted arrays and summary statistics 2019. Nucleic Acids Res 47(D1):D1005–D1012
Beck T, Shorter T, Brookes AJ (2020) GWAS Central: a comprehensive resource for the discovery and comparison of genotype and phenotype data from genome-wide association studies. Nucleic Acids Res 48(D1):D933–D940
Wolfe D et al (2013) Visualizing genomic information across chromosomes with PhenoGram. BioData Min 6(1):18
Lu X et al (2017) Exome chip meta-analysis identifies novel loci and East Asian-specific coding variants that contribute to lipid levels and coronary artery disease. Nat Genet 49(12):1722–1730
Willer CJ et al (2013) Discovery and refinement of loci associated with lipid levels. Nat Genet 45(11):1274–1283
Kanai M et al (2018) Genetic analysis of quantitative traits in the Japanese population links cell types to complex human diseases. Nat Genet 50(3):390–400
Acknowledgements
We acknowledge all the researchers who contributed to the areas of Chromogranin A and cholesterol research. All studies could not be cited due to space constraints. DRI and JV would like to thank Dr. Abrar Ali Khan (IIT Madras) for his valuable inputs.
Funding
NRM received research grants from the Department of Biotechnology (BT/PR25796/GET/119/98/2017; BT/PR23017/MED/30/1838/2017), Department of Science and Technology (SR/SO/HS-084/2013A) and Council of Scientific and Industrial Research (37/1564/12-EMR-II), Government of India. DRI and JV are thankful to Ministry of Human Resource Development (MHRD), Government of India for research fellowships. NV acknowledges support from the Agence Nationale pour la Recherche (ANR-19-CE44-0019 and ANR-22-CE44-0029).
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DRI and JV performed literature search, data analysis and drafted the manuscript. ET and NV provided critical inputs and edited the manuscript. NRM conceptualized and edited the manuscript. All authors approved the final version of the manuscript.
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The original online version of this article was revised: to update the entries in Table 1, 5th column heading is incorrect as “lipoproteins” and should have been reads as “apolipoproteins”. In entry Chylomicrons under the Pathophysiological implications column the term dietarytriglycerides should read as “dietary triglycerides”. In last entry LPA the value for size was incorrect as 30 and should have been reads as ~30.
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Iyer, D.R., Venkatraman, J., Tanguy, E. et al. Chromogranin A and its derived peptides: potential regulators of cholesterol homeostasis. Cell. Mol. Life Sci. 80, 271 (2023). https://doi.org/10.1007/s00018-023-04908-3
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DOI: https://doi.org/10.1007/s00018-023-04908-3