Abstract
CaV1.2 calcium channel is the primary conduit for Ca2+ influx into cardiac and smooth muscles that underscores its importance in the pathogenesis of hypertension, atherosclerosis, myocardial infarction, and heart failure. But, a few controversies still remain. Therefore, exploring new ways to modulate CaV1.2 channel activity will augment the arsenal of CaV1.2 channel-based therapeutics for treatment of cardiovascular diseases. Here, we will mainly introduce a couple of emerging CaV1.2 channel interacting proteins, such as Galectin-1 and Cereblon, and discuss their roles in hypertension and heart failure through fine-tuning CaV1.2 channel activity. Of current interest, we will also evaluate the implication of the role of CaV1.2 channel in SARS-CoV-2 infection and the potential treatments of COVID-19-related cardiovascular symptoms.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Akahani S, Nangia-Makker P, Inohara H, Kim HR, Raz A (1997) Galectin-3: a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family. Cancer Res 57:5272–5276
Al-Obaidi N et al (2019) Galectin-1 is a new fibrosis protein in type 1 and type 2 diabetes. FASEB J 33:373–387. https://doi.org/10.1096/fj.201800555RR
Al-Salam S, Hashmi S (2014) Galectin-1 in early acute myocardial infarction. PLoS One 9:e86994. https://doi.org/10.1371/journal.pone.0086994
Altier C et al (2011) The Cavbeta subunit prevents RFP2-mediated ubiquitination and proteasomal degradation of L-type channels. Nat Neurosci 14:173–180. https://doi.org/10.1038/nn.2712
Antzelevitch C et al (2007) Loss-of-function mutations in the cardiac calcium channel underlie a new clinical entity characterized by ST-segment elevation, short QT intervals, and sudden cardiac death. Circulation 115:442–449. https://doi.org/10.1161/CIRCULATIONAHA.106.668392
Bannister JP et al (2009) Smooth muscle cell alpha2delta-1 subunits are essential for vasoregulation by CaV1.2 channels. Circ Res 105:948–955. https://doi.org/10.1161/CIRCRESAHA.109.203620
Barnes EA, Chen CH, Sedan O, Cornfield DN (2017) Loss of smooth muscle cell hypoxia inducible factor-1alpha underlies increased vascular contractility in pulmonary hypertension. FASEB J 31:650–662. https://doi.org/10.1096/fj.201600557R
Besler C et al (2017) Plasma and cardiac Galectin-3 in patients with heart failure reflects both inflammation and fibrosis. Circ Heart Fail 10:e003804. https://doi.org/10.1161/CIRCHEARTFAILURE.116.003804
Calvier L et al (2016) Galectin-3 and aldosterone as potential tandem biomarkers in pulmonary arterial hypertension. Heart 102:390–396. https://doi.org/10.1136/heartjnl-2015-308365
Camby I et al (2001) Galectins are differentially expressed in supratentorial pilocytic astrocytomas, astrocytomas, anaplastic astrocytomas and glioblastomas, and significantly modulate tumor astrocyte migration. Brain Pathol 11:12–26
Camby I, Le Mercier M, Lefranc F, Kiss R (2006) Galectin-1: a small protein with major functions. Glycobiology 16:137R–157R., cwl025 [pii]. https://doi.org/10.1093/glycob/cwl025
Caniglia JL, Guda MR, Asuthkar S, Tsung AJ, Velpula KK (2020) A potential role for Galectin-3 inhibitors in the treatment of COVID-19. PeerJ 8:e9392. https://doi.org/10.7717/peerj.9392
Case D et al (2007) Mice deficient in galectin-1 exhibit attenuated physiological responses to chronic hypoxia-induced pulmonary hypertension. Am J Physiol Lung Cell Mol Physiol 292:L154–L164., 00192.2006 [pii]. https://doi.org/10.1152/ajplung.00192.2006
Cedeno-Laurent F, Dimitroff CJ (2012) Galectin-1 research in T cell immunity: past, present and future. Clin Immunol 142:107–116., S1521-6616(11)00280-4 [pii]. https://doi.org/10.1016/j.clim.2011.09.011
Cervantes-Alvarez E et al (2022) Galectin-3 as a potential prognostic biomarker of severe COVID-19 in SARS-CoV-2 infected patients. Sci Rep 12:1856. https://doi.org/10.1038/s41598-022-05968-4
Chamberlain PP et al (2019) Evolution of cereblon-mediated protein degradation as a therapeutic modality. ACS Med Chem Lett 10:1592–1602. https://doi.org/10.1021/acsmedchemlett.9b00425
Chen X et al (2011) Calcium influx through Cav1.2 is a proximal signal for pathological cardiomyocyte hypertrophy. J Mol Cell Cardiol 50:460–470. https://doi.org/10.1016/j.yjmcc.2010.11.012
Cheng YH et al (2022) Galectin-1 contributes to vascular remodeling and blood flow recovery after cerebral ischemia in mice. Transl Stroke Res 13:160–170. https://doi.org/10.1007/s12975-021-00913-5
Cho M, Cummings RD (1995a) Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. I. Physical and chemical characterization. J Biol Chem 270:5198–5206
Cho M, Cummings RD (1995b) Galectin-1, a beta-galactoside-binding lectin in Chinese hamster ovary cells. II. Localization and biosynthesis. J Biol Chem 270:5207–5212
Cooper DN, Barondes SH (1990) Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J Cell Biol 110:1681–1691
Cooper DN, Barondes SH (1999) God must love galectins; he made so many of them. Glycobiology 9:979–984., cwc107 [pii]
Crespi B, Alcock J (2020) Conflicts over calcium and the treatment of COVID-19. Evol Med Public Health 9:149–156. https://doi.org/10.1093/emph/eoaa046
de Boer RA et al (2012) A genome-wide association study of circulating Galectin-3. PLoS One 7:e47385. https://doi.org/10.1371/journal.pone.0047385
Derhaschnig U et al (2002) Increased levels of transforming growth factor-beta1 in essential hypertension. Am J Hypertens 15:207–211., S0895706101023275 [pii]
Dias-Baruffi M et al (2010) Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. Glycobiology 20:507–520., cwp203 [pii]. https://doi.org/10.1093/glycob/cwp203
Fan J et al (2019) Galectin-1 attenuates cardiomyocyte hypertrophy through splice-variant specific modulation of CaV1.2 calcium channel. Biochim Biophys Acta Mol Basis Dis 1865:218–229. https://doi.org/10.1016/j.bbadis.2018.08.016
Freitag N et al (2013) Interfering with Gal-1-mediated angiogenesis contributes to the pathogenesis of preeclampsia. Proc Natl Acad Sci U S A 110:11451–11456., 1303707110 [pii]. https://doi.org/10.1073/pnas.1303707110
Fujioka Y et al (2013) A Ca2+-dependent signalling circuit regulates influenza a virus internalization and infection. Nat Commun 4:2763. https://doi.org/10.1038/ncomms3763
Fujioka Y et al (2018) A sialylated voltage-dependent Ca(2+) channel binds hemagglutinin and mediates influenza a virus entry into mammalian cells. Cell Host Microbe 23:809-818 e805. https://doi.org/10.1016/j.chom.2018.04.015
Gong Y, Qin S, Dai L, Tian Z (2021) The glycosylation in SARS-CoV-2 and its receptor ACE2. Signal Transduct Target Ther 6:396. https://doi.org/10.1038/s41392-021-00809-8
Goonasekera SA et al (2012) Decreased cardiac L-type Ca(2)(+) channel activity induces hypertrophy and heart failure in mice. J Clin Invest 122:280–290. https://doi.org/10.1172/JCI58227
Hara A et al (2020) Galectin-3: a potential prognostic and diagnostic marker for heart disease and detection of early stage pathology. Biomol Ther 10:1277. https://doi.org/10.3390/biom10091277
Harazono Y et al (2014) Galectin-3 leads to attenuation of apoptosis through Bax heterodimerization in human thyroid carcinoma cells. Oncotarget 5:9992–10001. https://doi.org/10.18632/oncotarget.2486
Haudek KC et al (2010) Dynamics of galectin-3 in the nucleus and cytoplasm. Biochim Biophys Acta Gen Subj 1800:181–189. https://doi.org/10.1016/j.bbagen.2009.07.005
Henderson NC, Sethi T (2009) The regulation of inflammation by galectin-3. Immunol Rev 230:160–171. https://doi.org/10.1111/j.1600-065X.2009.00794.x
Ho JE et al (2012) Galectin-3, a marker of cardiac fibrosis, predicts incident heart failure in the community. J Am Coll Cardiol 60:1249–1256. https://doi.org/10.1016/j.jacc.2012.04.053
Hofmann F, Flockerzi V, Kahl S, Wegener JW (2014) L-type CaV1.2 calcium channels: from in vitro findings to in vivo function. Physiol Rev 94:303–326. https://doi.org/10.1152/physrev.00016.2013
Hu Z, Liang MC, Soong TW (2017) Alternative splicing of L-type CaV1.2 calcium channels: implications in cardiovascular diseases. Genes (Basel) 8. https://doi.org/10.3390/genes8120344
Hu Z et al (2018) Regulation of blood pressure by targeting CaV1.2-Galectin-1 protein interaction. Circulation 138:1431–1445. https://doi.org/10.1161/CIRCULATIONAHA.117.031231
Huang Y et al (2013) Hypoxia-inducible factor-1alpha in vascular smooth muscle regulates blood pressure homeostasis through a peroxisome proliferator-activated receptor-gamma-angiotensin II receptor type 1 axis. Hypertension 62:634–640. https://doi.org/10.1161/HYPERTENSIONAHA.111.00160
Hughes RC (1999) Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1473:172–185., S0304-4165(99)00177-4 [pii]
Ishibashi S et al (2007) Galectin-1 regulates neurogenesis in the subventricular zone and promotes functional recovery after stroke. Exp Neurol 207:302–313., S0014-4886(07)00260-9 [pii]. https://doi.org/10.1016/j.expneurol.2007.06.024
Jiang Y et al (2015) Increased SUMO-1 expression in response to hypoxia: interaction with HIF-1alpha in hypoxic pulmonary hypertension. Int J Mol Med 36:271–281. https://doi.org/10.3892/ijmm.2015.2209
Johannes L, Jacob R, Leffler H (2018) Galectins at a glance. J Cell Sci 131:jcs208884. https://doi.org/10.1242/jcs.208884
Johns RA et al (2016) Hypoxia-inducible factor 1alpha is a critical downstream mediator for hypoxia-induced mitogenic factor (FIZZ1/RELMalpha)-induced pulmonary hypertension. Arterioscler Thromb Vasc Biol 36:134–144., ATVBAHA.115.306710 [pii]. https://doi.org/10.1161/ATVBAHA.115.306710
Kharade SV et al (2013) The beta3 subunit contributes to vascular calcium channel upregulation and hypertension in angiotensin II-infused C57BL/6 mice. Hypertension 61:137–142. https://doi.org/10.1161/HYPERTENSIONAHA.112.197863
Kim YM et al (2013) Hypoxia-inducible factor-1alpha in pulmonary artery smooth muscle cells lowers vascular tone by decreasing myosin light chain phosphorylation. Circ Res 112:1230–1233. https://doi.org/10.1161/CIRCRESAHA.112.300646
Kim J, Lee KM, Park CS, Park WJ (2014) Ablation of cereblon attenuates myocardial ischemia-reperfusion injury. Biochem Biophys Res Commun 447:649–654. https://doi.org/10.1016/j.bbrc.2014.04.061
Kim HK et al (2016) Cereblon in health and disease. Pflugers Arch 468:1299–1309. https://doi.org/10.1007/s00424-016-1854-1
Lanteri M et al (2003) Altered T cell surface glycosylation in HIV-1 infection results in increased susceptibility to galectin-1-induced cell death. Glycobiology 13:909–918. https://doi.org/10.1093/glycob/cwg110. cwg110 [pii]
Li F (2016) Structure, function, and evolution of coronavirus spike proteins. Annu Rev Virol 3:237–261. https://doi.org/10.1146/annurev-virology-110615-042301
Li Y et al (2016) Suppression of the expression of hypoxia-inducible factor-1alpha by RNA interference alleviates hypoxia-induced pulmonary hypertension in adult rats. Int J Mol Med. https://doi.org/10.3892/ijmm.2016.2773
Liao P, Yong TF, Liang MC, Yue DT, Soong TW (2005) Splicing for alternative structures of Cav1.2 Ca2+ channels in cardiac and smooth muscles. Cardiovasc Res 68:197–203. https://doi.org/10.1016/j.cardiores.2005.06.024
Liao P et al (2007) A smooth muscle Cav1.2 calcium channel splice variant underlies hyperpolarized window current and enhanced state-dependent inhibition by nifedipine. J Biol Chem 282:35133–35142. https://doi.org/10.1074/jbc.M705478200
Lim MJ et al (2014) Induction of galectin-1 by TGF-beta1 accelerates fibrosis through enhancing nuclear retention of Smad2. Exp Cell Res 326:125–135., S0014-4827(14)00234-1 [pii]. https://doi.org/10.1016/j.yexcr.2014.06.001
Liu FT, Rabinovich GA (2005) Galectins as modulators of tumour progression. Nat Rev Cancer 5:29–41., nrc1527 [pii]. https://doi.org/10.1038/nrc1527
Loh KWZ, Liang MC, Soong TW, Hu Z (2020) Regulation of cardiovascular calcium channel activity by post-translational modifications or interacting proteins. Pflugers Arch 472:653–667. https://doi.org/10.1007/s00424-020-02398-x
MacKinnon AC et al (2008) Regulation of alternative macrophage activation by Galectin-3. J Immunol 180:2650. https://doi.org/10.4049/jimmunol.180.4.2650
McLeod K, Walker JT, Hamilton DW (2018) Galectin-3 regulation of wound healing and fibrotic processes: insights for chronic skin wound therapeutics. J Cell Commun Signal 12:281–287. https://doi.org/10.1007/s12079-018-0453-7
Moiseeva EP, Javed Q, Spring EL, de Bono DP (2000) Galectin 1 is involved in vascular smooth muscle cell proliferation. Cardiovasc Res 45:493–502., S0008-6363(99)00276-X [pii]
Moosmang S et al (2003) Dominant role of smooth muscle L-type calcium channel Cav1.2 for blood pressure regulation. EMBO J 22:6027–6034. https://doi.org/10.1093/emboj/cdg583
Nickel W (2005) Unconventional secretory routes: direct protein export across the plasma membrane of mammalian cells. Traffic 6:607–614., TRA302 [pii]. https://doi.org/10.1111/j.1600-0854.2005.00302.x
Nio-Kobayashi J (2016) Tissue- and cell-specific localization of galectins, beta-galactose-binding animal lectins, and their potential functions in health and disease. Anat Sci Int. https://doi.org/10.1007/s12565-016-0366-6. 10.1007/s12565-016-0366-6 [pii]
Nugent KM, Shanley JD (1984) Verapamil inhibits influenza a virus replication. Arch Virol 81:163–170. https://doi.org/10.1007/BF01309305
Ochieng J, Furtak V, Lukyanov P (2002) Extracellular functions of galectin-3. Glycoconj J 19:527–535. https://doi.org/10.1023/B:GLYC.0000014082.99675.2f
Ohkuchi AHC, Nagayama S, Suzaki H, Takahashi K, Matsubara S, Suzuki M (2014) In: XIXth world congress for the study of hypertension in pregnancy 284-POS (New Orleans, Louisiana, USA)
Ou D et al (2022) Galectin-1 alleviates myocardial ischemia-reperfusion injury by reducing the inflammation and apoptosis of cardiomyocytes. Exp Ther Med 23:143. https://doi.org/10.3892/etm.2021.11066
Ouellet M et al (2005) Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells. J Immunol 174:4120–4126., 174/7/4120 [pii]
Park JW, Voss PG, Grabski S, Wang JL, Patterson RJ (2001) Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein. Nucleic Acids Res 29:3595–3602. https://doi.org/10.1093/nar/29.17.3595
Park N et al (2022) Cereblon contributes to cardiac dysfunction by degrading Cav1.2alpha. Eur Heart J 43:1973–1989. https://doi.org/10.1093/eurheartj/ehac072
Petrović T, Lauc G, Trbojević-Akmačić I (2021) The importance of glycosylation in COVID-19 infection. Adv Exp Med Biol 1325:239–264. https://doi.org/10.1007/978-3-030-70115-4_12
Pullamsetti SS, Mamazhakypov A, Weissmann N, Seeger W, Savai R (2020) Hypoxia-inducible factor signaling in pulmonary hypertension. J Clin Invest 130:5638–5651. https://doi.org/10.1172/JCI137558
Quinta HR, Pasquini JM, Rabinovich GA, Pasquini LA (2014) Glycan-dependent binding of galectin-1 to neuropilin-1 promotes axonal regeneration after spinal cord injury. Cell Death Differ 21:941–955., cdd201414 [pii]. https://doi.org/10.1038/cdd.2014.14
Rabinovich GA, Toscano MA (2009) Turning ‘sweet’ on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat Rev Immunol 9:338–352., nri2536 [pii]. https://doi.org/10.1038/nri2536
Ramírez Hernández E et al (2021) The role of the SARS-CoV-2 S-protein glycosylation in the interaction of SARS-CoV-2/ACE2 and immunological responses. Viral Immunol 34:165–173. https://doi.org/10.1089/vim.2020.0174
Rapoport EM, Kurmyshkina OV, Bovin NV (2008) Mammalian galectins: structure, carbohydrate specificity, and functions. Biochemistry (Mosc) 73:393–405. https://doi.org/10.1134/S0006297908040032
Rini JM, Lobsanov YD (1999) New animal lectin structures. Curr Opin Struct Biol 9:578–584. https://doi.org/10.1016/S0959-440X(99)00008-1
Roldan-Montero R et al (2022) Galectin-1 prevents pathological vascular remodeling in atherosclerosis and abdominal aortic aneurysm. Sci Adv 8., eabm7322. https://doi.org/10.1126/sciadv.abm7322
Sato T, Ito T, Handa H (2021) Cereblon-based small-molecule compounds to control neural stem cell proliferation in regenerative medicine. Front Cell Dev Biol 9:629326. https://doi.org/10.3389/fcell.2021.629326
Savalli N et al (2016) The alpha2delta-1 subunit remodels CaV1.2 voltage sensors and allows Ca2+ influx at physiological membrane potentials. J Gen Physiol 148:147–159. https://doi.org/10.1085/jgp.201611586
Seropian IM et al (2013) Galectin-1 controls cardiac inflammation and ventricular remodeling during acute myocardial infarction. Am J Pathol 182:29–40. https://doi.org/10.1016/j.ajpath.2012.09.022
Seropian IM et al (2018) Galectin-1 as an emerging mediator of cardiovascular inflammation: mechanisms and therapeutic opportunities. Mediators Inflamm 2018:8696543. https://doi.org/10.1155/2018/8696543
Sharma UC et al (2004) Galectin-3 marks activated macrophages in failure-prone hypertrophied hearts and contributes to cardiac dysfunction. Circulation 110:3121–3128. https://doi.org/10.1161/01.Cir.0000147181.65298.4d
Song LS et al (2002) Ca(2+) signaling in cardiac myocytes overexpressing the alpha(1) subunit of L-type Ca(2+) channel. Circ Res 90:174–181. https://doi.org/10.1161/hh0202.103230
Splawski I et al (2004) Ca(V)1.2 calcium channel dysfunction causes a multisystem disorder including arrhythmia and autism. Cell 119:19–31. https://doi.org/10.1016/j.cell.2004.09.011
Splawski I et al (2005) Severe arrhythmia disorder caused by cardiac L-type calcium channel mutations. Proc Natl Acad Sci U S A 102:8089–8096.; discussion 8086–8088. https://doi.org/10.1073/pnas.0502506102
Starossom SC et al (2012) Galectin-1 deactivates classically activated microglia and protects from inflammation-induced neurodegeneration. Immunity 37:249–263., S1074-7613(12)00323-8 [pii]. https://doi.org/10.1016/j.immuni.2012.05.023
Straus MR et al (2021) Inhibitors of L-type calcium channels show therapeutic potential for treating SARS-CoV-2 infections by preventing virus entry and spread. ACS Infect Dis 7:2807–2815. https://doi.org/10.1021/acsinfecdis.1c00023
Suthahar N et al (2018) Galectin-3 activation and inhibition in heart failure and cardiovascular disease: an update. Theranostics 8:593–609. https://doi.org/10.7150/thno.22196
Suthanthiran M et al (2000) Transforming growth factor-beta 1 hyperexpression in African-American hypertensives: a novel mediator of hypertension and/or target organ damage. Proc Natl Acad Sci U S A 97:3479–3484. https://doi.org/10.1073/pnas.050420897. 050420897 [pii]
Takenaka Y et al (2004) Nuclear export of phosphorylated Galectin-3 regulates its antiapoptotic activity in response to chemotherapeutic drugs. Mol Cell Biol 24:4395–4406. https://doi.org/10.1128/MCB.24.10.4395-4406.2004
Thakurta A et al (2014) Absence of mutations in cereblon (CRBN) and DNA damage-binding protein 1 (DDB1) genes and significance for IMiD therapy. Leukemia 28:1129–1131. https://doi.org/10.1038/leu.2013.315
Wang J et al (2011) Splice variant specific modulation of CaV1.2 calcium channel by galectin-1 regulates arterial constriction. Circ Res 109:1250–1258., CIRCRESAHA.111.248849 [pii]. https://doi.org/10.1161/CIRCRESAHA.111.248849
Wang X et al (2022) Diltiazem inhibits SARS-CoV-2 cell attachment and internalization and decreases the viral infection in mouse lung. PLoS Pathog 18:e1010343. https://doi.org/10.1371/journal.ppat.1010343
Watanabe Y, Allen Joel D, Wrapp D, McLellan Jason S, Crispin M (2020) Site-specific glycan analysis of the SARS-CoV-2 spike. Science 369:330–333. https://doi.org/10.1126/science.abb9983
Weissgerber P et al (2006) Reduced cardiac L-type Ca2+ current in Ca(V)beta2−/− embryos impairs cardiac development and contraction with secondary defects in vascular maturation. Circ Res 99:749–757. https://doi.org/10.1161/01.RES.0000243978.15182.c1
Yang RY, Hsu DK, Liu FT (1996) Expression of galectin-3 modulates T-cell growth and apoptosis. Proc Natl Acad Sci U S A 93:6737–6742. https://doi.org/10.1073/pnas.93.13.6737
Zakrzewicz A et al (2007) The transforming growth factor-beta/Smad2,3 signalling axis is impaired in experimental pulmonary hypertension. Eur Respir J 29:1094–1104., 09031936.00138206 [pii]. https://doi.org/10.1183/09031936.00138206
Zhang Y et al (2018) Influence of LGALS3 gene polymorphisms on susceptibility and prognosis of dilated cardiomyopathy in a northern Han Chinese population. Gene 642:293–298. https://doi.org/10.1016/j.gene.2017.11.026
Zhao XY et al (2010) Hypoxia inducible factor-1 mediates expression of galectin-1: the potential role in migration/invasion of colorectal cancer cells. Carcinogenesis 31:1367–1375., bgq116 [pii]. https://doi.org/10.1093/carcin/bgq116
Zhao XY, Zhao KW, Jiang Y, Zhao M, Chen GQ (2011) Synergistic induction of galectin-1 by CCAAT/enhancer binding protein alpha and hypoxia-inducible factor 1alpha and its role in differentiation of acute myeloid leukemic cells. J Biol Chem 286:36808–36819., M111.247262 [pii]. https://doi.org/10.1074/jbc.M111.247262
Acknowledgements
This work was supported by Academic Research Fund Tier 2 Grant (T2EP30221-0042 to T.W.S.) from the Singapore Ministry of Education and Open Fund-Individual Research Grant (OF-IRG) (MOH-000650 to T.W.S.) from the National Medical Research Council of Singapore.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2023 The Author(s), under exclusive license to Springer Nature Switzerland AG
About this chapter
Cite this chapter
Loh, K.W.Z., Hu, Z., Soong, T.W. (2023). Modulation of CaV1.2 Channel Function by Interacting Proteins and Post-Translational Modifications: Implications in Cardiovascular Diseases and COVID-19. In: Striessnig, J. (eds) Voltage-gated Ca2+ Channels: Pharmacology, Modulation and their Role in Human Disease. Handbook of Experimental Pharmacology, vol 279. Springer, Cham. https://doi.org/10.1007/164_2023_636
Download citation
DOI: https://doi.org/10.1007/164_2023_636
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-031-38436-3
Online ISBN: 978-3-031-38437-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)