Abstract
Proteases catalyze the breakdown of proteins by hydrolysis of peptide bonds. These enzymes are involved in a number of pathophysiological processes ranging from the cellular to organism level. These processes include cell growth, homeostasis, remodeling, renewal, division, metabolic pathways, tumor growth, metastasis, etc. A number of proteases are found to be involved in mediating the biochemical pathogenesis of metabolic syndrome such as diabetes and cardiovascular diseases. This chapter summarizes types of proteases, classification, and their proteolytic function in diabetes-associated complications in the kidney, eye, liver, heart, and lung. Understanding the role of proteases will provide insights into the development of preventive and therapeutic modalities for diabetes and diabetic complications.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Dunn BM (2010) Introduction to the aspartic proteinase family. Aspartic Acid Proteases as Therapeutic Targets:1–21
Rao MB, Tanksale AM, Ghatge MS et al (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Biol Rev 62:597–635
Tyndall JD, Nall T, Fairlie DP (2005) Proteases universally recognize beta strands in their active sites. Chem Rev 105:973–1000
Govind NS, Mehta B, Sharma M et al (1981) Protease and carotenogenesis in Blakeslea trispora. Phytochemistry 20:2483–2485
Erez E, Fass D, Bibi E (2009) How intramembrane proteases bury hydrolytic reactions in the membrane. Nature 459:371–378
Polgár L (1987) The mechanism of action of aspartic proteases involves ‘push-pull’catalysis. FEBS Lett 219:1–4
Barrett AJ (1994) Proteolytic enzymes: serine and cysteine peptidases. Academic Press 244:1–765
Kotler MOSHE, Katz RA, Skalka AM (1988) Activity of avian retroviral protease expressed in Escherichia coli. J Virol 62:2696–2700
Kubo M, Imanaka T (1988) Cloning and nucleotide sequence of the highly thermostable neutral protease gene from Bacillus Stearothermophilus. Microbiology 134:1883–1892
Koszelak S, Ng JD, Day J et al (1997) The crystallographic structure of the subtilisin protease from Penicillium cyclopium. Biochemistry 36:6597–6604
Musante L, Tataruch D, Gu D et al (2015) Proteases and protease inhibitors of urinary extracellular vesicles in diabetic nephropathy. Journal of diabetes research 2015:1–15
Olbricht CJ, Geissinger B, Gutjahr E (1992) Renal hypertrophy in streptozotocin diabetic rats: role of proteolytic lysosomal enzymes. Kidney Int 41:966–972
Raju M, Santhoshkumar P, Sharma KK (2016) Alpha-crystallin-derived peptides as therapeutic chaperones. Biochimica et Biophysica Acta (BBA)-General Subjects 1860:246–251
Santhoshkumar P, Kannan R, Sharma KK (2015) Proteases in lens and cataract. In: Babizhayev MA, Li DW-C, Jacobi AK et al (eds) Studies on the cornea and lens. Springer, New York, pp 221–238
Hariharapura R, Santhoshkumar P, Sharma KK (2013) Profiling of lens protease involved in generation of αA-66-80 crystallin peptide using an internally quenched protease substrate. Exp Eye Res 109:51–59
Singh R, Kaushik S, Wang Y et al (2009) Autophagy regulates lipid metabolism. Nature 458:1131–1135
Papackova Z, Palenickova E, Dankova H et al (2012) Kupffer cells ameliorate hepatic insulin resistance induced by high-fat diet rich in monounsaturated fatty acids: the evidence for the involvement of alternatively activated macrophages. Nutrition & metabolism 9:1–15
Kalamidas SA, Kondomerkos DJ (2010) Autophagosomal glycogen-degrading activity and its relationship to the general autophagic activity in newborn rat hepatocytes: the effects of parenteral glucose administration. Microsc Res Tech 73:495–502
Peres GB, Juliano MA, Aguiar JAK et al (2014) Streptozotocin-induced diabetes mellitus affects lysosomal enzymes in rat liver. Braz J Med Biol Res 47:452–460
Uchimura K, Hayata M, Mizumoto T et al (2014) The serine protease prostasin regulates hepatic insulin sensitivity by modulating TLR4 signalling. Nat Commun 5:1–13
Hua Y, Nair S (2015) Proteases in cardiometabolic diseases: pathophysiology, molecular mechanisms and clinical applications. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease 1852:195–208
Lungarella G, Cavarra E, Lucattelli M et al (2008) The dual role of neutrophil elastase in lung destruction and repair. Int J Biochem Cell Biol 40:1287–1296
Pitocco D, Fuso L, Conte EG et al (2012) The diabetic lung-a new target organ? The review of diabetic studies: Rev Diabet Stud 9:23–35
van den Borst B, Gosker HR, Zeegers MP et al (2010) Pulmonary function in diabetes: a metaanalysis. Chest J 138:393–406
Irfan M, Jabbar A, Haque AS et al (2011) Pulmonary functions in patients with diabetes mellitus. Lung India 28:89–92
Kuziemski K, Specjalski K, Jassem E (2011) Diabetic pulmonary microangiopathy—fact or fiction? Endokrynol Pol 62:171–176
Weynand B, Jonckheere A, Frans A et al (1999) Diabetes mellitus induces a thickening of the pulmonary basal lamina. Respiration 66:14–19
Ljubic S, Metelko Z, Car N et al (1998) Reduction of diffusion capacity for carbon monoxide in diabetic patients. Chest J 114:1033–1035
Tetley TD (1993) New perspectives on basic mechanisms in lung disease. 6. Proteinase imbalance: its role in lung disease. Thorax 48:560–565
Boxer LA, Smolen JE (1988) Neutrophil granule constituents and their release in health and disease. Hematol Oncol Clin North Am 2:101–134
Acknowledgement
Authors are thankful to Prof. Ram Rajasekharan, Director, CSIR-CFTRI, for his interest and valuable suggestions. Dr. Ravindra P. V. thanks the Department of Biotechnology, New Delhi, for funding in the form of Ramalingaswami fellowship.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2017 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Ravindra, P.V., Girish, T.K. (2017). Role of Proteases in Diabetes and Diabetic Complications. In: Chakraborti, S., Dhalla, N. (eds) Proteases in Physiology and Pathology. Springer, Singapore. https://doi.org/10.1007/978-981-10-2513-6_13
Download citation
DOI: https://doi.org/10.1007/978-981-10-2513-6_13
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-10-2512-9
Online ISBN: 978-981-10-2513-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)