Activation of membrane-bound proteins and receptor systems: A link between tissue kallikrein and the KLK-related peptidases

Dong, Ying, Harrington, Brittney S., Adams, Mark N., Wortmann, Andreas, Stephenson, Sally-Anne, Lisle, Jessica E., Herington, Adrian, Hooper, John D., & Clements, Judith A. (2014) Activation of membrane-bound proteins and receptor systems: A link between tissue kallikrein and the KLK-related peptidases. Biological Chemistry, 395(9), pp. 977-990.

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The 15 members of the kallikrein-related serine peptidase (KLK) family have diverse tissue-specific expression profiles and roles in a range of cellular processes, including proliferation, migration, invasion, differentiation, inflammation and angiogenesis that are required in both normal physiology as well as pathological conditions. These roles require cleavage of a range of substrates, including extracellular matrix proteins, growth factors, cytokines as well as other proteinases. In addition, it has been clear since the earliest days of KLK research that cleavage of cell surface substrates is also essential in a range of KLK-mediated cellular processes where these peptidases are essentially acting as agonists and antagonists. In this review we focus on these KLK-regulated cell surface receptor systems including bradykinin receptors, proteinase-activated receptors, as well as the plasminogen activator, ephrins and their receptors, and hepatocyte growth factor/Met receptor systems and other plasma membrane proteins. From this analysis it is clear that in many physiological and pathological settings KLKs have the potential to regulate multiple receptor systems simultaneously; an important issue when these peptidases and substrates are targeted in disease.

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ID Code: 80213
Item Type: Journal Article
Refereed: Yes
Keywords: cell membrane-bound protein, kallikrein-related peptidase, receptor, signalling pathways, tissue kallikrein
DOI: 10.1515/hsz-2014-0147
ISSN: 1437-4315
Divisions: Current > Institutes > Institute of Health and Biomedical Innovation
Copyright Owner: Copyright 2014 De Gruyter
Deposited On: 20 May 2015 23:13
Last Modified: 01 Oct 2015 14:02

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