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Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by KLKB1 gene) has no known paralogue, while tissue kallikrein-related peptidases (KLKs) encode a family of fifteen closely related serine proteases.
Kallikreins are a family of proteases consisting of 15 closely related, secreted serine proteases with either trypsin-like or chymotrypsin-like specificity.
- Magdalena Kalinska, Ulf Meyer-Hoffert, Tomasz Kantyka, Jan Potempa, Jan Potempa
- 10.1016/j.biochi.2015.09.023
- 2016
- 2016/03
Nov 21, 2019 · Among the proteins essential for upholding the epidermal microenvironment are the members of the kallikrein (KLK) family composed of 15 secreted serine proteases. Most of the members of these epithelial-specific proteins are present in skin and regulate skin desquamation and inflammation.
- Pauline Nauroy, Alexander Nyström
- 10.1016/j.mbplus.2019.100019
- 2020
- Matrix Biol Plus. 2020 May; 6-7: 100019.
Kallikrein is a compound of high molecular weight which lowers blood pressure and stimulates the movement of the uterus and the intestine. It occurs in the pancreas, the submaxillary glands, and the urine of all mammals including man. It also occurs as the inactive precursor, kallikreinogen, in serum and pancreas.
Feb 14, 2019 · Overview about the multiple roles of kallikrein in L. obliqua–induced renal and vascular disturbances. L. obliqua venom is able to directly activate kallikrein in plasma. Consequently, prekallirein levels decrease, while increase plasma and tissue levels of active kallikrein.
- Markus Berger, João Alfredo de Moraes, João Alfredo de Moraes, Walter Orlando Beys-da-Silva, Lucélia...
- 10.1371/journal.pntd.0007197
- 2019
- 2019/02
Dec 23, 2021 · A new study has found that venoms found in snakes and mammals share a common origin. Researchers traced the origin of a class of toxins, called kallikrein serine proteases, to a salivary protein found in a common ancestor.
Mar 1, 2016 · Kallikreins are a family of proteases consisting of 15 closely related, secreted serine proteases with either trypsin-like or chymotrypsin-like specificity.
