Kallikrein-related peptidases.
(2008) In Cellular and Molecular Life Sciences 65. p.2019-2038- Abstract
- Kallikrein 1 (KLK1), a key component of the kallikrein-kinin system, originates from a locus on the long arm of chromosome 19 that contains several related serine endopeptidases. The biological role of these kallikrein-related peptidases is not clear, but emerging evidence suggests that they might be important in several physiological systems, e.g., in male reproduction, skin homeostasis, tooth enamel formation and neural development and plasticity. The kallikrein locus has undergone some major evolutionary events. Most spectacular are relatively recent duplications of KLK1 that have created 13 and 9 functional genes that are unique to the mouse and the rat, respectively. Human paralogs are KLK2 and KLK3: the latter encoding the cancer... (More)
- Kallikrein 1 (KLK1), a key component of the kallikrein-kinin system, originates from a locus on the long arm of chromosome 19 that contains several related serine endopeptidases. The biological role of these kallikrein-related peptidases is not clear, but emerging evidence suggests that they might be important in several physiological systems, e.g., in male reproduction, skin homeostasis, tooth enamel formation and neural development and plasticity. The kallikrein locus has undergone some major evolutionary events. Most spectacular are relatively recent duplications of KLK1 that have created 13 and 9 functional genes that are unique to the mouse and the rat, respectively. Human paralogs are KLK2 and KLK3: the latter encoding the cancer biomarker prostate-specific antigen. In this review on kallikrein-related peptidases, the focus is on their evolution, their role in skin homeostasis and semen liquefaction, and their utility as cancer biomarkers. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1052443
- author
- Lundwall, Åke LU and Brattsand, M
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Cellular and Molecular Life Sciences
- volume
- 65
- pages
- 2019 - 2038
- publisher
- Birkhäuser Verlag
- external identifiers
-
- pmid:18344018
- wos:000257368600004
- scopus:46449093665
- ISSN
- 1420-9071
- DOI
- 10.1007/s00018-008-8024-3
- language
- English
- LU publication?
- yes
- id
- fbba6ddd-8130-40c0-885e-791f634c439a (old id 1052443)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/18344018?dopt=Abstract
- date added to LUP
- 2016-04-04 09:18:44
- date last changed
- 2022-02-28 07:20:32
@article{fbba6ddd-8130-40c0-885e-791f634c439a,
abstract = {{Kallikrein 1 (KLK1), a key component of the kallikrein-kinin system, originates from a locus on the long arm of chromosome 19 that contains several related serine endopeptidases. The biological role of these kallikrein-related peptidases is not clear, but emerging evidence suggests that they might be important in several physiological systems, e.g., in male reproduction, skin homeostasis, tooth enamel formation and neural development and plasticity. The kallikrein locus has undergone some major evolutionary events. Most spectacular are relatively recent duplications of KLK1 that have created 13 and 9 functional genes that are unique to the mouse and the rat, respectively. Human paralogs are KLK2 and KLK3: the latter encoding the cancer biomarker prostate-specific antigen. In this review on kallikrein-related peptidases, the focus is on their evolution, their role in skin homeostasis and semen liquefaction, and their utility as cancer biomarkers.}},
author = {{Lundwall, Åke and Brattsand, M}},
issn = {{1420-9071}},
language = {{eng}},
pages = {{2019--2038}},
publisher = {{Birkhäuser Verlag}},
series = {{Cellular and Molecular Life Sciences}},
title = {{Kallikrein-related peptidases.}},
url = {{http://dx.doi.org/10.1007/s00018-008-8024-3}},
doi = {{10.1007/s00018-008-8024-3}},
volume = {{65}},
year = {{2008}},
}