Tissue kallikrein is a serine protease thought to be involved in the generation of bioactive peptide kinins from kininogen in many organs such as
the kidneys, colon, salivary glands, pancreas, and blood vessels. Unlike pepsin, members of the glandular kallikrein subfamily of
serine proteases demonstrate a high degree of substrate specificity. The true physiologic role of specific kallikreins is often unrelated to the kininogenase activity.
Expression profiling of purified mouse gonadal somatic cells during the critical time window of sex determination reveals novel candidate genes for human sexual dysgenesis syndromes Beverdam A, et al.
NCBI Summary:
Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. This protein is functionally conserved in its capacity to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.
General function
Enzyme, Hydrolase, Peptidase/Protease
Comment
Cellular localization
Secreted
Comment
Ovarian function
Ovulation
Comment
Holland AM, et al reported kallikrein gene expression in the gonadotrophin-stimulated
rat ovary.
.
The kallikreins (KLKs) are a highly conserved multi-gene family of serine
proteases that are expressed in a wide variety of tissues and act on a diverse
range of substrates. KLK-like enzyme activity has variously been reported to
increase or decrease during the period leading up to ovulation in the equine
chorionic gonadotrophin (eCG)primed, human chorionic gonadotrophin
(hCG)-stimulated immature rat ovary. They used a gene-specific
RT-PCR/Southern hybridisation strategy to delineate the expression patterns
of six of the individual KLK genes expressed in the rat ovary (rKLK1-3 and
rKLK7-9) and have identified three broad patterns of expression in the
eCG/hCG-stimulated ovary in which there is either a post-eCG
increase/pre-ovulatory decrease in rKLK expression (rKLK1, rKLK3), a
peri-ovulatory decrease in expression (rKLK2, rKLK8) or a relatively
unchanged pattern of expression (rKLK7, rKLK9). In addition to clarifying
the earlier biochemical studies, these findings support a differential role for the
individual KLKs in the ovulatory process.