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Kallikrein-related peptidase 12

KLK12, kallikrein 12, kallikrein-related peptidase 12, KLK-L5
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. Alternate splicing of this gene results in three transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Kallikrein, KLK6, KLK13, KLK5, hK11
Papers on KLK12
Transcriptome changes upon in vitro challenge with Mycobacterium bovis in monocyte-derived macrophages from bovine tuberculosis-infected and healthy cows.
Zhou et al., Beijing, China. In Vet Immunol Immunopathol, Mar 2015
For macrophages, kallikrein-related peptidase 12 (KLK12) and protease, serine, 2 (trypsin 2) (PRSS2), as well as a secreted protein, acidic, cysteine-rich (osteonectin) (SPARC)-centered matricellular gene network, were differentially expressed in infected animals.
Characterization of Spink6 in mouse skin: the conserved inhibitor of kallikrein-related peptidases is reduced by barrier injury.
Meyer-Hoffert et al., Kiel, Germany. In J Invest Dermatol, 2014
Recombinant Spink6 efficiently inhibited mouse Klk5 and human KLK2, KLK4, KLK5, KLK6, KLK7, KLK12, KLK13, and KLK14, whereas human KLK1 and KLK8 were not inhibited.
Angiogenesis stimulated by human kallikrein-related peptidase 12 acting via a platelet-derived growth factor B-dependent paracrine pathway.
Heuzé-Vourc'h et al., Tours, France. In Faseb J, 2014
KLK12, a kallikrein peptidase, is thought to take part in the control of angiogenesis.
An exploration of pathways involved in lung carcinoid progression using gene expression profiling.
Speel et al., Maastricht, Netherlands. In Carcinogenesis, 2013
At the individual gene level, BIRC5 (survivin), BUB1, CD44, IL20RA, KLK12 and OTP were independent predictors of patient outcome.
Common variation in Kallikrein genes KLK5, KLK6, KLK12, and KLK13 and risk of prostate cancer and tumor aggressiveness.
Australian Prostate Cancer BioResource et al., Brisbane, Australia. In Urol Oncol, 2013
We sought to elucidate the role of common genetic variation in four of the Kallikrein genes, KLK5, KLK6, KLK12, and KLK13, in prostate cancer risk and tumor aggressiveness.
Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12.
Whittaker et al., Ithaca, United States. In J Biol Chem, 2013
Each peptidase appears to have a preference for particular influenza subtypes, with kallikrein 5 cleaving the H1 and H3 subtypes most efficiently and kallikrein 12 cleaving the H1 and H2 subtypes most efficiently.
Elevated immunoglobulin to tissue KLK11 in patients with Sjögren syndrome.
Shao et al., Louisville, United States. In Cornea, 2013
METHODS: Sera from 11 patients diagnosed with SS, 8 patients with dry eye disease (DED), and 8 normal age/sex-matched controls (NL) were collected for detecting antibodies against tissue KLK1, KLK11, KLK12, and KLK13 by capture enzyme-linked immunosorbent assay.
Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor.
Heuzé-Vourc'h et al., Tours, France. In Biol Chem, 2013
Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway.
Clinical significance of human kallikrein 12 gene expression in gastric cancer.
Cao et al., Shanghai, China. In World J Gastroenterol, 2013
AIM: To investigate whether the expression of kallikrein 12 (KLK12) is related to the development of gastric cancer (GC) and to determine the role of KLK12 in gastric cancer cells growth, invasion and migration.
Human kallikrein-related peptidase 12 (KLK12) splice variants expression in breast cancer and their clinical impact.
Ardavanis et al., Athens, Greece. In Tumour Biol, 2012
Results suggest that kallikrein-related peptidase 12 (KLK12) splice variant KLK12sv3 can be regarded as a marker of good prognosis in breast cancer.
Inhibition of transcription factor specificity protein 1 alters the gene expression profile of keratinocytes leading to upregulation of kallikrein-related peptidases and thymic stromal lymphopoietin.
Leung et al., Denver, United States. In J Invest Dermatol, 2011
Strikingly, six kallikrein (KLK)-related peptidase genes, namely KLK5, KLK6, KLK7, KLK8, KLK10, and KLK12, were upregulated in NHKs following Sp1 silencing.
Kallikrein-related peptidase 12 hydrolyzes matricellular proteins of the CCN family and modifies interactions of CCN1 and CCN5 with growth factors.
Courty et al., Tours, France. In J Biol Chem, 2011
KLK12 may indirectly regulate the bioavailability and activity of several growth factors through processing of their CCN binding partners
Inhibition of kallikrein-related peptidases by the serine protease inhibitor of Kazal-type 6.
Meyer-Hoffert et al., Kiel, Germany. In Peptides, 2011
Serine protease of Kazal-type (SPINK6) expressed in normal human skin is a potent natural inhibitor of Kallikrein-related peptidases, KLK12 and KLK13.
Activation profiles of human kallikrein-related peptidases by proteases of the thrombostasis axis.
Blaber et al., Tallahassee, United States. In Protein Sci, 2008
Pro-KLK11 and 12 can be activated by a broad-spectrum of thrombostasis proteases, with thrombin exhibiting a high degree of selectivity for pro-KLK12.
Enzymatic properties of human kallikrein-related peptidase 12 (KLK12).
Luo et al., Toronto, Canada. In Biol Chem, 2007
KLK12 has trypsin-like activity, cleaving peptide bonds after both arginine & lysine. It quickly loses its activity due to autodegradation, its activity can also be rapidly inhibited by zinc ions & by alpha2-antiplasmin through covalent complex formation.
Splice-site genetic polymorphism of the human kallikrein 12 (KLK12) gene correlates with no substantial expression of KLK12 protein having serine protease activity.
Sugimura et al., Hamamatsu, Japan. In Hum Mutat, 2004
4 types of polymorphisms were found in Japanese gastric cancer: 1 at an intron 4 splice-donor site (c.457+2T>C), 2 in exon 6 (c.618_619delTG:p.Cys206fsX72 & c.735G>A:p.Met245Ile), & 1 in intron 3. c.457+2C/C has no hK12 serine protease expression.
The new human kallikrein gene family: implications in carcinogenesis.
Obiezu et al., Toronto, Canada. In Trends Endocrinol Metab, 2000
Another five putative kallikrein genes, provisionally named KLK-L2, KLK-L3, KLK-L4, KLK-L5 and KLK-L6, have also been identified.
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