Kallikrein

Kallikrein-8 is a serine protease which degrades various proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Kallikrein-8 takes part in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is essential for memory acquisition and synaptic plasticity. Kallikrein-8 participates in the secondary phase of pathogenesis following spinal cord injury and also takes part in skin desquamation and keratinocyte proliferation.

KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 cleaves insulin B chain at ''6-Leu- -Cys-7'', ''16-Tyr- -Leu-17'', ''25-Phe- -Tyr-26'' and ''26-Tyr--Thr-27''. KLK7 is involved in the activation of precursors to inflammatory cytokines.

KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 is involved in the activation of precursors to inflammatory cytokines.

Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.

Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.

Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 is assumed to act normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

Kallikrein-3 or KLK3 is a serine proteases subgroup, enzymes can cleave peptide bonds. KLK3 is found in the prostate and may be hold accountable to the regulation of semen liquefaction via seminogelin hydrolysis. The protein is expressed in low concentrations in men with healthy prostates serum. When elevated quantities are found it may show prostate cancer or different prostate disorders such as prostatitis and benign prostatic hyperplasia.

KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.

KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.

Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.

Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.

Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.

Kallikreins are a subgroup of serine proteases having various physiological functions. Many kallikreins are implicated in carcinogenesis and some have potential of becoming novel cancer and other disease biomarkers. Kallikrein-13 (KLK13) is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK13 gene expression is regulated by steroid hormones and may be useful as a marker for breast cancer.

Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.

Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

Kallikreins are serine protease enzymes having various physiological functions.
Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.
Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin.
Kallikrein-1, which derived from human or porcine, have been used as drugs for a long time, they are mainly used in the treatment f light to medium hypertension and occlusion of cerebral and surrounding blood vessels.
KLK1 demonstrates both trypsin- and chymotrypsin-like selectivities with Tyr/Arg preferred at site P1, Ser/Arg strongly preferred at P1', and Phe/Leu at P2.
rs5517 in the KLK1 gene is considerably connected with hypertension in a Chinese Han population. KLK1 is expressed de novo in endothelial cells and mediates relaxation of human umbilical veins. The K allele of KLK1 promoter and TT genotype of TGF-beta1 are a genetic KLK1 -130 GN and -128 G-C, and the defenselessness factor contributing to progressive renal descent in Taiwanese primary vesicoureteric reflux children.
Induction of KLK1 in carotid arteriosclerosis doesn’t lead to kallikrein-kinins pathway activation. Transgenic rats expressing KLK1 have impaired renal response to acute volume expansion Endothelial cells synthesize and release active form of KLK1on the surface which is important function in maintenance of circulation homeostasis.
KLK1 participates in epidermal desquamation through cleavage of desmoglein 1 and regulation by lympho-epithelial Kazal-type-related inhibitor (LEKTI).

Kallikreins are serine protease enzymes having various physiological functions.
Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.
Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin.
Kallikrein-1, which derived from human or porcine, have been used as drugs for a long time, they are mainly used in the treatment f light to medium hypertension and occlusion of cerebral and surrounding blood vessels.
KLK1 demonstrates both trypsin- and chymotrypsin-like selectivities with Tyr/Arg preferred at site P1, Ser/Arg strongly preferred at P1', and Phe/Leu at P2.
rs5517 in the KLK1 gene is considerably connected with hypertension in a Chinese Han population. KLK1 is expressed de novo in endothelial cells and mediates relaxation of human umbilical veins. The K allele of KLK1 promoter and TT genotype of TGF-beta1 are a genetic KLK1 -130 GN and -128 G-C, and the defenselessness factor contributing to progressive renal descent in Taiwanese primary vesicoureteric reflux children.
Induction of KLK1 in carotid arteriosclerosis doesn’t lead to kallikrein-kinins pathway activation. Transgenic rats expressing KLK1 have impaired renal response to acute volume expansion Endothelial cells synthesize and release active form of KLK1on the surface which is important function in maintenance of circulation homeostasis.
KLK1 participates in epidermal desquamation through cleavage of desmoglein 1 and regulation by lympho-epithelial Kazal-type-related inhibitor (LEKTI).