Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro. By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177.
CD177 is polymorphic and has at least two alleles: PRV1 and NB1. Human PRV1 is a Glycosyl-Phosphatidylinositol (GPI)-linked cell surface glycoprotein that belongs to the uPAR/CD59/Ly6 family of receptors. PRV1 is expressed by neutrophils and neutrophil precursors,and changes in expression serve as diagnostic markers for myeloproliferative disorders such as polycythemia vera and essential thrombocythemia. PRV1 may also be expressed by Erythroblasts, B cells, and Monocytes. NB1, a Glycosyl-Phosphatidylinositol (GPI)-linked cell surface glycoprotein, was first described in a case of neonatal alloimmune neutropenia. It is reported that CD177 functions as a novel heterophilic binding partner that engages PECAM-1 in membrane-proximal IgD6.
PS6K, also known as RPS6KB1, is a serine/threonine-protein kinase. It belongs to the RSK (ribosomal s6 kinase) family. Members of this family function in signal transduction. PS6K is an isoform of p70 ribosomal S6 kinase (S6K). S6K can be activated by mitogenic stimuli such as growth factors, insulin and cytokines. It phosphorylates the ribosomal protein S6. PS6K also phosphorylates other proteins such as elF4B, eEF2K and SKAR. It is a crucial effector of mTOR(rapamycin) signaling. PS6K is dissociated from the EIF3 complex and activated upon mitogenic stimulation, phosphorylation by the mammalian target of mTOR complex 1 (mTORC1). Its active form then phosphorylates and activates several substrates in the preinitiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. PS6K also functions in cell proliferation, cell growth and cell cycle progression.
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 members of the Kallikrein subfamily located in a cluster on chromosome 19. Its encoded protein is secreted and may play a role in suppression of tumorigenesis in breast and prostate cancers. Alternate splicing of this gene results in multiple transcript variants encoding the same protein.
KLK3; also known as APS; is short for Prostate-specific antigen. It is a 261 aa. protein which belongs to the peptidase S1 family and Kallikrein subfamily. This protein has 5 isforms produced by alternative splicing. It is a secreted protein and can forms a heterodimer with SERPINA5 which can inhibit its activity. KLK3 is also strongly inhibited by Zn2+; 100 times more abundant in semen than in serum. This inhibition is relieved by exposure to semenogelins; which are avid zinc binders. KLK3 can hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.
KLK3(Kallikrein 3); also known as Prostate Specific Antigen (PSA); kallikrein-related peptidase 3; Gamma-seminoprotein; is a secreted protein of the glandular kallikrein subfamily of serine proteases.KLK3 contains one peptidase S1 domain.KLK3 is a glycoprotein produced almost exclusively by the prostate gland. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers.
This gene encodes a highly conserved preproprotein that is proteolytically processed to generate four main cleavage products including saposins A, B, C, and D. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Mutations in this gene have been associated with Gaucher disease and metachromatic leukodystrophy. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
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