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Kallikrein
Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by ''KLKB1 gene'') has no known paralogue, while tissue kallikrein-related peptidases (''KLKs'') encode a family of fifteen closely related serine proteases. These genes are localised to chromosome 19q13, forming the largest contiguous cluster of proteases within the human genome. Kallikreins are responsible for the coordination of various physiological functions including blood pressure, semen liquefaction and skin desquamation. Occurrence In 1934, Eugen Werle reported finding a substance in the pancreas of humans and various animals in such large amounts that the pancreas could be taken for its site of origin. He named it kallikrein, by derivation from the Greek word for pancreas. Since then, similar enzymes have been found in the biological fluids of humans and other mammals, as well as in some snake venoms. Venom The caterpillar known ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KLK1
Kallikrein-1 is a protein that in humans is encoded by the ''KLK1'' gene. KLK1 is a member of the peptidase S1 family. 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. See also * Kinin–kallikrein system * Kininogen 1 References Further reading * * * * * * * * * * * * * * * * * * * External links * The MEROPS MEROPS is an online database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors. The classification scheme for peptidases was published by Rawlings & Barrett in 1993, and that for protei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KLK2
Kallikrein-2 is a protein that in humans is encoded by the ''KLK2'' gene, and is particularly associated with prostatic tissue. References Further reading * * * * * * * * * * * * * * * * * * * External links * The MEROPS MEROPS is an online database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors. The classification scheme for peptidases was published by Rawlings & Barrett in 1993, and that for protein inhibi ... online database for peptidases and their inhibitorsS01.161 * {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KLK12
Kallikrein-12 is a protein that in humans is encoded by the ''KLK12'' gene. 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. References Further reading * * * * * * * * * * * External links * The MEROPS MEROPS is an online database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors. The classification scheme for peptidases was published by Rawlings & Barrett in 1993, and that for protein inhibi ... online database for peptidases and their inhibitorsS01.020 {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kinin
A kinin is any of various structurally related polypeptides, such as bradykinin and kallidin. They are members of the autacoid family. Kinins are peptides that are cleaved from kininogens by the process of kallikreins. Kallikreins activate kinins when stimulated. It is a component of the kinin-kallikrein system. Their precursors are kininogens. Kininogens contain a 9-11 amino acid bradykinin sequence. In botany, the plant hormones known as cytokinins were first called kinins, but the name was changed to avoid confusion. Effects of Kinins Kinin are short lived peptides that cause pain sensation, arteriolar dilation, increase vascular permeability and cause contractions in smooth muscle. Kinins transmit their effects through G protein- coupled receptors. Kinin act on axons to block nervous impulses, which leads to distal muscle relaxation. Kinin are also potent nerve stimulators. which is mostly responsible for the sense of pain (and sometimes itching). Kinin increase vascula ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Skin Desquamation
Desquamation occurs when the outermost layer of a tissue, such as the skin, is shed. The term is . Physiologic desquamation Keratinocytes are the predominant cells of the epidermis, the outermost layer of the skin. Living keratinocytes reside in the basal, spinous, or granular layers of the epidermis. The outermost layer of the epidermis is called the Stratum corneum and it is composed of terminally differentiated keratinocytes, the Corneocytes. In the absence of disease, desquamation occurs when corneocytes are individually shed unnoticeably from the surface of the skin. Typically the time it takes for a corneocyte to be formed and then shed is about 14 weeks but this time can vary depending on the anatomical location that the skin is covering. For example, desquamation occurs more slowly at acral (palm and sole) surfaces and more rapidly where the skin is thin, such as the eyelids. Normal desquamation can be visualized by immersing skin in warm or hot water. This induces the oute ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
KLKB1
KLKB1 is a gene that, in humans, encodes the ''Plasma kallikrein'' protein. Function Plasma prekallikrein is a glycoprotein that participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation. It is synthesized in the liver and secreted into the blood as a single polypeptide chain. Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond. Plasma kallikrein therefore is composed of a heavy chain and a light chain held together by a disulfide bond. The heavy chain originates from the amino-terminal end of the zymogen and contains 4 tandem repeats of 90 or 91 amino acids. Each repeat harbors a novel structure called the apple domain. The heavy chain is required for the surface-dependent pro-coagulant activity of plasma kallikrein. The light chain contains the active site or catalytic domain of the enzyme and is homologous to the trypsin family of serine proteas ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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