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Plasmin is an important enzyme present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein is encoded by the PLG gene.
High-molecular-weight kininogen is a circulating plasma protein which participates in the initiation of blood coagulation, and in the generation of the vasodilator bradykinin via the kallikrein-kinin system. HMWK is inactive until it either adheres to binding proteins beneath an endothelium disrupted by injury, thereby initiating coagulation; or it binds to intact endothelial cells or platelets for functions other than coagulation.
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.
Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein 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.
Plasma kallikrein is an enzyme that catalyses the following chemical reaction:
Kininogens are precursor proteins for kinins, biologically active polypeptides involved in blood coagulation, vasodilation, smooth muscle contraction, inflammatory regulation, and the regulation of the cardiovascular and renal systems.
Kallikrein-1 is a protein that in humans is encoded by the KLK1 gene. KLK1 is a member of the peptidase S1 family.
Bradykinin receptor B1 (B1) is a G-protein coupled receptor encoded by the BDKRB1 gene in humans. Its principal ligand is bradykinin, a 9 amino acid peptide generated in pathophysiologic conditions such as inflammation, trauma, burns, shock, and allergy. The B1 receptor is one of two of G protein-coupled receptors that have been found which bind bradykinin and mediate responses to these pathophysiologic conditions.
In enzymology, a phosphoacetylglucosamine mutase is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphoamidase (EC 3.9.1.1) is an enzyme that catalyzes the chemical reaction
Kininogen-1 (KNG1), also known as alpha-2-thiol proteinase inhibitor, Williams-Fitzgerald-Flaujeac factor or the HMWK-kallikrein factor is a protein that in humans is encoded by the KNG1 gene. Kininogen-1 is the precursor protein to high-molecular-weight kininogen (HMWK), low-molecular-weight kininogen (LMWK), and bradykinin.
Palmitoyl-CoA hydrolase (EC 3.1.2.2) is an enzyme in the family of hydrolases that specifically acts on thioester bonds. It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the corresponding thiol:
In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction
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Ecallantide is a drug used for the treatment of hereditary angioedema (HAE) and in the prevention of blood loss in cardiothoracic surgery. It is an inhibitor of the protein kallikrein and a 60-amino acid polypeptide which was developed from a Kunitz domain through phage display to mimic antibodies inhibiting kallikrein.
Xaa-Pro aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
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In the contact activation system or CAS, three proteins in the blood, factor XII (FXII), prekallikrein (PK) and high molecular weight kininogen (HK), bind to a surface and cause blood coagulation and inflammation. FXII and PK are proteases and HK is a non-enzymatic co-factor. The CAS can activate the kinin–kallikrein system and blood coagulation through its ability to activate multiple downstream proteins. The CAS is initiated when FXII binds to a surface and reciprocal activation of FXII and PK occurs, forming FXIIa and PKa. FXIIa can initiate the coagulation cascade by cleaving and activating factor XI (FXI), which leads to formation of a blood clot. Additionally, the CAS can activate the kinin–kallikrein system when PKa cleaves HK to form cHK, releasing a peptide known as bradykinin (BK). BK and its derivatives bind to bradykinin receptors B1 and B2 to mediate inflammation.
In enzymology, a prostaglandin-F synthase (PGFS; EC 1.1.1.188) is an enzyme that catalyzes the chemical reaction:
References
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- ↑ Anundi H, Ronne H, Peterson PA, Rask L (December 1982). "Partial amino-acid sequence of the epidermal growth-factor-binding protein". European Journal of Biochemistry. 129 (2): 365–71. doi: 10.1111/j.1432-1033.1982.tb07059.x . PMID 6295764.
- ↑ Pesquero JL, Boschcov P, Oliveira MC, Paiva AC (October 1982). "Effect of substrate size on tonin activity". Biochemical and Biophysical Research Communications. 108 (4): 1441–6. doi:10.1016/s0006-291x(82)80068-5. PMID 6295383.
- ↑ Gutkowska J, Corvol P, Figueiredo AF, Inagami T, Bouhnik J, Genest J (1984). "Kinetic studies of rat renin and tonin on purified rat angiotensinogen". Canadian Journal of Biochemistry and Cell Biology. 62 (2–3): 137–42. doi:10.1139/o84-020. PMID 6097352.
- ↑ Kato H, Enjyoji K, Miyata T, Hayashi I, Oh-ishi S, Iwanaga S (February 1985). "Demonstration of arginyl-bradykinin moiety in rat HMW kininogen: direct evidence for liberation of bradykinin by rat glandular kallikreins". Biochemical and Biophysical Research Communications. 127 (1): 289–95. doi:10.1016/s0006-291x(85)80157-1. PMID 3844939.
- ↑ Akiyama K, Nakamura T, Iwanaga S, Hara M (December 1987). "The chymotrypsin-like activity of human prostate-specific antigen, gamma-seminoprotein". FEBS Letters. 225 (1–2): 168–72. doi: 10.1016/0014-5793(87)81151-1 . PMID 3691800.
- ↑ Evans BA, Drinkwater CC, Richards RI (June 1987). "Mouse glandular kallikrein genes. Structure and partial sequence analysis of the kallikrein gene locus". The Journal of Biological Chemistry. 262 (17): 8027–34. doi: 10.1016/S0021-9258(18)47521-7 . PMID 3036794.
- ↑ Fiedler F (March 1987). "Effects of secondary interactions on the kinetics of peptide and peptide ester hydrolysis by tissue kallikrein and trypsin". European Journal of Biochemistry. 163 (2): 303–12. doi: 10.1111/j.1432-1033.1987.tb10801.x . PMID 3643848.
- ↑ Fujinaga M, James MN (May 1987). "Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution". Journal of Molecular Biology. 195 (2): 373–96. doi:10.1016/0022-2836(87)90658-9. PMID 2821276.
- ↑ Kato H, Nakanishi E, Enjyoji K, Hayashi I, Oh-ishi S, Iwanaga S (December 1987). "Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes". Journal of Biochemistry. 102 (6): 1389–404. doi:10.1093/oxfordjournals.jbchem.a122185. PMID 3482210.
- ↑ Bailey GS (1989). "Rat pancreas kallikrein". Immunochemical Techniques Part M: Chemotaxis and Inflammation. Methods in Enzymology. Vol. 163. pp. 115–28. doi:10.1016/0076-6879(88)63013-8. ISBN 978-0-12-182064-0. PMID 3237072.
- ↑ Blaber M, Isackson PJ, Marsters JC, Burnier JP, Bradshaw RA (September 1989). "Substrate specificities of growth factor associated kallikreins of the mouse submandibular gland". Biochemistry. 28 (19): 7813–9. doi:10.1021/bi00445a043. PMID 2611215.
- ↑ Chao J, Chao L (1988). "Rat urinary kallikrein". Immunochemical Techniques Part M: Chemotaxis and Inflammation. Methods in Enzymology. Vol. 163. pp. 128–43. doi:10.1016/0076-6879(88)63014-x. ISBN 978-0-12-182064-0. PMID 3070295.
- ↑ Geiger R, Miska W (1988). "[101 Human tissue kallikrein". Immunochemical Techniques Part M: Chemotaxis and Inflammation. Methods in Enzymology. Vol. 163. pp. 102–15. doi:10.1016/0076-6879(88)63012-6. ISBN 978-0-12-182064-0. PMID 3237071.
- ↑ Bertrand R, Derancourt J, Kassab R (March 1989). "Selective cleavage at lysine of the 50 kDa-20 kDa connector loop segment of skeletal myosin S-1 by endoproteinase Arg-C". FEBS Letters. 246 (1–2): 171–6. doi: 10.1016/0014-5793(89)80277-7 . PMID 2523317.
- ↑ Wines DR, Brady JM, Pritchett DB, Roberts JL, MacDonald RJ (May 1989). "Organization and expression of the rat kallikrein gene family". The Journal of Biological Chemistry. 264 (13): 7653–62. doi: 10.1016/S0021-9258(18)83284-7 . PMID 2708383.
- ↑ Elmoujahed A, Gutman N, Brillard M, Gauthier F (June 1990). "Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland". FEBS Letters. 265 (1–2): 137–40. doi: 10.1016/0014-5793(90)80903-v . PMID 2194829.
- ↑ Xiong W, Chen LM, Chao J (February 1990). "Purification and characterization of a kallikrein-like T-kininogenase". The Journal of Biological Chemistry. 265 (5): 2822–7. doi: 10.1016/S0021-9258(19)39875-8 . PMID 2303430.
