KLKB1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Kallikrein B, plasma (Fletcher factor) 1
Protein KLKB1 PDB 2anw.png
PDB rendering based on 2anw.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols KLKB1 ; KLK3; PPK
External IDs OMIM229000 MGI102849 HomoloGene68097 ChEMBL: 2000 GeneCards: KLKB1 Gene
EC number 3.4.21.34
RNA expression pattern
PBB GE KLKB1 206541 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3818 16621
Ensembl ENSG00000164344 ENSMUSG00000031640
UniProt P03952 P26262
RefSeq (mRNA) NM_000892 NM_008455
RefSeq (protein) NP_000883 NP_032481
Location (UCSC) Chr 4:
187.13 – 187.18 Mb
Chr 8:
45.27 – 45.29 Mb
PubMed search [1] [2]

Plasma kallikrein is a protein that in humans is encoded by the KLKB1 gene.[1][2]

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 proteases. Plasma prekallikrein deficiency causes a prolonged activated partial thromboplastin time in patients.[3]

Interactions[edit]

KLKB1 has been shown to interact with High-molecular-weight kininogen.[4][5][6][7]

References[edit]

  1. ^ Yu H, Bowden DW, Spray BJ, Rich SS, Freedman BI (April 1998). "Identification of human plasma kallikrein gene polymorphisms and evaluation of their role in end-stage renal disease". Hypertension 31 (4): 906–11. doi:10.1161/01.hyp.31.4.906. PMID 9535413. 
  2. ^ Chung DW, Fujikawa K, McMullen BA, Davie EW (August 1986). "Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats". Biochemistry 25 (9): 2410–7. doi:10.1021/bi00357a017. PMID 3521732. 
  3. ^ "Entrez Gene: KLKB1 kallikrein B, plasma (Fletcher factor) 1". 
  4. ^ Thompson, R E; Mandle R; Kaplan A P (October 1979). "Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 76 (10): 4862–6. doi:10.1073/pnas.76.10.4862. ISSN 0027-8424. PMC 413037. PMID 291905. 
  5. ^ Page, J D; You J L; Harris R B; Colman R W (October 1994). "Localization of the binding site on plasma kallikrein for high-molecular-weight kininogen to both apple 1 and apple 4 domains of the heavy chain". Arch. Biochem. Biophys. (UNITED STATES) 314 (1): 159–64. doi:10.1006/abbi.1994.1424. ISSN 0003-9861. PMID 7944388. 
  6. ^ Herwald, H; Jahnen-Dechent W, Alla S A, Hock J, Bouma B N, Müller-Esterl W (July 1993). "Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the prekallikrein heavy chain". J. Biol. Chem. (UNITED STATES) 268 (19): 14527–35. ISSN 0021-9258. PMID 7686159. 
  7. ^ Renné, T; Dedio J, Meijers J C, Chung D, Müller-Esterl W (September 1999). "Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2". J. Biol. Chem. (UNITED STATES) 274 (36): 25777–84. doi:10.1074/jbc.274.36.25777. ISSN 0021-9258. PMID 10464316. 

Further reading[edit]

  • Thompson RE, Mandle R, Kaplan AP (1980). "Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain". Proc. Natl. Acad. Sci. U.S.A. 76 (10): 4862–6. doi:10.1073/pnas.76.10.4862. PMC 413037. PMID 291905. 
  • Aznar JA, España F, Aznar J et al. (1978). "Fletcher factor deficiency: report of a new family". Scandinavian journal of haematology 21 (2): 94–8. doi:10.1111/j.1600-0609.1978.tb02498.x. PMID 694428. 
  • Henderson LM, Figueroa CD, Muller-Esterl W et al. (1993). "Immunovisualisation of plasma prekallikrein and H-kininogen on human neutrophils and in human hepatocytes". Agents Actions Suppl. 38 (1): 590–4. doi:10.1007/978-3-0348-7321-5_72. PMID 1466300. 
  • Beaubien G, Rosinski-Chupin I, Mattei MG et al. (1991). "Gene structure and chromosomal localization of plasma kallikrein". Biochemistry 30 (6): 1628–35. doi:10.1021/bi00220a027. PMID 1993180. 
  • McMullen BA, Fujikawa K, Davie EW (1991). "Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule". Biochemistry 30 (8): 2050–6. doi:10.1021/bi00222a007. PMID 1998666. 
  • España F, Berrettini M, Griffin JH (1989). "Purification and characterization of plasma protein C inhibitor". Thromb. Res. 55 (3): 369–84. doi:10.1016/0049-3848(89)90069-8. PMID 2551064. 
  • Fujikawa K, Chung DW, Hendrickson LE, Davie EW (1986). "Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein". Biochemistry 25 (9): 2417–24. doi:10.1021/bi00357a018. PMID 3636155. 
  • Herwald H, Jahnen-Dechent W, Alla SA et al. (1993). "Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the prekallikrein heavy chain". J. Biol. Chem. 268 (19): 14527–35. PMID 7686159. 
  • Page JD, You JL, Harris RB, Colman RW (1994). "Localization of the binding site on plasma kallikrein for high-molecular-weight kininogen to both apple 1 and apple 4 domains of the heavy chain". Arch. Biochem. Biophys. 314 (1): 159–64. doi:10.1006/abbi.1994.1424. PMID 7944388. 
  • Henderson LM, Figueroa CD, Müller-Esterl W, Bhoola KD (1994). "Assembly of contact-phase factors on the surface of the human neutrophil membrane". Blood 84 (2): 474–82. PMID 8025275. 
  • Shimomura T, Kondo J, Ochiai M et al. (1993). "Activation of the zymogen of hepatocyte growth factor activator by thrombin". J. Biol. Chem. 268 (30): 22927–32. PMID 8226803. 
  • Ciechanowicz A, Bader M, Wagner J, Ganten D (1994). "Extra-hepatic transcription of plasma prekallikrein gene in human and rat tissues". Biochem. Biophys. Res. Commun. 197 (3): 1370–6. doi:10.1006/bbrc.1993.2628. PMID 8280154. 
  • Petersen LC, Sprecher CA, Foster DC et al. (1996). "Inhibitory properties of a novel human Kunitz-type protease inhibitor homologous to tissue factor pathway inhibitor". Biochemistry 35 (1): 266–72. doi:10.1021/bi951501d. PMID 8555184. 
  • Hermann A, Buchinger P, Somlev B, Rehbock J (1996). "High and low molecular weight kininogen and plasma prekallikrein/plasma kallikrein in villous capillaries of human term placenta". Placenta 17 (4): 223–30. doi:10.1016/S0143-4004(96)90042-9. PMID 8761966. 
  • Durham SK, Suwanichkul A, Hayes JD et al. (1999). "The heparin binding domain of insulin-like growth factor binding protein (IGFBP)-3 increases susceptibility of IGFBP-3 to proteolysis". Horm. Metab. Res. 31 (2–3): 216–25. doi:10.1055/s-2007-978722. PMID 10226805. 
  • Renné T, Dedio J, Meijers JC et al. (1999). "Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2". J. Biol. Chem. 274 (36): 25777–84. doi:10.1074/jbc.274.36.25777. PMID 10464316. 
  • Hermann A, Arnhold M, Kresse H et al. (1999). "Expression of plasma prekallikrein mRNA in human nonhepatic tissues and cell lineages suggests special local functions of the enzyme". Biol. Chem. 380 (9): 1097–102. doi:10.1515/BC.1999.136. PMID 10543447. 
  • Cerf M, Raidoo D, Fink E et al. (2000). "Plasma kallikrein localisation in human blood vessels". Immunopharmacology 44 (1–2): 75–80. doi:10.1016/S0162-3109(99)00112-5. PMID 10604527.