KLKB1

KLKB1
Identificadores
Número EC	3.4.21.34
Número CAS	410538-33-9
Bases de datos
IntEnz	vista de IntEnz
BRENDA	entrada de BRENDA
ExPASy	vista de NiceZyme
KEGG	entrada de KEGG
MetaCyc	vía metabólica
PRIAM	perfil
Estruturas PDB	RCSB PDB PDBe PDBj PDBsum
Procura
PMC	artigos
PubMed	artigos
NCBI Protein	procura

KLKB1
Estruturas dispoñibles
PDB	Buscar ortólogos: PDBe, RCSB Lista de códigos PDB 4OGY, 2ANW , 4OGX , 4ZJ4 , 2ANY , 4ZJ5 , 4ZJ6 ;
Identificadores
Nomenclatura	Outros nomes KLKB1, KLK3, PPK, PKKD, PKK, calicreína B1 ;
Símbolos	KLKB1 (HGNC: 6371) KLKB1, KLK3, PPK, PKKD, PKK, calicreína B1
Identificadores; externos	OMIM: 229000 ; MGI: 102849 ; HomoloGene: 68097 ; EBI: KLKB1; GeneCards: Xene KLKB1; UniProt: KLKB1;
Locus	Cr. 4 q35.2
Ontoloxía Xénica	Referencias: AmiGO / QuickGO
	Referencias: AmiGO / QuickGO
Padrón de expresión de ARNm
	Máis información
Ortólogos
Especies
Humano	Rato
Entrez
3818	16621
Ensembl
Véxase HS	Véxase MM
UniProt
P03952	ENSMUSG00000109764
RefSeq; (ARNm)
NM_000892	NM_008455
RefSeq; (proteína) NCBI
NP_000883	NP_032481
Localización (UCSC)
Cr. 4:; 186.21 – 186.26 Mb	Cr. 8:; 45.72 – 45.75 Mb
PubMed (Busca)
3818 ;	16621

O KLKB1 é un xene que nos humanos está situado no cromosoma 4 e que codifica a proteína encimática calicreína plasmática (EC 3.4.21.34),^[1]^[2] que tamén recibe, entre outros, os nomes de calicreína sérica, calicreína B1 e calicreína B.^[3]^[4]^[5]^[6]^[7] Este encima cataliza a seguinte reacción química: corte selectivo dalgúns enlaces peptídicos nos que interveñen a arxinina ou a lisina no cininóxeno humano, incluíndo os enlaces lisina-arxinina e arxinina-serina para liberar bradicinina.

Este encima fórmase a partir da precalicreína plasmática (factor de Fletcher) por acción do factor XIIa.

Función[editar | editar a fonte]

A precalicreína plasmática é unha glicoproteína que participa na activación dependente de superficie da coagulación do sangue, fibrinólise, xeración de cininas e inflamación. Sintetízase no fígado e segrégase ao sangue como unha soa cadea polipeptídica. A precalicreína plasmática convértese en calicreína plasmática pola acción do factor XIIa polo corte dun enlace interno Arg-Ile. A calicreína plasmática, por tanto, está composta por unha cadea pesada e unha lixeira unidas por unha ponte disulfuro. A cadea pesada orixínase a partir do extremo amino terminal do cimóxeno e contén 4 repeticións en tándem de 90 ou 91 aminoácidos. Cada repetición contén unha estrutura peculiar chamada dominio mazá. A cadea pesada é necesaria para a actividade procoagulante dependete de supericie da calicreína plasmática. A cadea lixeira contén o sitio activo ou dominio catalítico do encima e é homóloga da familia da tripsina de serina proteases. A deficiencia en precalicreína plasmática causa unha activación prolongada do tempo de tromboplastina parcial nos pacientes. O empalme alternativo orixina múltiples variantes de transcrición que codifican diferentes isoformas^[8]

Interaccións[editar | editar a fonte]

A KLKB1 (calicreína plasmática) presenta interaccións co cininóxeno de alto peso molecular.^[9]^[10]^[11]^[12]

Notas[editar | editar a fonte]

↑ Yu H, Bowden DW, Spray BJ, Rich SS, Freedman BI (abril de 1998). "Identification of human plasma kallikrein gene polymorphisms and evaluation of their role in end-stage renal disease". Hypertension 31 (4): 906–11. PMID 9535413. doi:10.1161/01.hyp.31.4.906.
↑ Chung DW, Fujikawa K, McMullen BA, Davie EW (agosto de 1986). "Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats". Biochemistry 25 (9): 2410–7. PMID 3521732. doi:10.1021/bi00357a017.
↑ Heimark RL, Davie EW (1981). "Bovine and human plasma prekallikrein". Methods in Enzymology. 80 Pt C: 157–72. PMID 6918767. doi:10.1016/s0076-6879(81)80016-x.
↑ McRae BJ, Kurachi K, Heimark RL, Fujikawa K, Davie EW, Powers JC (decembro de 1981). "Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates". Biochemistry 20 (25): 7196–206. PMID 6976185. doi:10.1021/bi00528a022.
↑ Silverberg M, Kaplan AP (1988). "Prekallikrein". Methods in Enzymology 163: 85–95. ISBN 9780121820640. PMID 3237096. doi:10.1016/0076-6879(88)63010-2.
↑ Seidah NG, Ladenheim R, Mbikay M, Hamelin J, Lutfalla G, Rougeon F, Lazure C, Chrétien M (outubro de 1989). "The cDNA structure of rat plasma kallikrein". DNA 8 (8): 563–74. PMID 2598771. doi:10.1089/dna.1989.8.563.
↑ Tsuda Y, Teno N, Okada Y, Wanaka K, Bohgaki M, Hijikata-Okunomiya A, Okamoto U, Naito T, Okamoto S (novembro de 1989). "Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein". Chemical & Pharmaceutical Bulletin 37 (11): 3108–11. PMID 2534361. doi:10.1248/cpb.37.3108.
↑ "Entrez Gene: KLKB1 kallikrein B, plasma (Fletcher factor) 1".
↑ Thompson RE, Mandle R, Kaplan AP (outubro de 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. 76 (10): 4862–6. Bibcode:1979PNAS...76.4862T. PMC 413037. PMID 291905. doi:10.1073/pnas.76.10.4862.
↑ Page JD, You JL, Harris RB, Colman RW (outubro de 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. PMID 7944388. doi:10.1006/abbi.1994.1424.
↑ Herwald H, Jahnen-Dechent W, Alla SA, Hock J, Bouma BN, Müller-Esterl W (xullo de 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. doi:10.1016/S0021-9258(19)85270-5.
↑ Renné T, Dedio J, Meijers JC, Chung D, Müller-Esterl W (setembro de 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. PMID 10464316. doi:10.1074/jbc.274.36.25777.

Véxase tamén[editar | editar a fonte]

Bibliografía[editar | editar a fonte]

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. PMC 413037. PMID 291905. doi:10.1073/pnas.76.10.4862.
Aznar JA, España F, Aznar J, Tascon A, Jimenez C (1978). "Fletcher factor deficiency: report of a new family". Scandinavian Journal of Haematology 21 (2): 94–8. PMID 694428. doi:10.1111/j.1600-0609.1978.tb02498.x.
Henderson LM, Figueroa CD, Muller-Esterl W, Stain A, Bhoola KD (1993). "Immunovisualisation of plasma prekallikrein and H-kininogen on human neutrophils and in human hepatocytes". Recent Progress on Kinins. Agents Actions Suppl. 38. pp. 590–4. ISBN 978-3-0348-7323-9. PMID 1466300. doi:10.1007/978-3-0348-7321-5_72.
Beaubien G, Rosinski-Chupin I, Mattei MG, Mbikay M, Chrétien M, Seidah NG (1991). "Gene structure and chromosomal localization of plasma kallikrein". Biochemistry 30 (6): 1628–35. PMID 1993180. doi:10.1021/bi00220a027.
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. PMID 1998666. doi:10.1021/bi00222a007.
España F, Berrettini M, Griffin JH (1989). "Purification and characterization of plasma protein C inhibitor". Thromb. Res. 55 (3): 369–84. PMID 2551064. doi:10.1016/0049-3848(89)90069-8.
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. PMID 3636155. doi:10.1021/bi00357a018.
Herwald H, Jahnen-Dechent W, Alla SA, Hock J, Bouma BN, Müller-Esterl W (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. doi:10.1016/S0021-9258(19)85270-5.
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. PMID 7944388. doi:10.1006/abbi.1994.1424.
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. doi:10.1182/blood.V84.2.474.474.
Shimomura T, Kondo J, Ochiai M, Naka D, Miyazawa K, Morimoto Y, Kitamura N (1993). "Activation of the zymogen of hepatocyte growth factor activator by thrombin". J. Biol. Chem. 268 (30): 22927–32. PMID 8226803. doi:10.1016/S0021-9258(18)41615-8.
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. PMID 8280154. doi:10.1006/bbrc.1993.2628.
Petersen LC, Sprecher CA, Foster DC, Blumberg H, Hamamoto T, Kisiel W (1996). "Inhibitory properties of a novel human Kunitz-type protease inhibitor homologous to tissue factor pathway inhibitor". Biochemistry 35 (1): 266–72. PMID 8555184. doi:10.1021/bi951501d.
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. PMID 8761966. doi:10.1016/S0143-4004(96)90042-9.
Durham SK, Suwanichkul A, Hayes JD, Herington AC, Powell DR, Campbell PG (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. PMID 10226805. doi:10.1055/s-2007-978722.
Renné T, Dedio J, Meijers JC, Chung D, Müller-Esterl W (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. PMID 10464316. doi:10.1074/jbc.274.36.25777.
Hermann A, Arnhold M, Kresse H, Neth P, Fink E (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. PMID 10543447. doi:10.1515/BC.1999.136.
Cerf M, Raidoo D, Fink E, Fritz H, Bhoola K (2000). "Plasma kallikrein localisation in human blood vessels". Immunopharmacology 44 (1–2): 75–80. PMID 10604527. doi:10.1016/S0162-3109(99)00112-5.

Outros artigos[editar | editar a fonte]

Calicreína, un grupo de encimas que cortan enlaces peptídicos nas proteínas

Ligazóns externas[editar | editar a fonte]

Plasma kallikrein Medical Subject Headings (MeSH) na Biblioteca Nacional de Medicina dos EUA.

[pmid9535413-1] Yu H, Bowden DW, Spray BJ, Rich SS, Freedman BI (abril de 1998). "Identification of human plasma kallikrein gene polymorphisms and evaluation of their role in end-stage renal disease". Hypertension 31 (4): 906–11. PMID 9535413. doi:10.1161/01.hyp.31.4.906.

[pmid3521732-2] Chung DW, Fujikawa K, McMullen BA, Davie EW (agosto de 1986). "Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats". Biochemistry 25 (9): 2410–7. PMID 3521732. doi:10.1021/bi00357a017.

[3] Heimark RL, Davie EW (1981). "Bovine and human plasma prekallikrein". Methods in Enzymology. 80 Pt C: 157–72. PMID 6918767. doi:10.1016/s0076-6879(81)80016-x.

[4] McRae BJ, Kurachi K, Heimark RL, Fujikawa K, Davie EW, Powers JC (decembro de 1981). "Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates". Biochemistry 20 (25): 7196–206. PMID 6976185. doi:10.1021/bi00528a022.

[5] Silverberg M, Kaplan AP (1988). "Prekallikrein". Methods in Enzymology 163: 85–95. ISBN 9780121820640. PMID 3237096. doi:10.1016/0076-6879(88)63010-2.

[6] Seidah NG, Ladenheim R, Mbikay M, Hamelin J, Lutfalla G, Rougeon F, Lazure C, Chrétien M (outubro de 1989). "The cDNA structure of rat plasma kallikrein". DNA 8 (8): 563–74. PMID 2598771. doi:10.1089/dna.1989.8.563.

[7] Tsuda Y, Teno N, Okada Y, Wanaka K, Bohgaki M, Hijikata-Okunomiya A, Okamoto U, Naito T, Okamoto S (novembro de 1989). "Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein". Chemical & Pharmaceutical Bulletin 37 (11): 3108–11. PMID 2534361. doi:10.1248/cpb.37.3108.

[entrez-8] "Entrez Gene: KLKB1 kallikrein B, plasma (Fletcher factor) 1".

[pmid291905-9] Thompson RE, Mandle R, Kaplan AP (outubro de 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. 76 (10): 4862–6. Bibcode:1979PNAS...76.4862T. PMC 413037. PMID 291905. doi:10.1073/pnas.76.10.4862.

[pmid7944388-10] Page JD, You JL, Harris RB, Colman RW (outubro de 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. PMID 7944388. doi:10.1006/abbi.1994.1424.

[pmid7686159-11] Herwald H, Jahnen-Dechent W, Alla SA, Hock J, Bouma BN, Müller-Esterl W (xullo de 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. doi:10.1016/S0021-9258(19)85270-5.

[pmid10464316-12] Renné T, Dedio J, Meijers JC, Chung D, Müller-Esterl W (setembro de 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. PMID 10464316. doi:10.1074/jbc.274.36.25777.

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