Kininogen 1

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Kininogen 1
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols KNG1 ; BDK; BK; KNG
External IDs OMIM612358 MGI3027157 HomoloGene88343 GeneCards: KNG1 Gene
RNA expression pattern
PBB GE KNG1 206054 at tn.png
PBB GE KNG1 217512 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3827 16644
Ensembl ENSG00000113889 ENSMUSG00000022875
UniProt P01042 O08677
RefSeq (mRNA) NM_000893 NM_001102411
RefSeq (protein) NP_000884 NP_001095881
Location (UCSC) Chr 3:
186.44 – 186.46 Mb
Chr 16:
23.06 – 23.08 Mb
PubMed search [1] [2]

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.[1]

Function[edit]

The KNG1 gene uses alternative splicing to generate two different proteins- high-molecular-weight kininogen (HMWK) and low-molecular-weight kininogen (LMWK). HMWK is essential for blood coagulation and assembly of the kallikrein-kinin system. Also, bradykinin, a peptide causing numerous physiological effects, is released from HMWK. In contrast to HMWK, LMWK is not involved in blood coagulation. Three transcript variants encoding different isoforms have been found for this gene.[1]

Kininogen-1 is a constituent of the blood coagulation system as well as the kinin-kallikrein system.

See also[edit]

References[edit]

Further reading[edit]

  • Iarovaia GA (2001). "[Kallikrein-kinin system: novel facts and concepts (literature review)]". Vopr. Med. Khim. 47 (1): 20–42. PMID 11385996. 
  • Matthews KW, Mueller-Ortiz SL, Wetsel RA (2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Mol. Immunol. 40 (11): 785–93. doi:10.1016/j.molimm.2003.10.002. PMID 14687935. 
  • Scharfstein J, Schmitz V, Svensjö E et al. (2007). "Kininogens coordinate adaptive immunity through the proteolytic release of bradykinin, an endogenous danger signal driving dendritic cell maturation". Scand. J. Immunol. 66 (2-3): 128–36. doi:10.1111/j.1365-3083.2007.01983.x. PMID 17635790. 
  • 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. 
  • Kerbiriou DM, Griffin JH (1980). "Human high molecular weight kininogen. Studies of structure-function relationships and of proteolysis of the molecule occurring during contact activation of plasma". J. Biol. Chem. 254 (23): 12020–7. PMID 500690. 
  • Colman RW, Bagdasarian A, Talamo RC et al. (1976). "Williams trait. Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways". J. Clin. Invest. 56 (6): 1650–62. doi:10.1172/JCI108247. PMC 333144. PMID 1202089. 
  • Gailani D, Broze GJ (1991). "Factor XI activation in a revised model of blood coagulation". Science 253 (5022): 909–12. doi:10.1126/science.1652157. PMID 1652157. 
  • Cheung PP, Cannizzaro LA, Colman RW (1992). "Chromosomal mapping of human kininogen gene (KNG) to 3q26----qter". Cytogenet. Cell Genet. 59 (1): 24–6. doi:10.1159/000133192. PMID 1733668. 
  • Fong D, Smith DI, Hsieh WT (1991). "The human kininogen gene (KNG) mapped to chromosome 3q26-qter by analysis of somatic cell hybrids using the polymerase chain reaction". Hum. Genet. 87 (2): 189–92. doi:10.1007/BF00204179. PMID 2066106. 
  • Schmaier AH, Kuo A, Lundberg D et al. (1988). "The expression of high molecular weight kininogen on human umbilical vein endothelial cells". J. Biol. Chem. 263 (31): 16327–33. PMID 2460446. 
  • Takagaki Y, Kitamura N, Nakanishi S (1985). "Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens". J. Biol. Chem. 260 (14): 8601–9. PMID 2989293. 
  • Kitamura N, Kitagawa H, Fukushima D et al. (1985). "Structural organization of the human kininogen gene and a model for its evolution". J. Biol. Chem. 260 (14): 8610–7. PMID 2989294. 
  • Ishiguro H, Higashiyama S, Namikawa C et al. (1987). "Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations". Biochemistry 26 (10): 2863–70. doi:10.1021/bi00384a030. PMID 3038169. 
  • Vogel R, Assfalg-Machleidt I, Esterl A et al. (1988). "Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions". J. Biol. Chem. 263 (25): 12661–8. PMID 3045123. 
  • Maeda H, Matsumura Y, Kato H (1988). "Purification and identification of [hydroxyprolyl3]bradykinin in ascitic fluid from a patient with gastric cancer". J. Biol. Chem. 263 (31): 16051–4. PMID 3182782. 
  • Kato H, Matsumura Y, Maeda H (1988). "Isolation and identification of hydroxyproline analogues of bradykinin in human urine". FEBS Lett. 232 (1): 252–4. doi:10.1016/0014-5793(88)80427-7. PMID 3366244. 
  • Kellermann J, Lottspeich F, Henschen A, Müller-Esterl W (1986). "Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication". Eur. J. Biochem. 154 (2): 471–8. doi:10.1111/j.1432-1033.1986.tb09421.x. PMID 3484703. 
  • Kellermann J, Thelen C, Lottspeich F et al. (1988). "Arrangement of the disulphide bridges in human low-Mr kininogen". Biochem. J. 247 (1): 15–21. PMC 1148362. PMID 3689342. 
  • Warn-Cramer BJ, Bajaj SP (1986). "Stoichiometry of binding of high molecular weight kininogen to factor XI/XIa". Biochem. Biophys. Res. Commun. 133 (2): 417–22. doi:10.1016/0006-291X(85)90922-2. PMID 3936495. 
  • Lottspeich F, Kellermann J, Henschen A et al. (1985). "The amino acid sequence of the light chain of human high-molecular-mass kininogen". Eur. J. Biochem. 152 (2): 307–14. doi:10.1111/j.1432-1033.1985.tb09199.x. PMID 4054110. 

External links[edit]