Hepatocyte growth factor: Difference between revisions
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<StructureSection load='1shy' size='350' side='right' caption='Structure of human HGF β chain (grey) complex with HGF receptor Sema and ψ domains (green) (PDB entry [[1shy]])' scene=''> | <StructureSection load='1shy' size='350' side='right' caption='Structure of human HGF β chain (grey) complex with HGF receptor Sema and ψ domains (green) (PDB entry [[1shy]])' scene=''> | ||
== Function == | == Function == | ||
'''Hepatocyte growth factor''' (HGF) regulates cell growth, motility and morphogenesis. HGF binds to proto-oncogene c-Met receptor and activates a tyrosine kinase signaling cascade. HGF precursor is cleaved by serine protease to α (69 kD) and β (34 kD) chains which form a disulfide bond to produce the active heterodimer<ref>PMID:1838014</ref>. HGF α chain contains an N-terminal hairpin and 4 kringle domains. The kringle domain participates in protein-protein interaction and its structure is of a large loop which is stabilized by 3 Cys-Cys bonds. '''HGF NK1''' - a natural splice variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF<ref>PMID:9488442</ref>. '''HGF NK2''' variant is comprised of residues 28-289 containing the N-terminus and the first 2 kringle domains of HGF. | '''Hepatocyte growth factor''' (HGF) regulates cell growth, motility and morphogenesis. HGF binds to proto-oncogene c-Met receptor and activates a tyrosine kinase signaling cascade. HGF precursor is cleaved by serine protease to α (69 kD) and β (34 kD) chains which form a disulfide bond to produce the active heterodimer<ref>PMID:1838014</ref>. HGF α chain contains an N-terminal hairpin and 4 kringle domains. The kringle domain participates in protein-protein interaction and its structure is of a large loop which is stabilized by 3 Cys-Cys bonds. HGF β chain is catalytically inactive serine protease-like. '''HGF NK1''' - a natural splice variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF<ref>PMID:9488442</ref>. '''HGF NK2''' variant is comprised of residues 28-289 containing the N-terminus and the first 2 kringle domains of HGF. | ||
== Relevance == | == Relevance == | ||
Revision as of 12:44, 21 March 2016
FunctionHepatocyte growth factor (HGF) regulates cell growth, motility and morphogenesis. HGF binds to proto-oncogene c-Met receptor and activates a tyrosine kinase signaling cascade. HGF precursor is cleaved by serine protease to α (69 kD) and β (34 kD) chains which form a disulfide bond to produce the active heterodimer[1]. HGF α chain contains an N-terminal hairpin and 4 kringle domains. The kringle domain participates in protein-protein interaction and its structure is of a large loop which is stabilized by 3 Cys-Cys bonds. HGF β chain is catalytically inactive serine protease-like. HGF NK1 - a natural splice variant is comprised of residues 28-210 containing the N-terminus and the first kringle domain of HGF[2]. HGF NK2 variant is comprised of residues 28-289 containing the N-terminus and the first 2 kringle domains of HGF. RelevanceHigh levels of HGF are associated with liver diseases[3], lung diseases, acute cardiac infraction, vascular diseases, renal failure, neurologic diseases like Alzheimer Disease, pancreatic diseases, several types of cancer and diabetes type II[4][5]. HGF administration can reverse liver chirrosis[6]. |
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3D structures of hepatocyte growth factor3D structures of hepatocyte growth factor
Updated on 21-March-2016
ReferencesReferences
- ↑ Nakamura T. Structure and function of hepatocyte growth factor. Prog Growth Factor Res. 1991;3(1):67-85. PMID:1838014
- ↑ Jakubczak JL, LaRochelle WJ, Merlino G. NK1, a natural splice variant of hepatocyte growth factor/scatter factor, is a partial agonist in vivo. Mol Cell Biol. 1998 Mar;18(3):1275-83. PMID:9488442
- ↑ Shiota G, Okano J, Kawasaki H, Kawamoto T, Nakamura T. Serum hepatocyte growth factor levels in liver diseases: clinical implications. Hepatology. 1995 Jan;21(1):106-12. PMID:7806142
- ↑ Anan F, Masaki T, Yonemochi H, Takahashi N, Nakagawa M, Eshima N, Saikawa T, Yoshimatsu H. Hepatocyte growth factor levels are associated with the results of 123I-metaiodobenzylguanidine myocardial scintigraphy in patients with type 2 diabetes mellitus. Metabolism. 2009 Feb;58(2):167-73. doi: 10.1016/j.metabol.2008.09.009. PMID:19154948 doi:http://dx.doi.org/10.1016/j.metabol.2008.09.009
- ↑ Shiota G, Okano J, Kawasaki H, Kawamoto T, Nakamura T. Serum hepatocyte growth factor levels in liver diseases: clinical implications. Hepatology. 1995 Jan;21(1):106-12. PMID:7806142
- ↑ Funakoshi H, Nakamura T. Hepatocyte growth factor: from diagnosis to clinical applications. Clin Chim Acta. 2003 Jan;327(1-2):1-23. PMID:12482615