Molecular cloning and characterization of cDNA encoding mouse hepatocyte growth factor.
A cDNA encoding mouse hepatocyte growth factor (HGF) has been cloned and completely sequenced by use of reverse transcriptase-polymerase chain reaction (RT-PCR) and subsequent cloning. Sequence analysis reveals that mouse HGF, similar to its human and rat counterparts, consists of 728 amino acids, and both the alpha- and beta-chains are encoded in a single open reading frame. Strong homology exists in the primary structure of HGF among the three species of mouse, rat and human (more than 90%), especially in Kringle 1 of the alpha chain which is assumed to be an essential domain for binding of HGF to its receptor, c-MET, a proto-oncogene product. Our results suggest the existence of evolutionary pressure to conserve the distinct structure, and presumably the biological functions, of HGF.
Liu
Y
Y
Department of Pathology, School of Medicine, University of Pittsburgh, PA 15261.
Michalopoulos
G K
GK
Zarnegar
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000096:biosynthesis* / Q000737:chemistry; D017228:Hepatocyte Growth Factor / Q000235:genetics*; D006801:Humans; D018082:Kringles; D051379:Mice; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016133:Polymerase Chain Reaction; D000090063:Proto-Oncogene Mas; D051381:Rats; D016415:Sequence Alignment
D018076:DNA, Complementary; C000715470:MAS1 protein, human; D000090063:Proto-Oncogene Mas; D017228:Hepatocyte Growth Factor