NDLI: A functional domain in the heavy chain of scatter factor/hepatocyte growth factor binds the c-Met receptor and induces cell dissociation but not mitogenesis.

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A functional domain in the heavy chain of scatter factor/hepatocyte growth factor binds the c-Met receptor and induces cell dissociation but not mitogenesis.

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A functional domain in the heavy chain of scatter factor/hepatocyte growth factor binds the c-Met receptor and induces cell dissociation but not mitogenesis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Birchmeier, W. Hartmann, G. Weidner, K. M. Comoglio, P. M. Naldini, L. Sachs, M. Vigna, E.
Description	Author Affiliation: Hartmann G ( Institut für Zellbiologie (Tumorforschung), University of Essen Medical School, Federal Republic of Germany.);
Abstract	We recently found that scatter factor (SF), a cell motility factor with a multimodular structure, is identical to hepatocyte growth factor (HGF), a potent mitogen of various cell types. SF/HGF is the ligand of the c-Met receptor tyrosine kinase. Here we used transient expression of naturally occurring and in vitro mutagenized cDNAs of SF/HGF to delineate the protein domains necessary for biological activity and binding to the c-Met receptor. (i) A single-chain SF/HGF resulting from the destruction of the protease cleavage site between heavy and light chain (Arg-494--> Gln) was largely inactive, indicating that proteolytic cleavage is essential for acquisition of the biologically active conformation. (ii) A SF/HGF splice variant encoding a protein with a 5-amino acid deletion in the first kringle domain was as highly active as the wild-type molecule. (iii) The separately expressed light chain (with serine protease homology) was inactive in all assays tested. (iv) The separate heavy chain as well as a naturally occurring splice variant consisting of the N terminus and the first two kringle domains bound the c-Met receptor, stimulated tyrosine auto-phosphorylation, and induced scattering of epithelial cells but not mitogenesis. These data indicate that a functional domain in the N terminus/first two kringle regions of SF/HGF is sufficient for binding to the Met receptor and that this leads to the activation of the downstream signal cascade involved in the motility response. However, the complete SF/HGF protein seems to be required for mitogenic activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hepatocyte Growth Factor Metabolism Proto-Oncogene Proteins Receptors, Cell Surface Amino Acid Sequence Animals Cell Division Cell Movement Cells, Cultured DNA Genetics DNA Mutational Analysis In Vitro Techniques Molecular Sequence Data Mutagenesis, Site-Directed Phosphotyrosine Protein-Tyrosine Kinases Proto-Oncogene Proteins C-met Recombinant Proteins Structure-Activity Relationship Tyrosine Analogs & Derivatives Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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