PMID- 7527397
OWN - NLM
STAT- MEDLINE
DCOM- 19950112
LR  - 20220310
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 269
IP  - 50
DP  - 1994 Dec 16
TI  - Hepatocyte growth factor/scatter factor induces tyrosine phosphorylation of focal 
      adhesion kinase (p125FAK) and promotes migration and invasion by oral squamous 
      cell carcinoma cells.
PG  - 31807-13
AB  - Fibroblasts or their conditioned medium stimulated invasion by squamous cell 
      carcinoma cells. The fibroblast-derived activity responsible for increased 
      invasion is the hepatocyte growth factor/scatter factor (HGF/SF), a ligand for 
      the c-Met receptor. HGF/SF stimulated migration of the cells on various 
      extracellular matrix substrates but did not alter their adhesion efficiency nor 
      integrin expression. HGF/SF stimulated motility in a two step process: initially 
      cells spread rapidly and formed focal adhesions, and then they disassembled these 
      condensations, which was followed by increased cell locomotion. The focal 
      adhesions contained vinculin, p125FAK, beta 1 integrin, and phosphotyrosine. 
      Within minutes after exposure of cells to HGF/SF, proteins of 125 and 145 kDa 
      showed elevated tyrosine phosphorylation and were identified as p125FAK and 
      c-Met, respectively. Gradual loss of tyrosine phosphorylation coincided with 
      disruption of focal adhesions and conversion to a motile phenotype. 
      HGF/SF-mediated tyrosine phosphorylation of p125FAK was inhibited by the tyrosine 
      kinase inhibitor, herbimycin A, which also blocked spreading and the migratory 
      response. These results indicate that fibroblast-derived HGF/SF triggers 
      migration through the initial recruiting of integrins, cytoskeletal proteins, and 
      p125FAK into focal adhesions that is dependent on tyrosine kinase activity.
FAU - Matsumoto, K
AU  - Matsumoto K
AD  - Department of Anatomy, University of California, San Francisco 94143.
FAU - Matsumoto, K
AU  - Matsumoto K
FAU - Nakamura, T
AU  - Nakamura T
FAU - Kramer, R H
AU  - Kramer RH
LA  - eng
GR  - CA51884/CA/NCI NIH HHS/United States
GR  - DE10306/DE/NIDCR NIH HHS/United States
GR  - DE10356/DE/NIDCR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Benzoquinones)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Integrins)
RN  - 0 (Lactams, Macrocyclic)
RN  - 0 (Quinones)
RN  - 1W306TDA6S (Rifabutin)
RN  - 21820-51-9 (Phosphotyrosine)
RN  - 42HK56048U (Tyrosine)
RN  - 67256-21-7 (Hepatocyte Growth Factor)
RN  - 70563-58-5 (herbimycin)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.1 (Proto-Oncogene Proteins c-met)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Focal Adhesion Kinase 1)
RN  - EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (PTK2 protein, human)
SB  - IM
MH  - Benzoquinones
MH  - Carcinoma, Squamous Cell/*pathology
MH  - Cell Adhesion/drug effects
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Movement/*drug effects
MH  - Focal Adhesion Kinase 1
MH  - Focal Adhesion Protein-Tyrosine Kinases
MH  - Hepatocyte Growth Factor/*pharmacology
MH  - Humans
MH  - In Vitro Techniques
MH  - Integrins/metabolism
MH  - Lactams, Macrocyclic
MH  - Mouth Neoplasms/*pathology
MH  - Neoplasm Invasiveness
MH  - Phosphotyrosine
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - Proto-Oncogene Proteins c-met
MH  - Quinones/pharmacology
MH  - Receptor Protein-Tyrosine Kinases/metabolism
MH  - Rifabutin/analogs & derivatives
MH  - Tumor Cells, Cultured
MH  - Tyrosine/*analogs & derivatives/metabolism
EDAT- 1994/12/16 00:00
MHDA- 1994/12/16 00:01
CRDT- 1994/12/16 00:00
PHST- 1994/12/16 00:00 [pubmed]
PHST- 1994/12/16 00:01 [medline]
PHST- 1994/12/16 00:00 [entrez]
AID - S0021-9258(18)31767-8 [pii]
PST - ppublish
SO  - J Biol Chem. 1994 Dec 16;269(50):31807-13.