A fibroblast elongation factor purified from colon carcinoma cells shares sequence identity with TIMP-1.
We have previously reported that human colon cancer cells secrete a factor(s) which induces elongation of colon fibroblasts in vitro. Isolation of this factor led to the identification of a 55kD protein with fibroblast stretching activity. Two internal amino acid sequences identified in this protein (YEI; GFQALGDAADI) share complete homology with tissue inhibitor of metalloproteinase (TIMP-1).
Agrez
M V
MV
Faculty of Medicine, University of Newcastle, N.S.W., Australia.
Meldrum
C J
CJ
Sim
A T
AT
Aebersold
R H
RH
Clark
I M
IM
Cawston
T E
TE
Burns
G F
GF
D000595:Amino Acid Sequence; D002460:Cell Line; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003106:Colon / Q000166:cytology / Q000187:drug effects; D003110:Colonic Neoplasms / Q000737:chemistry*; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D006801:Humans; D061965:Matrix Metalloproteinase Inhibitors; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D019714:Tissue Inhibitor of Metalloproteinases; D014407:Tumor Cells, Cultured
D006023:Glycoproteins; D061965:Matrix Metalloproteinase Inhibitors; D009363:Neoplasm Proteins; D019714:Tissue Inhibitor of Metalloproteinases