Gelatinolytic metalloproteinase secretion patterns in ocular melanoma.
Fifteen posterior uveal melanoma cell lines were analyzed qualitatively for gelatinolytic and caseinolytic proteinase activity after one to five in vitro passages. All 15 cell lines secreted a gelatinolytic metalloproteinase, with an apparent molecular weight of 72 kD, into protein-free culture media; nine of these secreted an additional gelatinolytic metalloproteinase with an apparent molecular weight of 92 kD. Neither species had the ability to degrade casein. This approach may provide insight into the mechanisms of tumor metastasis in uveal melanoma.
Cottam
D W
DW
Department of Experimental and Clinical Microbiology, University of Sheffield Institute for Cancer Studies, University of Sheffield Medical School, United Kingdom.
Rennie
I G
IG
Woods
K
K
Parsons
M A
MA
Bunning
R A
RA
Rees
R C
RC
D000368:Aged; D000369:Aged, 80 and over; D003470:Culture Media; D005260:Female; D018093:Gelatinases; D006801:Humans; D008297:Male; D008545:Melanoma / Q000201:enzymology*; D008666:Metalloendopeptidases / Q000378:metabolism*; D008875:Middle Aged; D008970:Molecular Weight; D010434:Pepsin A / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014604:Uveal Neoplasms / Q000201:enzymology*
D003470:Culture Media; D010434:Pepsin A; D018093:Gelatinases; D008666:Metalloendopeptidases