Production of matrix metalloproteinase 2 (gelatinase/type IV collagenase) and 3 (stromelysin) by cultured oral squamous cell carcinoma.
Matrix metalloproteinases (MMPs) are believed to play an important role in tumor invasion and metastasis. MMPs have been identified as proforms of malignant tumor-associated enzymes, such as procollagenase (proMMP-1) of M(r) = 53,000, progelatinase (proMMP-2) of M(r) = 72,000, proMMP-9 of M(r) = 92,000, and prostromelysin (proMMP-3) of M(r) = 59,000. Here we report that two cell lines of squamous cell carcinoma (SCC9 and SCC25) produce at least two matrix metalloproteinases (MMPs) in zymogen form, which have been identified as proMMP-2 and 3 by indirect immunofluorescence technique, immunoblot analysis, and gelatin-substrate gel enzymography. Additionally, a 92-kDa gelatinolytic metalloproteinase (proMMP-9) was detected by gelatin-substrate gel enzymography. We propose that the ability of these tumor cells to secrete MMPs plays an important role in the malignant behavior of oral squamous cell carcinomas.
Kusukawa
J
J
Department of Pathology, Kurume University School of Medicine, Japan.
Sasaguri
Y
Y
Shima
I
I
Kameyama
T
T
Morimatsu
M
M
D000328:Adult; D000368:Aged; D002294:Carcinoma, Squamous Cell / Q000201:enzymology*; D017364:Collagenases / Q000032:analysis / Q000096:biosynthesis*; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D006801:Humans; D015151:Immunoblotting; D008297:Male; D019278:Matrix Metalloproteinase 3; D020780:Matrix Metalloproteinase 9; D008666:Metalloendopeptidases / Q000032:analysis / Q000096:biosynthesis*; D009363:Neoplasm Proteins / Q000032:analysis / Q000096:biosynthesis*; D012967:Sodium Dodecyl Sulfate; D014062:Tongue Neoplasms; D014407:Tumor Cells, Cultured
D009363:Neoplasm Proteins; D012967:Sodium Dodecyl Sulfate; D017364:Collagenases; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D020780:Matrix Metalloproteinase 9