sodium-dodecyl-sulfate and Tongue-Neoplasms

sodium-dodecyl-sulfate has been researched along with Tongue-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for sodium-dodecyl-sulfate and Tongue-Neoplasms

Article	Year
Production of matrix metalloproteinase 2 (gelatinase/type IV collagenase) and 3 (stromelysin) by cultured oral squamous cell carcinoma. Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology, 1992, Volume: 21, Issue:5 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. Topics: Adult; Aged; Carcinoma, Squamous Cell; Collagenases; Electrophoresis, Polyacrylamide Gel; Fluorescent Antibody Technique; Humans; Immunoblotting; Male; Matrix Metalloproteinase 3; Matrix Metalloproteinase 9; Metalloendopeptidases; Neoplasm Proteins; Sodium Dodecyl Sulfate; Tongue Neoplasms; Tumor Cells, Cultured	1992

Article

Year

Production of matrix metalloproteinase 2 (gelatinase/type IV collagenase) and 3 (stromelysin) by cultured oral squamous cell carcinoma.

Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology, 1992, Volume: 21, Issue:5

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.

Topics: Adult; Aged; Carcinoma, Squamous Cell; Collagenases; Electrophoresis, Polyacrylamide Gel; Fluorescent Antibody Technique; Humans; Immunoblotting; Male; Matrix Metalloproteinase 3; Matrix Metalloproteinase 9; Metalloendopeptidases; Neoplasm Proteins; Sodium Dodecyl Sulfate; Tongue Neoplasms; Tumor Cells, Cultured

1992