Collagenase activity in cultures of rat prostate carcinoma

Huang, Chih-Cheng; Wu, Chen-Hsiung; Abramson, Maxwell

doi:10.1016/0005-2744(79)90209-2

Cited by 18 publications

(2 citation statements)

References 17 publications

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“…For example, the molecular weight of rheumatoid synovial collagenase is 33,000, skin collagenase 63,000 (66,67,68) and bovine gingival collagenase 80,000 (69). Tumor-derived collagenases fall into the same range of molecular weights; i.e., rabbit V2 carcinoma collagenase 33-35,000 (55) and rat prostate carcinoma eollagenase 71,000 (70). In the studies of Woolley et al (25), collagenase obtained from human carcinomas and melanomas was shown to immunologically cross react with antibodies to collagenase produced by rheumatoid synovium.…”

Section: Tumor Cell Collagenases Which Degrade Types I Ii and Iii Comentioning

confidence: 99%

“…All of these types of host cells are capable of producing collagenases. Cultured tumor cell lines free of contaminating host cells such as sarcomas, carcinomas and melanomas have been shown to produce collagenases (49,53,70). Even though tumor cells have the potential to produce collagenases in vitro it does not necessarily mean that tumor cells can produce collagenases in vivo.…”

Section: Cell Source Of Collagenasementioning

confidence: 99%

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Role of collagenases in tumor cell invasion

1982

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Collagenases are a family of metalloproteinases which may play a role in facilitating tumor cell invasion of the extracellular matrix. Tumor cells traverse two types of extracellular matrix: basement membranes and interstitial stroma, at multiple stages of the metastatic process. The matrix is a dense meshwork of collagen, proteoglycans, elastin and glycoproteins. Normally the matrix does not contain open spaces large enough for cell movement. Therefore numerous investigators have postulated that collagenolytic proteases, secreted by tumor cells or associated host cells, breakdown the extracellular matrix during tumor cell invasion. A large number of animal and human tumors have been shown to contain collagenase at a higher level than corresponding benign tissues. Separate collagenolytic metalloproteinases have been identified which degrade specific types of collagen. A basement membrane collagenolytic protease was shown to be elevated in a series of metastatic murine tumor cells. Immunologic studies using antibodies specific for collagenase have demonstrated that in vivo, tumor cells can produce collagenase. Therefore identification of collagenase in cultured lines of tumor cells is not an artifact of in vitro cultivation. In some cases, tumor cells may induce host cells to produce collagenase. The best evidence to date that collagenases actually play a role in invasion is derived from experiments in which natural collagenase inhibitors block tumor cell invasion of extracellular matrix in vitro.

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Section: Tumor Cell Collagenases Which Degrade Types I Ii and Iii Comentioning

confidence: 99%

Section: Cell Source Of Collagenasementioning

confidence: 99%

Role of collagenases in tumor cell invasion

1982

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A fibrosarcoma model derived from mouse embryo cells: Growth properties and secretion of collagenase and metalloproteinase inhibitor (TIMP) by tumour cell lines

Hicks

Ward

Reynolds

1984

Intl Journal of Cancer

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A new murine fibrosarcoma model has been developed in which it is possible to compare in vitro the behaviour of tumour cells with that of normal parental cells from which the tumour was originally derived by spontaneous transformation in vitro. Tumour cell lines were obtained which showed differing capacities for localized invasion of the skin following subcutaneous injection: these were categorized as either highly invasive or poorly invasive and were compared with the normal cells for (I) their respective saturation densities when grown on plastic, (2) their ability to grow in agar, and (3) their secretions of the metalloenzyme collagenase and the specific inhibitor of metalloproteinases (TIMP). Although increased in vitro saturation density showed some correlation with increased invasiveness in vivo, the most striking correlation was the 10- to 20-fold reduction in TIMP secretion by tumour cells of high invasive potential compared with normal cells or tumour cells with low invasive potential. No collagenase secretion by tumour cells was ever detected. It is proposed that local TIMP levels may play a crucial in the control of tumour invasion in vivo.

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Characterization of Gelatin‐Degrading Metalloproteinase Activities of the Dunning Rat Prostate Tumor Grown in Nude Mice

et al. 1991

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Proteinase activities in the Dunning R-3327 prostatic tumor grown in nude mice and the dorsal lobe of the normal Copenhagen rat prostate were characterized using gelatin-containing SDS-polyacrylamide gel electrophoresis. Calcium-stimulated activities of approximately 33, 42, 64, 71, 76, 85, 98, 115, and 120 Kd as well as a 91 Kd calcium-independent proteinase were detected in the tumor, whereas the dorsal prostate showed calcium-dependent activities of approximately 62 and 80 Kd and a calcium-independent activity much greater than 120 Kd. The zymographic calcium-dependent proteinase patterns in the other rat prostatic lobes (a 62 Kd proteinase in the anterior lobe; 59, 62, and 67 Kd forms in the ventral lobe; and 52, 62, and 72 Kd activities in the lateral lobe) were distinctive from that of the tumor and of the dorsal lobe. The calcium-dependent and -independent proteinases of the tumor were active over a broad range of pH values with optimal activity near pH 8.0-8.4. The calcium-dependent activities were inhibited by EDTA and EGTA. Barium and strontium could partially substitute for calcium. The calcium-independent activities were not affected by these chelators nor by the proteinase inhibitors benzamidine, epsilon-aminocaproic acid, tranexamic acid, hydrocinnamic acid, or iodoacetate. Similarly, the metalloproteinase activities were not affected by the latter inhibitors. There was little change in the predominant molecular forms (64, 71, and 76 Kd) of proteinase following castration of tumor-bearing nude mice; however, the 98 Kd calcium-dependent activity decreased and the 91 Kd calcium-independent activity increased as a result of this treatment.

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Collagenase activity in cultures of rat prostate carcinoma

Cited by 18 publications

References 17 publications

Role of collagenases in tumor cell invasion

Role of collagenases in tumor cell invasion

A fibrosarcoma model derived from mouse embryo cells: Growth properties and secretion of collagenase and metalloproteinase inhibitor (TIMP) by tumour cell lines

Characterization of Gelatin‐Degrading Metalloproteinase Activities of the Dunning Rat Prostate Tumor Grown in Nude Mice

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