Rabbit collagenase. Immunological identity of the enzymes released from cells and tissues in normal and pathological conditions

Werb, Zena; Reynolds, John J.

doi:10.1042/bj1510665

Cited by 10 publications

(3 citation statements)

References 28 publications

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“…It has also been suggested that fibroblasts may be involved in the resorption of cartilage collagen that occurs in association with granulation tissue (pannus) formation during experimental arthritis in rats (Cullen, 1972). Fibroblasts isolated from synovium of rabbits with experimental arthritis have been shown to produce a collagenase identical to the collagenase produced by normal rabbit fibroblasts (Werb and Reynolds, 1975). Fibroblasts and lymphocytes are the predominating cells in chronic arthritis induced in the rabbit by injecting a cell-free extract of Group A Streptococci (Stein et a/., 1973).…”

Section: Discussionmentioning

confidence: 99%

The possible role of the fibroblast in granuloma‐induced bone resorption in the rat

Deporter

1979

The Journal of Pathology

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Granulomas were produced over the calvaria of rats by injection of a mixture of turpentine and peanut oil. The granulomas induced localised areas of bone resorption and these resorptive lesions were examined at the fine structural level. A close association was found between osteoclasts and fibroblasts at resorbing surfaces. Furthermore, fibroblasts but not osteoclasts were observed to engulf and phagocytose bone collagen fibrils. It is suggested that the fibroblast either alone or in collaboration with the osteoclast is involved in the destruction of bone collagen during chronic inflammatory disorder of bone.

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Section: Discussionmentioning

confidence: 99%

The possible role of the fibroblast in granuloma‐induced bone resorption in the rat

Deporter

1979

The Journal of Pathology

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“…In previous attempts to localize interstitial collagenase associated with neoplasms, antisera had been raised against enzyme from non-neoplastic, mesenchymal cells rather than from neoplastic cells (5,6,(12)(13)(14). These antisera crossreacted with collagenase from tumour explants (15) and tumour extracts (5) but in neither ease was the cellular source of the collagenase clear, as it may have originated from surrounding host fibroblasts rather than from neoplastic cells.…”

Section: Introductionmentioning

confidence: 99%

“…These antisera crossreacted with collagenase from tumour explants (15) and tumour extracts (5) but in neither ease was the cellular source of the collagenase clear, as it may have originated from surrounding host fibroblasts rather than from neoplastic cells.…”

Section: Introductionmentioning

confidence: 99%

Immunolocalization of collagenase in neoplastic epithelial cells

1989

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SummaryThe distribution of interstitial collagenase in a ral mammary carcinoma model system has been studied by immunocytochemistry. Rabbit antibodies were raised against collagenase from neoplastic epithelial cells which were derived from an anapiastic. invasive, ral mammary carcinoma (BCl). Specificity of the antibodies was determined by Western blot analysis which showed reactivity with the inactive procollagenase from conditioned culture medium of BCl cells as well as with purified, active BCl collagenase. Anti-BCl collagenase antibodies did not recognize BCl collagenase entrapped by the inhibitor, rat a-2-macroglobulin (a2M). or collagenase derived from TPA-stimulated human fibroblasts. Anti-human fibroblast eollagenase antibodies did not recognize BCl collagenase. suggesting that the human-mesenchymal and ral-epithelial enzymes are immunologieally distinct molecules.Collagenase was immunolocalized intracellularly in BC1 cells cultured in the presence of monensin. Neither BCl collagenase, a2M nor enzyme-inhibitor complexes were demonstrated in or around invading tumours by immunostaining of tissue sections of rat mammary carcinomas.

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Septic arthritis

Schurman

1990

Arthritis & Rheumatism

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We report herein that cartilage proteolytic activity increased in bovine and rabbit articular cartilage after treatment with a purified staphylococcal culture medium or intraarticular infection with Staphylococcus aureus. Staphylococcal culture medium increased the release of gelatinolytic, collagenolytic, and caseinolytic activity into the medium of isolated chondrocytes or cartilage organ culture. The proteolytic activities were determined in assays using radiolabeled substrate and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Staphylococcal culture medium was proteolytically inactive by both assay techniques. RNA synthesis of isolated chondrocytes was unaffected by staphylococcal culture medium, whereas overall protein synthesis was inhibited by 84%. An analysis of extracts of Staphylococcus aureus-infected rabbit knee cartilage by substrate gels showed increased gelatinolytic and caseinolytic activity compared with extracts of uninfected knee cartilage. Our data suggest that the rapid loss of proteoglycan and persistent degradation of cartilage in staphylococcal septic arthritis is due to the production and activation of chondrocyte proteases.Septic arthritis continues to be a serious problem in urban medical centers (I ,2) and is recognized as a complicating factor in rheumatoid arthritis and other chronic arthritic conditions (3). Although most joint infections are acquired hematogenously, direct infection can result from deep wounds, surgical procedures, and intraarticular joint injections (2). In nongonococcal septic arthritis, Staphylococcus aureus is the organism most frequently found by culture (64%); in 25% of the patients positive for S aureus, the bacteria are methicillin resistant (1). Sterile "postinfectious" arthritis provides the potential for residual joint damage (43).In an animal model of staphylococcal infectious arthritis, cartilage degradation was shown to continue, despite early antibiotic treatment (5). Infection of rabbit knees with S aureus was shown to cause a rapid loss of cartilage proteoglycan (PG) (a), with a loss of as much as 40% of the total PG from the cartilage matrix within the first 48 hours after infection (8). Loss of collagen becomes significant between the second and third weeks after infection (8). Antibiotic treatment begun within 24 hours of infection decreases collagen loss but fails to prevent loss of PG from the matrix (5).In vitro, S aureus or S aureus-conditioned culture medium induces cartilage degradation in viable cartilage explants (9). Cartilage degradation is marked by a loss of partially degraded PG, which is consistent with increased proteolytic activity. PG release from cartilage by S aureus or staphylococcal culture medium is significantly reduced by freeze-thawing cartilage (9). Killed bacteria have no effect on cartilage degradation. Staphylococcus-induced PG release is dependent on chondrocyte metabolism and can be blocked by inhibitors of RNA and protein synthesis, i.e., actinomycin D and cycloheximide, respectively

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Rabbit collagenase. Immunological identity of the enzymes released from cells and tissues in normal and pathological conditions

Cited by 10 publications

References 28 publications

The possible role of the fibroblast in granuloma‐induced bone resorption in the rat

The possible role of the fibroblast in granuloma‐induced bone resorption in the rat

Immunolocalization of collagenase in neoplastic epithelial cells

Septic arthritis

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