Solid-phase radioimmunoassay of rat skin collagenase comparative studies and in vivo measurement of the enzyme

Eisen, Arthur Z.; Nepute, James; Stricklin, George P.; Bauer, Eugene A.; Jeffrey, John J.

doi:10.1016/0005-2744(74)90520-8

Cited by 5 publications

(1 citation statement)

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“…(1971) also showed that isoenzymes of cathepsin D showed complete identity, and we do not rule out the possibility that there are isoenzyme forms of rabbit collagenase. The results of Bauer et al (1970) and Eisen et al (1974) with human and rat collagenases also point to the species differences rather than tissue differences, and it is noteworthy that although there is no immunological cross-reaction between collagenases from different species, they conserve such specialized enzymic activity (see Harris & Krane, 1974a,b,c). However, our antisera cannot give information on the chemical identity of the collagenase and only purification of the enzyme from different tissues will show if they have similar molecular weights.…”

Section: Discussionmentioning

confidence: 97%

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

Werb

Reynolds

1975

Biochemical Journal

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1. The immunological cross-reactivity between rabbit collagenases from a variety of normal and pathological sources was examined. The specific antibody raised against collagenase secreted from normal rabbit synovial fibroblasts gave reactions of complete identity with collagenases secreted from fibroblasts derived from rabbit skin, and from synovium from experimentally arthritic rabbits. 2. The rabbit fibroblast collagenase was immunologically identical with collagenases obtained from the organ culture medium of normal rabbit skin, synovium, ear fibrocartilage and subchondral bone. 3. Collagenases from the culture media of normal rabbit synovium and from hyperplastic synovium of rabbits made experimentally arthritic were identical. 4. The collagenase secreted from rabbit fibroblasts gave a reaction completely identical with that of a collagenase extracted directly from a rabbit carcinoma. 5. IgG (immunoglobulin G) from a specific antiserum to rabbit fibroblast collagenase was a potent inhibitor of the collagenases obtained from the culture media of the various rabbit cells and tissues. 6. Collagenases from human synovium and from mouse macrophages and bone were neither precipitated nor inhibited by antibodies to rabbit collagenase. 7. No immunoreactive material was found in lysates of rabbit polymorphonuclear leucocyte granules with the specific antisera to rabbit fibroblast collagenase. No evidence for inactive forms of rabbit collagenase in lysates of the rabbit synovial fibroblasts could be found, either by double immunodiffusion against the specific collagenase, or by displacement of active enzyme from inhibition by the IgG.

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Section: Discussionmentioning

confidence: 97%