Literature DB >> 23763

Proteoglycan-degrading enzymes. A radiochemical assay method and the detection of a new enzyme cathepsin F.

J T Dingle, A M Blow, A J Barrett, P E Martin.   

Abstract

1. Polyacrylamide beads containing entrapped 35S-labelled proteoglycan molecules have been prepared. 2. The measurement of release of radioactivity provides an extremely sensitive assay for proteoglycan-degrading enzymes, including proteinases and hyaluronidase. 3. The amount of label released is a logarithmic function of enzyme concentration or time of incubation. Experiments were made in an attempt to explain this. 4. Assays were made by the new method at several pH values, and with the inclusion of inhibitors to identify the proteoglycan-degrading enzymes of rabbit ear cartilage. 5. A previously undescribed proteinase active against proteoglycan at pH4.5 but unaffected by pepstatin, was discovered. The enzyme was named cathepsin F, and was partially purified and characterized; it was detected in human articular cartilage.

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Year:  1977        PMID: 23763      PMCID: PMC1183726          DOI: 10.1042/bj1670775

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  25 in total

1.  A photometric assay for protease digestion of the proteoglycan subunit.

Authors:  A I Sapolsky; J F Woessner; D S Howell
Journal:  Anal Biochem       Date:  1975-08       Impact factor: 3.365

2.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

3.  Cathepsin D activity in normal and osteoarthritic human cartilage.

Authors:  A I Sapolsky; R D Altman; D S Howell
Journal:  Fed Proc       Date:  1973-04

4.  Breakdown of noncollagenous chondromucoprotein matrix by leukocyte lysosome granule lysates from guinea pig, rabbit, and human.

Authors:  L J Ignarro; A L Oronsky; R J Perper
Journal:  Clin Immunol Immunopathol       Date:  1973-11

5.  Chicken alpha2-proteinase inhibitor: a serum protein homologous with ovoinhibitor of egg white.

Authors:  A J Barrett
Journal:  Biochim Biophys Acta       Date:  1974-11-05

6.  Metal-dependent proteinase of the lens. Assay, purification and properties of the bovine enzyme.

Authors:  A M Blow; R V Heyningen; A J Barrett
Journal:  Biochem J       Date:  1975-03       Impact factor: 3.857

7.  The secretion of enzymes into the pericellular environment.

Authors:  J T Dingle
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  1975-07-17       Impact factor: 6.237

8.  Human cathepsin B1. Purification and some properties of the enzyme.

Authors:  A J Barrett
Journal:  Biochem J       Date:  1973-04       Impact factor: 3.857

9.  The interaction of alpha 2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism.

Authors:  A J Barrett; P M Starkey
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

10.  Cathepsin D in cartilage: the immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions.

Authors:  A R Poole; R M Hembry; J T Dingle
Journal:  J Cell Sci       Date:  1974-01       Impact factor: 5.285

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  15 in total

1.  Neutral metallo-proteinases of rabbit bone. Separation in latent forms of distinct enzymes that when activated degrade collagen, gelatin and proteoglycans.

Authors:  A Sellers; J J Reynolds; M C Meikle
Journal:  Biochem J       Date:  1978-05-01       Impact factor: 3.857

2.  Proteoglycan-degrading enzymes of rabbit fibroblasts and granulocytes.

Authors:  Z Werb; J T Dingle; J J Reynolds; A J Barrett
Journal:  Biochem J       Date:  1978-09-01       Impact factor: 3.857

Review 3.  Cathepsin B as a cancer target.

Authors:  Christopher S Gondi; Jasti S Rao
Journal:  Expert Opin Ther Targets       Date:  2013-01-08       Impact factor: 6.902

4.  Selective and signal-dependent recruitment of membrane proteins to secretory granules formed by heterologously expressed von Willebrand factor.

Authors:  Anastasia D Blagoveshchenskaya; Matthew J Hannah; Simon Allen; Daniel F Cutler
Journal:  Mol Biol Cell       Date:  2002-05       Impact factor: 4.138

5.  The site of cartilage matrix degradation.

Authors:  J T Dingle; T T Dingle
Journal:  Biochem J       Date:  1980-08-15       Impact factor: 3.857

Review 6.  Cell-to-cell interactions in the secretion of enzymes of connective tissue breakdown, collagenase and proteoglycan-degrading neutral proteases. A review.

Authors:  G Vaes
Journal:  Agents Actions       Date:  1980-12

7.  The extraction of a neutral metalloproteinase from the involuting rat uterus, and its action on cartilage proteoglycan.

Authors:  A Sellers; J F Woessner
Journal:  Biochem J       Date:  1980-09-01       Impact factor: 3.857

8.  A direct simultaneous plate assay of proteoglycan and collagen degradation by cells in culture and its application to synovial cells.

Authors:  C Peeters-Joris; X Emonds-Alt; G Vaes
Journal:  Biochem J       Date:  1981-04-15       Impact factor: 3.857

9.  Secretion of an articular cartilage proteoglycan-degrading enzyme activity by murine T lymphocytes in vitro.

Authors:  G M Kammer; A I Sapolsky; C J Malemud
Journal:  J Clin Invest       Date:  1985-08       Impact factor: 14.808

10.  The production in culture of metalloproteinases and an inhibitor by joint tissues from normal rabbits, and from rabbits with a model arthritis. I. Synovium.

Authors:  G J Cambray; G Murphy; D P Page-Thomas; J J Reynolds
Journal:  Rheumatol Int       Date:  1981       Impact factor: 2.631

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