Abstract
3-Aminobenzamide is an inhibitor of poly-(ADP-ribosyl)ation. In concentrations from 3 to 10 mM it reduced the collagenase activity in culture supernatants of interleukin-1β-stimulated rabbit synovial fibroblasts. 3-Aminobenzoate, not an inhibiter of poly(ADP-ribosyl)ation, had no effect on collagenase activity at a concentration of 10 mM. We concluded that poly(ADP-ribosyl)ation plays a role in the induction of the expression of collagenase and that 3-aminobenzamide can inhibit this process.
Similar content being viewed by others
References
Harris ED (1993) Etiology and pathology of rheumatoid arthritis. In: Kelly WN, Harris ED Jr, Ruddy S, Sledge CB (eds) Textbook of rheumatology. Saunders, Philadelphia, pp 833–858
Harris ED, Sporn MB (1981) Proliferative diseases. Am J Med 70:1231–1236
Brinckerhof CE, Harris ED (1981) Survival of rheumatoid synovium in nude mice. Am J Pathol 103:411–419
Murphy G, Nagase H, Brinckerhoff CE (1988) Relationship of procollagenase activator, stromelysin, and matrix metalloprotease 3. Coll Relat Res 8:389–391
Gross RH, Sheldon LA, Fletcher CF, Brinckerhoff CE (1984) Isolation of a collagenase cDNA clone and measurement of changing collagenase mRNA levels during induction in rabbit synovial fibroblasts. Proc Natl Acad Sci USA 81:1981–1985
Fini ME, Karmilowicz MJ, Ruby PL, Beeman AM, Borges KA, Brinckerhoff CE (1987) Cloning of a complementary DNA for rabbit proactivator. A metalloprotease that activates synovial cell collagenase shares homology with stromelysin and transin, and is coordinately regulated with collagenase. Arthritis Rheum 30:1254–1264
Frisch SM, Clark EJ, Werb Z (1987) Coordinate regulation of stromelysin and collagenase genes determined with cDNA probes. Proc Natl Acad Sci USA 84:2600–2604
Althaus FR, Richter C (1987) ADP-ribosylation of proteins. Springer, Berlin, pp 115–116
Ueda K, Hayaishi O (1985) ADP-ribosylation. Annu Rev Biochem 54:73–100
Kieval RI, Young CT, Prohazka D, Brinckerhoff CE, Trentham DE (1989) Evaluation of a modified hexose sugar amiprilose hydrochloride, in experimental models of synovitis. J Rheumatol 16:67–74
Dayer JM, Krane SM, Russel RGG, Robinson DR (1976) Production of collagenase and prostaglandins by isolated adherent synovial cells. Proc Natl Acad Sci USA 73:945–949
Brinckerhoff CE, Benoit MC, Culp WJ (1985) Autoregulation of collagenase production by a protein synthesized and secreted by synovial fibroblasts: a cellular mechanism for control of collagen degradation. Proc Natl Acad Sci USA 82:1916–1920
Nethery A, Lyons JG, O'Grady RL (1986) A spectrophotometric collagenase assay. Anal Biochem 159:390–395
Labarca C, Paigen K (1980) A simple, rapid, and sensitive DNA assay procedure. Anal Biochem 102:344–352
Yamanaka H, Willis EH, Penning CA, Peebles CL, Tan EM, Carson DA (1989) Characterization of the human autoantibody response to poly(ADP-ribose)polymerase. In: Jacobson MK, Jacobson EL (eds) ADP-ribose transfer reactions. Springer, New York, pp 139–144
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ehrlich, W., Huser, H. & Kröger, H. Inhibition of the induction of collagenase by interleukin-1 β in cultured rabbit synovial fibroblasts after treatment with the poly(ADP-ribose)-polymerase inhibitor 3-aminobenzamide. Rheumatol Int 15, 171–172 (1995). https://doi.org/10.1007/BF00301776
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00301776