Abstract
The cell-surface neutral endopeptidase 3.4.24.11 (NEP) activity of the common acute lymphoblastic leukaemia antigen (CALLA) cleaves diverse peptide mediators at specific sites and it has been postulated that it regulates immune responses. The concentration of NEP was quantified in detergent extracts of synovial tissues by the percentage hydrolysis of [3H-D-Ala]-Leu enkephalin/hr/100 mg of tissue. The synovial tissue concentration of NEP was higher in all patients with rheumatoid arthritis (n = 7; group mean +/- SD = 29.4 +/- 20.2%), and was higher with degenerative joint disease (n = 6 of 8; group mean +/- SD = 11.9 +/- 10.4%) than with traumatic arthropathy (n = 3; 1.1 +/- 0.7%). The lack of direct relationship between synovial tissue NEP concentration and leukocytic infiltration suggests that the cellular source of NEP may be synoviocytes or fibroblasts, and that NEP may have distinctive pathogenetic roles in human arthritis.
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Selected References
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- Erdös E. G., Skidgel R. A. Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 1989 Feb;3(2):145–151. [PubMed] [Google Scholar]
- Jongeneel C. V., Quackenbush E. J., Ronco P., Verroust P., Carrel S., Letarte M. Common acute lymphoblastic leukemia antigen expressed on leukemia and melanoma cell lines has neutral endopeptidase activity. J Clin Invest. 1989 Feb;83(2):713–717. doi: 10.1172/JCI113936. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Llorens C., Malfroy B., Schwartz J. C., Gacel G., Roques B. P., Roy J., Morgat J. L., Javoy-Agid F., Agid Y. Enkephalin dipeptidyl carboxypeptidase (enkephalinase) activity: selective radioassay, properties, and regional distribution in human brain. J Neurochem. 1982 Oct;39(4):1081–1089. doi: 10.1111/j.1471-4159.1982.tb11500.x. [DOI] [PubMed] [Google Scholar]
- Lorkowski G., Zijderhand-Bleekemolen J. E., Erdös E. G., von Figura K., Hasilik A. Neutral endopeptidase-24.11 (enkephalinase). Biosynthesis and localization in human fibroblasts. Biochem J. 1987 Dec 1;248(2):345–350. doi: 10.1042/bj2480345. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Malfroy B., Kuang W. J., Seeburg P. H., Mason A. J., Schofield P. R. Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase). FEBS Lett. 1988 Feb 29;229(1):206–210. doi: 10.1016/0014-5793(88)80828-7. [DOI] [PubMed] [Google Scholar]
- Painter R. G., Dukes R., Sullivan J., Carter R., Erdös E. G., Johnson A. R. Function of neutral endopeptidase on the cell membrane of human neutrophils. J Biol Chem. 1988 Jul 5;263(19):9456–9461. [PubMed] [Google Scholar]
- Pierart M. E., Najdovski T., Appelboom T. E., Deschodt-Lanckman M. M. Effect of human endopeptidase 24.11 ("enkephalinase") on IL-1-induced thymocyte proliferation activity. J Immunol. 1988 Jun 1;140(11):3808–3811. [PubMed] [Google Scholar]
- Puri J., Factorovich Y. Selective inhibition of antigen presentation to cloned T cells by protease inhibitors. J Immunol. 1988 Nov 15;141(10):3313–3317. [PubMed] [Google Scholar]
- Shipp M. A., Vijayaraghavan J., Schmidt E. V., Masteller E. L., D'Adamio L., Hersh L. B., Reinherz E. L. Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): direct evidence by cDNA transfection analysis. Proc Natl Acad Sci U S A. 1989 Jan;86(1):297–301. doi: 10.1073/pnas.86.1.297. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Werb Z., Clark E. J. Phorbol diesters regulate expression of the membrane neutral metalloendopeptidase (EC 3.4.24.11) in rabbit synovial fibroblasts and mammary epithelial cells. J Biol Chem. 1989 Jun 5;264(16):9111–9113. [PubMed] [Google Scholar]