The serine protease inhibitor trappin-2 is present in cartilage and synovial fluid in osteoarthritis

Journal of Rheumatology

Volumn 33, Issue 2, 2006, Pages 318-325

  Jaovisidha, Kanyakorn ^a   Etim, Ann ^b   Yamakawa, Koji ^b   Masuda, Ikuko ^b   Gohr, Claudia M ^b   Wakim, Bassam T ^c   Boonapatcharoen, Nimaradee ^a   Ninomiya, James ^d   Rosenthal, Ann K ^b  

^a CHULALONGKORN UNIVERSITY   (Thailand)

^b CLEMENT J ZABLOCKI VETERANS AFFAIRS MEDICAL CENTER   (United States)

^c Department of Biochemistry ^*

^d MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

Articular cartilage; Elafin; Osteoarthritis; Serine protease inhibitors; Transglutaminase; Trappin

Indexed keywords

COMPLEMENTARY DNA; DANSYLCADAVERINE; ELAFIN; FIBROMODULIN; MESSENGER RNA; POLYAMINE; SERINE PROTEINASE INHIBITOR; TRAPPIN 2; UNCLASSIFIED DRUG;

ARTHRITIS; ARTICLE; ARTICULAR CARTILAGE; CARTILAGE CELL; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; OSTEOARTHRITIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SYNOVIAL FLUID; WESTERN BLOTTING;

ADOLESCENT; ADULT; CARTILAGE, ARTICULAR; CELLS, CULTURED; CHONDROCYTES; CULTURE MEDIA, CONDITIONED; HUMANS; IMMUNOENZYME TECHNIQUES; LEUKOCYTE ELASTASE; OSTEOARTHRITIS; PROTEIN PRECURSORS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; SYNOVIAL FLUID;

EID: 32144440435     PISSN: 0315162X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (42)

1. Schalkwijk J, Wiedow O, Hirose S. The trappin gene family: proteins defined by an N-terminal transglutaminase substrate domain and a C-terminal four-disulphide core. Biochem 1999;340:569-77.
2. Pfundt R, van Ruissen F, van Vlijmen-Willems I, et al. Constitutive and inducible expression of SKALP/elafin provides anti-elastase defense in human epithelia. J Clin Invest 1996;98:1389-99.
3. Steinen P, Marekov L. The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J Biol Chem 1995;270:17702-11.
4. Kuijpers A, Zeeuwen P, de Jongh G, et al. Skin-derived antileukoproteinase (SKALP) is decreased in pustular forms of psoriasis. A clue to the pathogenesis of pustule formation? Arch Dermatol Res 1996;288:641-7.
5. Momohara S, Kashiwazaki S, Inoue K, Saito S, Nakagawa T. Elastase from polymorphonuclear leukocyte in articular cartilage and synovial fluids of patients with rheumatoid arthritis. Clin Rheumatol 1997;16:133-40.
6. Furmaniak-Kazmierczak E, Cooke T, Manuel R, et al. Studies of thrombin-induced proteoglycan release in the degradation of human and bovine cartilage. J Clin Invest 1994;94:472-80.
7. Ayral X, Pickering E, Woodworth T, Mackillop N, Dougados M. Synovitis: a potential predictive factor of structural progression of medial tibiofemoral knee osteoarthritis - results of a 1 year longitudinal arthroscopic study in 422 patients. Osteoarthritis Cartilage 2005;13:361-7.
8. Clemmons D, Busby WJ, Garmong A, et al. Inhibition of insulin-like growth factor binding protein 5 proteolysis in articular cartilage and joint fluid results in enhanced concentrations of insulin-like growth factor 1 and is associated with improved osteoarthritis. Arthritis Rheum 2002;46:694-703.
9. Chidwick K, Whichelow C, Zhang Z, et al. Relationship between α1-antitrypsin inactivation and tumor necrosis factor α concentration in the synovial fluid of patients with rheumatoid arthritis. Arthritis Rheum 1994;37:1723-6.
10. Murphy G, Ward R, Gavrilovic J, Atkinson S. Physiologic mechanisms for metalloproteinase activation. Matrix Suppl 1992;1:224-30.
11. Milner J, Elliot S-F, Cawston T. Activation of procollagenases is a key control point in cartilage collagen degradation: Interaction of serine and metalloproteinase pathways. Arthritis Rheum 2001;44:2084-96.
12. Walker B, Lynas J. Strategies for the inhibition of serine proteases. Cell Mol Life Sci 2001;58:596-624.
13. Shtacher G, Maayan R, Feinstein G. Proteinase inhibitors in human synovial fluid. Biochim Biophys Acta 1973;303:138-47.
14. Abbink J, Kamp A, Nuijens J, Swaak T, Hack C. Proteolytic inactivation of α1-antitrypsin and α1-chymotrypsin by neutrophils in arthritic joints. Arthritis Rheum 1993;36:168-80.
15. Melrose J, Smith S, Rodgers K, et al. Immunolocalisation of BPTI-like serine protease inhibitory proteins in mast cells, chondrocytes and intervertebral disc fibrochondrocytes of ovine and bovine connective tissues. An immunohistochemical and biochemical study. Histochem Cell Biol 2000;114:137-46.
16. Ghosh P, Andrews JL, Osborne RA, Lesjak MS. Variation with ageing and degeneration of the serine and cysteine proteinase inhibitors of human articular cartilage. Agents Actions Suppl 1986;18:69-81.
17. Kawabata K, Moore A, Willoughby D. Impaired activity of protease inhibitors towards neutrophil elastase bound to human articular cartilage. Ann Rheum Dis 1996;55:248-52.
18. Nara K, Ito S, Ito T, et al. Elastase inhibitor elafin is a new type of proteinase inhibitor which has a transglutaminase-mediated anchoring sequence termed "cementoin". J Biochem Tokyo 1994;115:441-8.
19. Lorand L, Graham RM. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 2003;4:140-56.
20. Rosenthal AK, Derfus BA, Henry LA. Transglutaminase activity in aging articular chondrocytes and articular cartilage vesicles. Arthritis Rheum 1997;40:966-70.
21. Johnson K, Hashimoto S, Lotz M, Pritzker K, Terkeltaub R. Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa. Am J Pathol 2001;159:149-63.
22. Rosenthal A, Cheung H, Ryan L. Transforming growth factor beta 1 stimulates inorganic pyrophosphate elaboration by porcine cartilage. Arthritis Rheum 1991;34:904-11.
23. Lowry O, Rosebrough N, Farr A, Randall R. Protein measurement with Folin-phenol reagent. J Biol Chem 1951;193:265-75.
24. Zeeuwen P, Hendriks W, de Jong W, Schalkwijk J. Identification and sequence analysis of two new members of the SKALP/elafin and SPAI-2 gene family. Biochemical properties of the transglutaminase substrate motif and suggestions for a new nomenclature. J Biol Chem 1997;272:20741-8.
25. Sanger F, Nicklen S, Coulson A. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977;74:5463-7.
26. Molhuizen H, Alkemade H, Zeeuwen P, et al. SKALP/elafin: An elastase inhibitor from cultured human keratinocytes. J Biol Chem 1993;268:12028-32.
27. Ohlsson S, Tufvesson B, Polling A, Ohlsson K. Distribution of the secretory leukocyte proteinase inhibitor in human articular cartilage. Biol Chem 1997;378:1055-8.
28. Molhuizen H, Schalkwijk J. Structural, biochemical, and cell biological aspects of the serine protease inhibitor SKALP/elafin/ESI. Biol Chem Hoppe-Seyler 1995;376:1-7.
29. Alkemade J, Molhiuzen H, Ponec M, et al. SKALP/elafin is an. inducible proteinase inhibitor in human epidermal keratinocytes. J Cell Sci 1994;107:2335-42.
30. Tanaka N, Fujioka A, Tajima S, Ishibashi A, Hirose S. Elafin is induced in epidermis in skin disorders with dermal neutrophilic infiltration: interleukin-1β and tumor necrosis factor-α stimulate its secretion in vitro. Br J Dermatol 2000;143:728-32.
31. Reid P, Marsden M, Cunningham G, Haslett C, Sallenave J-M. Human neutrophil elastase regulates the expression and secretion of elafin (elastase-specific inhibitor) in type II alveolar epithelial cells. FEBS Letts 1999;457:33-7.
32. O'Blenes SB, Zaidi SH, Cheah AY, McIntyre B, Kaneda Y, Rabinovitch M. Gene transfer of the serine elastase inhibitor elafin protects against vein graft degeneration. Circulation 2000;102:III289-95.
33. Ying Q, Simon S. Kinetics of the inhibition of proteinase 3 by elafin. Am J Resp Cell Mol Biol 2001;24:83-9.
34. Nakano S, Ikata T, Kinoshita I, Kanematsu J, Yasuoka S. Characteristics of the protease activity in synovial fluid from patients with rheumatoid arthritis and osteoarthritis. Clin Exp Rheumatol 1999;17:161-70.
35. Ossanna P, Test S, Matheson N, Regiani S, Weiss S. Oxidative regulation of neutrophil elastase-alpha-1-proteinase inhibitor interactions. J Clin Invest 1986;77:1939-51.
36. Vissers M, George P, Bathurst I, Brennan S, Winterbourn C. Cleavage and inactivation of alpha 1-antitrypsin by metalloproteinases released from neutrophils. J Clin Invest 1988;82:706-11.
37. Henry M, McMahon K, Costello C, Fitzgerald M, O'Connor C. Secretory leukocyte proteinase inhibitor and elafin are resistant to degradation by MMP-8. Exp Lung Res 2002;28:85-97.
38. Nakane H, Ishida-Yamamoto A, Takahashi H, Iizuka H. Elafin, a secretory protein, is cross-linked into the cornified cell envelopes from the inside of psoriatic keratinocytes. J Invest Dermatol 2002;119:50-5.
39. Knudson C, Knudson W. Cartilage proteoglycans. Cell Dev Biol 2001;12:69-78.
40. Cs-Szabo G, Roughley P, Plaas A, Glant T. Large and small proteoglycans of osteoarthritic and rheumatoid articular cartilage. Arthritis Rheum 1995;38:660-8.
41. Saamanen A-M, Salminen H, Rantakokko A, Heinegard D, Vuorio E. Murine fibromodulin: cDNA and genomic structure, and age-related expression and distribution in the knee joint. Biochem J 2001;355:577-85.
42. Svensson L, Aszodi A, Reinholt F, et al. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J Biol Chem 1999;274:9636-47.