Immunolocalization of the cleavage of the aggrecan core protein at the Asn341-Phe342 bond, as an indicator of the location of the metalloproteinases active in the lysis of the rat growth plate

Anatomical Record

Volumn 252, Issue 1, 1998, Pages 117-132

  Lee, Eunice R ^a   Lamplugh, Lisa ^a   Leblond, Charles Philippe ^a   Mordier, Sylvie ^b   Magny, Marie Claude ^b   Mort, John S ^b  

^a SHRINERS HOSPITAL FOR CHILDREN   (Canada)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

Aggrecan degradation; Bone growth; Epiphyseal growth plate; Metalloproteinases

Indexed keywords

AGGRECAN; METALLOPROTEINASE;

ANIMAL TISSUE; ARTICLE; BONE GROWTH; BONE MATRIX; CONTROLLED STUDY; ENZYME LOCALIZATION; EPIPHYSIS PLATE; GROWTH PLATE; IMMUNOHISTOCHEMISTRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT; TIBIA;

AGGRECANS; AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ANTIBODY SPECIFICITY; ASPARAGINE; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; EXTRACELLULAR MATRIX PROTEINS; GROWTH PLATE; LECTINS, C-TYPE; METALLOENDOPEPTIDASES; MICROSCOPY, ELECTRON; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PHENYLALANINE; PROTEOCHONDROITIN SULFATES; PROTEOGLYCANS; RABBITS; RATS; TIBIA;

ANIMALIA;

EID: 0031688163     PISSN: 0003276X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0185(199809)252:1<117::AID-AR10>3.0.CO;2-R     Document Type: Article

References (56)

1. Anand-Apte B, Bao L, Smith R, Iwata K, Olsen BJ, Zetter B, Apte SS. A review of tissue inhibitor of metalloproteinases-3 (TIMP-3) and experimental analysis of its effect on primary tumor growth. Biochem. Cell. Biol. 1996;74:853-862.
2. Belanger LF. Autoradiographic visualization of the entry and transit of 35S in cartilage, bone, and dentine of young rats and the effect of hyaluronidase in vitro. Can. J. Physiol. Biochem. 1954;32:161-169.
3. Blair HC, Dean DD, Howell DS, Teitelbaum SL, Jeffrey JJ. Hypertrophic chondrocytes produce immunoreactive collagenase in vivo. Connect, Tissue Res. 1989;23:65-73.
4. Brown CC, Hembry RM, Reynolds JJ. Immunolocalisation of metalloproteinases and their inhibitor in the rabbit growth plate. J. Bone Joint Surg. 1989;71A:580-593.
5. Brown RA, Kayse M, McLaughlin B, Weiss JB. Collagenase and gelatinase production by calcifying growth plate chondrocytes. Exp. Cell Res. 1993;208:1-9.
6. Cole AA, Boyd T, Luchene L, Kuettner KE, Schmid TM. Type X collagen degradation in long-term serum-free culture of the embryonic chick tibia following production of active collagenase and gelatinase. Dev. Biol. 1993;159:528-534.
7. Dean DD, Muniz OE, Berman I, Pita JC, Carreno MR, Woessner JF, Howell DS. Localization of collagenase in the growth plate of rachitic rats. J. Clin. Invest. 1985;76:716-722.
8. Denhardt D, Feng B, Edwards DJ, Cocuzzi ET, Malyankar UM. Tissue inhibitor of metalloproteinases (TIMP, aka EPA): Structure, control of expression and biological functions. Pharmacol. Ther. 1993;59:329-341.
9. Doege K, Sasaki M, Horigan E, Hassell JR, Yamada Y. Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones. J. Biol. Chem. 1987;262:17757-17767.
10. Doege KJ, Sasaki M, Kimura T, Yamada Y. Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. J. Biol. Chem. 1991;266:894-902.
11. Flannery CR, Lark MW, Sandy JD. Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage. J. Biol. Chem. 1992;267:1008-1014.
12. Fosang AJ, Neame PJ, Hardingham TE, Murphy G, Hamilton JA. Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins. J. Biol. Chem. 1991;266:15579-15582.
13. Fosang AJ, Neame PJ, Last K, Hardingham TE, Murphy G, Hamilton JE. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J. Biol. Chem. 1992;267:19470-19474.
14. Fosang AJ, Last K, Knauper V, Neame PJ, Murphy G, Hardingham TE, Tschesche H, Hamilton JA. Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain. Biochem. J. 1993;295:273-276.
15. Fosang AJ, Last K, Knauper V, Murphy G, Neame PJ. Degradation of cartilage aggrecan by collagenase-3 (MMP-13). FEBS Lett. 1996;380: 17-20.
16. Gibson GJ, Lin DL, Schaffler MB, Kimura JH. Endochondral resorption of chick sterna in culture. J. Orthop. Res. 1995;13:542-552.
17. Greulich RC, Leblond CP. Radioautographic visualization of radiocarbon in the organs and the tissues of newborn rats following administration of 14C labeled bicarbonate. Anat. Rec. 1953;115:559-585.
18. Griendling KK, Alexander RW. Endothelial control of the cardiovascular system: Recent advances. FASEB J. 1996;10:283-292.
19. Hardingham TE, Fosang AJ, Dudhia J. The structure, function and turnover of aggrecan, the large aggregating proteoglycan from cartilage. Eur. J. Clin. Chem. Clin. Biochem. 1994;32:249-257.
20. Hill PA, Reynolds JJ, Meikle MC. Inhibition of stimulated bone resorption in vitro by TIMP-1 and TIMP-2. Biochim. Biophys. Acta 1993;1177:71-74.
21. Hill PA, Murphy G, Docherty AJ, Hembry RM, Millican TA, Reynolds JJ, Meikle MC. The effects of selective inhibitors of matrix metalloproteinases (MMP's) on bone resorption and the identification of MMP's and TIMP-1 in isolated osteoclasts. J. Cell Sci. 1994;107:3055-3064.
22. Hsu S-M, Raine L, Fanger H. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques. J. Histochem. Cytochem. 1981;29:577-580.
23. Hughes CE, Caterson B, White RJ, PJ Roughley, Mort JS. Monoclonal antibodies recognizing protease-generated neoepitopes from cartilage proteoglycan degradation. J. Biol. Chem. 1992;267:16011-16014.
24. Hunter WL, Arsenault AL. Vascular invasion of the epiphyseal growth plate: Analysis of metaphyseal capillary ultrastructure and growth. Anat. Rec. 1990;227:223-231.
25. Hunziker EB, Schenk RF, Cruz-Orive LM. Quantitation of chondrocyte performance in growth-plate cartilage during longitudinal bone growth. J. Bone Joint Surg. Am. 1987;69A:162-173.
26. Ilic MZ, Handley CJ, Robinson HC, Mok MT. Mechanism of catabolism of aggrecan by articular cartilage. Arch. Biochem. Biophys. 1992;294: 115-122.
27. Jensen WA. Microscopic histochemistry and cell morphology. In: Botanical Histochemistry: Principles and Practice. San Francisco: WH Freeman, 1962: 175-208.
28. King J, Laemmli UK. Polypeptides of the tail fibers of bacteriophage T4. J. Mol. Biol. 1971;62:465-477.
29. Lark MW, Williams H, Hoernner LA, Weidner J, Ayala JM, Harper CF, Christen A, Olszewski J, Konteatis Z, Webber R, Mumford RA. Quantification of a matrix metalloproteinase-generated aggrecan G1 fragment using monospecific anti-peptide serum. Biochem. J. 1995a;307:245-252.
30. Lark MW, Gordy JT, Weidner JR, Ayala J, Kimura JH, Williams HR, Mumford RA, Flannery CR, Carlson SS, Iwata M, Sandy JD. Cell-mediated catabolism of aggrecan. Evidence that cleavage at the "aggrecanase" site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain. J. Biol. Chem. 1995b;270:2550-2556.
31. Leblond CP, Wilkinson GW, Belanger LF, Robichon J. Radioautographic visualization of bone formation in the rat. Am. J. Anat. 1950;87:289-327.
32. Lee ER, Matsui Y, Poole AR. Immunochemical and immunocytochemical studies of the C-propeptide of type II procollagen in chondrocytes of the growth plate. J. Histochem. Cytochem. 1990;38:659-673.
33. Lee ER, Lamplugh L, Shepard NJ, Mort JS. The septoclast, a cathepsin B-rich cell involved in the resorption of the growth plate. J. Histochem. Cytochem. 1995;43:525-536.
34. Matsui Y, Alini M, Webber C, Poole AR. Characterization of aggregating proteoglycans from the proliferative, maturing, hypertrophic and calcifying zones of the cartilaginous physis. J. Bone Joint Surg. Am. 1991;73A:1064-1074.
35. McLean I, Nakane PI. Periodate-lysine-paraformaldehyde fixative. A new fixative for immunoelectron microscopy. J. Histochem. Cytochem. 1974;22:1077-1083.
36. Nagase H. Activation mechanisms of matrix metalloproteinases. J. Biol. Chem. 1997;378:151-160.
37. Pal S, Tang L-H, Choi H, Habermann E, Rosenberg L, Roughley PJ, Poole AR. Structural changes during development in bovine fetal epiphyseal cartilage. Coll. Relat. Res. 1981;1:151-176.
38. Paulsson M, Morgelin M, Wiedemann H, Beardmore-Gray M, Dunham D, Hardingham T, Heinegard D, Timpl R, Engel J. Extended and globular protein domains in cartilage proteoglycans. Biochem. J. 1987;245:763-772.
39. Plaas AHK, Sandy JD. A cartilage expiant system for studies of aggrecan structure, biosynthesis and catabolism in discrete zones of the mammalian growth plate. Matrix 1993;13:135-147.
40. Poole AR. Cartilage in health and disease. In: McCarty DJ, Koopman WJ, eds. Arthritis and Allied Conditions. Philadelphia: Lea & Febiger, 1993: 279-333.
41. Rath NC, Huff WE, Balog JM, Bayyari GR, Reddy RP. Matrix metalloproteinase activities in avian tibial dyschondroplasia. Poult. Sci. 1997;76:501-505.
42. Roberts CR, Roughley PJ, Mort JS. Degradation of human proteoglycan aggregate induced by hydrogen peroxide. Biochem. J. 1989;259: 805-811.
43. Roughley PJ, Lee ER. Cartilage proteoglycans: Structure and potential functions. Microsc. Res. Tech. 1994;28:385-397.
44. Roughley PJ, White RJ, Poole AR. Identification of a hyaluronic acid-binding protein that interferes with the preparation of high-buoyant-density proteoglycan aggregates from adult human articular cartilage. Biochem. J. 1985;231:129-138.
45. Sandy JD, Neame PJ, Boynton RE, Flannery CR. Catabolism of aggrecan in cartilage expiants. Identification of a major cleavage site within the interglobular domain. J. Biol. Chem. 1991a;266:8683-8685.
46. Sandy JD, Boynton RE, Flannery CR. Analysis of the catabolism of aggrecan in cartilage expiants by quantitation of peptides from the three globular domains. J. Biol. Chem. 1991b;266:8198-8205.
47. Schenk RK, Spiro D, Wiener J. Cartilage resorption in the tibial epiphyseal plate of growing rats. J. Cell Biol. 1967;34:275-291.
48. Schmitz JP, Dean DD, Schwartz Z, Cochran DL, Grant GM, Klebe RJ, Nakaya H, Boyan BD. Chondrocyte cultures express matrix metalloproteinase mRNA and immunoreactive protein; stromelysin-1 and 72 kDa gelatinase are localized in extracellular matrix vesicles. J. Cell. Biochem. 1996;61:375-391.
49. Shapses SA, Sandell LJ, Ratcliffe A. Differential rates of aggrecan synthesis and breakdown in different zones of the bovine growth plate. Matrix Biol. 1994;14:77-86.
50. Singer II, Kawka DW, Bayne EK, Donatelli SA, Weidner JR, Williams HR, Ayala JM, Mumford RA, Lark MW, Giant TT, Nabozny GH, David CS. VDIPEN, a metalloproteinase-generated neoepitope, is induced and immunolocalized in articular cartilage during inflammatory arthritis. J. Clin. Invest. 1995;95:2178-2186.
51. Stahle-Backdahl M, Sandstedt B, Bruce K, Lindahl A, Jimenez MB, Vega JA, Lopez-Otin C. Collagenase-3 (MMP-13) is expressed during human fetal ossification and re-expressed in postnatal bone remodeling and in rheumatoid arthritis. Lab. Invest. 1997;76:717-728.
52. Sztrolovics R, Alini M, Roughley PJ, Mort JS. Aggrecan degradation in human intervertebral disc and articular cartilage. Biochem. J. 1997;326:235-241.
53. Vaes G, Delaisee JM, Eeckhout Y. Relative roles of collagenase and lysosomal. Matrix 1992;S1:383-388.
54. Walker KVR, Kember NF. Cell kinetics of growth cartilage in the rat tibia. I. Measurements in young male rats. Cell. Tiss. Kinet. 1972;5:401-408.
55. Woessner JF. Regulation of matrilysin in the rat uterus. Biochem. Cell. Biol. 1996;74:777-784.
56. Yu AE, Hewitt RE, Kleiner DE, Stetler-Stevenson WG. Molecular regulation of cellular invasion-role of gelatinase A and TIMP-2. Biochem. Cell. Biol. 1996;74:823-831.