La cartilagine articolare è un tessuto connettivo avascolare, aneurale che ricopre le superfici articolari. La funzione di assorbimento delle sollecitazioni meccaniche, a protezione dell'osso subcondrale, rende la supeficie articolare idonea a sostenere il carico.
Le funzioni inerenti le modalità di assorbimento della sollecitazione meccanica, che fanno sì che la deformazione sia reversibile, dipendono in larga parte dalle caratteristiche della cartilagine, intesa come struttura altamente organizzata. Nell'osteoartrosi umana e nei suoi modelli animali l'alterazione strutturale dei proteoglicani cartilaginei rappresenta l'evento centrale.
Vengono discusse, alla luce delle acquisizioni più recenti, le implicazioni sulle proprieta fisico-chimiche e morfo-strutturali della cartilagine articolare riguardanti le caratteristiche di base dei proteoglicani, la struttura dei collageni, l'organizzazione della matrice extracellulare e le sue modificazioni nella senescenza ed in corso di osteoartrosi con le relative conseguenze sulle proprietà biomeccaniche del disco intervertebrale. Le conoscenze relative alle alterazioni della struttura proteoglicanica e lo sviluppo di nuovi metodi di determinazione dei markers biochimici del danno cartilagineo potrebbero migliorare la comprensione delle relazioni fra senescenza ed osteoartrosi, nonchè il riconoscimento delle modificazioni più precoci e la valutazione della risposta terapeutica.
AtkinsEDT: Molecular architecture of the animal and some microbial extracellular polysaccharides. In: WaltronAG (eds): Proceedings of the first Cleveland symposium on macromolecules. Elsevier Scientific, Amsterdam1977: 61–85.
2.
BaylissM: Proteoglycan structure and biosynthesis: changes during development and ageing of human articular cartilage. In: VerbruggenG & VeysEM (eds): Degenerative Joints. Excerpta Medica. Amsterdam1985: vol 2, 13–19.
3.
BaylissMTVennMMaroudasAAliSY: Structure of proteoglycans from different layers of human articular cartilage. Biochem J209: 387–400, 1983.
4.
BaylissMT: Proteoglycan structure in normal and osteoarthrotic human cartilage. In: KuettnerKSchleyerbachRHascallVC (eds): Articular cartilage biochemistry. Raven Press, New York1986: 295–310.
5.
BaylissMT: Synthesis and extracellular assembly of proteoglycans in human articular cartilage. Agents Actions23: 1–2, 1988.
6.
BrandtKDFifeRS: Ageing in relation to the pathogenesis of osteoartrhitis. Clin Rheum Dis12: 117–130, 1986.
7.
BurmesterGRMencheD: Application of monoclonal antibodies to the characterization of cells eluted from human articular cartilage. Arthritis Rheum26: 1187–1191, 1983.
8.
CarneySLBillinghamMEJMuirH: The structure and metabolism of collagen and proteoglycan in normal and osteoarthritic articular cartilage. In: VerbruggenGVeysEM: Degenerative Joint, 1985: 117–128.
9.
CerviniCBaldassarreA: Le artropatie degenerative: aspetti statistico-epidemiologici. L'INADEL13: 113–139, 1962.
CerviniCPaolinelliE: Artrosi (artropatie degenerative). Malattie artro-reumatiche e connettiviti. Parte X del Trattato Italiano di Medicina Interna. P Introzzi, USES, Firenze1983: 717–754.
12.
CerviniCSalaffiF: Lavoro e malattie di interesse reumatologico. Il Reumatologo14: 91–97, 1993.
13.
CerviniC: Il ruolo artrosigeno della senescenza. Geriatria1: 45–50, 1989.
14.
CerviniC: Incidenza e frequenza dell'artrosi e delle sue principali localizzazioni. Reumatologia Oggi2: 5–10, 1983.
15.
CerviniC: L'artrosi: quale prevenzione?Il Reumatologo5: 183–187, 1991.
16.
ChampionBRReinerARoughleyPJ: Age-related changes in the antigenicity of human cartilage proteoglycans. Collagen and Related Research2: 45–60, 1982.
17.
DudhiaJFosangAJHardinghamTE: Domain structures and sequence similarities in cartilage proteoglycans. Biochem Soc Trans19: 198–200, 1990.
18.
DunlopRBAdamsMAHuttonWC: Disc space narrowing and the lumbar facet joints. J Bone Joint Surg (Br)66: 706–710, 1984.
19.
ElliottRJGardnerDL: Changes with age in the glycosaminoglycans of human articular cartilage. Ann Rheum Dis38: 371–377, 1979.
20.
EyreDMcDevittCA: Biosynthesis of collagen and other matrix proteins by articular cartilage in experimental osteoarthitis. Biochem J188: 823–837, 1980.
21.
EyreDRWuJJWoodsPEWeisMA: The cartilage collagens and joint degeneration. Br J Rheumatol30 (suppl 1): 10–15, 1991.
22.
EyreDR: Collagens of the disc. In: GhoshP, ed, Biology of the intervertebral disc. CRC Press, vol. 1, Boca Raton FL1988: 171–88.
FosangAJHardinghamTE: Isolation of the N-terminal globular domains from cartilage proteoglycans. Biochem J261: 801–809, 1989.
25.
GallagherJT: The extended family of proteoglycans: social residents of the pericellular zone. Curr Op Cell Bio1: 1201–1218, 1989.
26.
GarvinPJJenningsRBSternIJ: Enzymatic digestion of the nucleus pulposus: a review of experimental studies with chymopapain. Orthop Clin N Am8: 27–35, 1977.
27.
GoodfellowJWBulloughPG: The pattern of ageing of the articular cartilage of the elbow joint. J Bone Joint Surg49B: 175–181, 1967.
28.
GotfriedYBradfordDSOegemaTR: Facet joint changes after chemonucleolysis-induced disc space narrowing. Spine11: 944–950, 1986.
29.
GrecoFSpecchiaNFalcigliaF: Aspetti ultrastrutturali del processo di adattamento della cartilagine articolare allo stimolo meccanico. Giorn It Ort Traum18: 319–329, 1992.
30.
GuernePACarsonDALotzM: IL-6 production by human articular chondrocytes. Modulation of its synthesis by cytokines, growth factors, and hormones in vitro. J Immunol144: 499–505, 1990.
31.
HalbergDGFroulxGDoegeK: A segment of the cartilage proteoglycan core protein has lectin like activity. Biol Chem263: 9486–9490, 1988.
32.
HardinghamTBaylissM: Proteoglycans of articular cartilage: changes in agin g and in joint disease. Semin Arthritis Rheum20 (suppl 1): 12–23, 1990.
33.
HardinghamTECatersonBBaylissMT: Appearance of novel chndroitin sulphate structures in the articular cartilage from experimental canine osteoarthritis joints. Trans 35th Orthop Res Soc USA14: 305, 1989.
34.
HardinghamTEMuirH: Biosynthesis of proteoglycans in cartilage slices. Fractionation by gel chromatography and equilibrium density-gradient centrifugation. Biochem J126: 791–803, 1972.
35.
HardinghamTE: Biosyntesis, assembly and turnover of cartilage proteoglycans. In: Glauert (ed): Control of tissue damage. Elsevier, Amsterdam1988: 215–290.
36.
HardinghamTE: Proteoglycans: their structure, interactions and molecular organisation in cartilage. Biohem Sic Trans9: 489–497, 1981.
37.
LawrenceJSBremnerJMBierF: Osteoarthrosis. Prevalence in the population and relationship between symptoms and x-ray changes. Ann Rheum Dis25:1–24, 1966.
38.
LawrenceJS: Rheumatism in populations. Heinemann Medical, London1977: 1–572.
39.
LipsonSJMuirH: Proteoglycans in experimental intervertebral disc degeneration. Spine6: 194–210, 1981.
40.
LohmanderLSLarkMWDahlebergL: Cartilage matrix metabolism in osteoarthritis: markers in synovial fluid, serum and urine. Clin Biochem25: 167–174, 1992.
41.
LohmanderLSSaxneTHeinegardDK: Release of cartilage oligomeric matrix protein (COMP) into joint fluid after knee injury and in osteoarthritis. Ann Rheum Dis53: 8–13, 1994.
42.
LucheriniTCerviniC: La senescenza dei connettivi di sostegno. Relazione al «X Congr. Naz. della Società Italiana di Gerontologia e Geriatria». Gior Gerontol24: 63–151, 1961.
43.
ManganelliPSalaffiF: Le citochine:mediatori del danno cartilagineo ed osseo nelle artropatie. Il Reumatologo4: 137–143, 1992.
44.
MaroudasA: Transport through articular cartilage and some physiologic implications. In AliSYElvesMW and LeabackDH. Normal and osteoarthritic articular cartilage. Institute of Orthopaedics, London1974: 37–47.
45.
MasarykTJModicMT: Lumbar spine. In: SarkDDBradleyWGJr (eds): Magnetic Resonance Imaging. CV Mosby, St Louis1988: 666–682.
46.
MasciocchiCBarileADi PietroA: La risonanza magnetica nella patologia degenerativa della colonna vertebrale. Il Reumatologo1: 23–26, 1992.
47.
MasonRM: Recent advances in the biochemistry of hyaluronic acid in cartilage. Prog Clin Biol Res54: 87–112, 1981.
48.
McDevittCA: Proteoglycans of the intervertebral disc. In GhoshP (eds). Biology of the intervertebral disc, New York1988: 151–170.
49.
MeachimGStockwellRA: The matrix. In: Adult articular cartilage, 2nd ed. Edited by FreemanMAR. Pitman Medical, Tunbridge Wells1979.
50.
MillerEJvan der KorstJKSokoloffL: Collagen of human articular and costal cartilage. Arthritis Rheum12: 21–29, 1969.
51.
MitchellDHardinghamT: The ffects of cycloheximide on the biosynthesis and secretion of proteoglycans by chondrocytes in culture. Biochem J196: 521–529, 1981.
52.
ModicMTMasarykTJRossJS: Imaging od degenerative disk disease. Radiology168: 177–186, 1988.
53.
MortJSPooleARRoughleyPJ: Age-related changes in the structure of proteoglycan link proteins present in normal human cartilage. Biochem J196: 521–529, 1983.
54.
NeamePJChristnerJEBakerJR: Cartilage proteoglycan aggregates. The link protein and proteoglycan amino-terminal globular domains have similar structure. J Biol Chem262: 17768–17778, 1987.
55.
NietfeldJJWilbrinkB: Interleukin-1 induced interleukin-6 is required for the inhibition of proteoglycan synthesis by interleukin-1 in human articular cartilage. Arthritis Rheum33: 1695–1701, 1990.
56.
OegemaTRBradfordDS: The inter-relationship of facet joint osteoartritis and degenerative disc disease. Br J Rheumatol30 (suppl 1): 16–20, 1991.
57.
OgatonAG: The biological functions of the glycosaminoglycans. In: BalazsEA, Ed: Chemistry and Molecular Biology of the Intercellular Matrix. Vol 3. Academic Press, London1970: 1231–1232.
58.
PaulssonMMorgelinM: Extended and globular protein domains in cartilage proteoglycans. Biocchem J245: 763–772, 1987.
59.
PearceRHThompsonP: Magnetic resonance imaging reflects the chemical changes of aging degeneration in the human intervertebral disk. J Rheumatol18 (Suppl 27): 42–43, 1991.
60.
PedriniVAPonsetiIVDohrmanSC: Glycosaminoglycans of intervertebral disc in idiopathic scoliosis. J Lab Clin Med82: 938–50, 1973.
61.
PeyronJG: The epidemiology of osteoarthritis. In: MoskowitzRWHowellDS (eds): Osteoarthritis: Diagnosis and Management. WB Saunders, Philadelphia1984: 9–27.
62.
PooleAR: Immunochemical markers of joint inflammation, skeletal damage and repair: where are we now?Ann Rheum Dis53: 3–5, 1994.
63.
PooleCAFlintMHBeamountBW: Morphological and functional interrelationships of articular cartilage matrices. J Anatomy138: 113–138, 1984.
64.
RathNCOronskyALKerwarSS: Synthesis of interleukin-1-like activity by normal rat chondrocytes in culture. Cin Immunol Immunopathol47: 39–46, 1988.
65.
ReateliffeATylerJAHardinghamTE: Articular cartilage cultured with interleukin-1: Increased release of link-protein, hyaluronate-binding region and other proteoglycan fragments. Biochem J238: 571–580, 1986.
66.
RosembergLCChoiHU: Isolation of dermatan sulphate proteoglycans from mature bovine articular cartilages. J Biol Chem260: 6304–6313, 1985.
67.
RyuJTreadwellBVManchinHJ: Biochemical and metabolic abnormalities in normal and osteoarthritic human cartilage. Ann Rheum Dis41: 164–167, 1984.
68.
SalaffiFCavalieriF: Analysis of disability in knee osteoarthritis Relationship with age and psychological variables but not with radiographic score. J Rheumatol18: 1581–1586, 1991.
69.
SchmidTMLinsenmayerTF: Immunohistochemical localization of short chain cartilage collagen (type X) in avian tissues. J Cell Biol100: 598–605, 1985.
70.
SchmidtMBMowVC: Effects of proteoglycan extraction on the tensile behaviour of articular cartilage. J Orthop Res8: 353–63, 1990.
TikuMLTikuK: Production of interleukin-1 (IL-1) and inhibitor to IL-1 by articular chondrocytes. Arthritis Rheum30: S90, 1987.
76.
Van KampenGVeldhuijzenJP: Cartilage response to mechanical force in high-density chondrocyte cultures. Arthritis Rheum28: 419–424, 1985.
77.
WuJJEyreDRSlayterHS: Type VI collagen of the intervertebral disc. Biochemical and electronmicroscopic characterization of the native protein. Biochem J248: 373–81, 1987.
