Artículos de revistas
In Vitro Rapid Organization Of Rabbit Meniscus Fibrochondrocytes Into Chondro-like Tissue Structures
Registro en:
Journal Of Submicroscopic Cytology And Pathology. , v. 34, n. 3, p. 335 - 343, 2002.
11229497
2-s2.0-0036652210
Autor
Araujo V.G.
Figueiredo C.A.
Joazeiro P.P.
Mora O.A.
Toledo O.M.S.
Institución
Resumen
We described the behaviour of 120 days rabbit knee-meniscus cells in monolayer culture. The cells were grown forming cellular aggregates resembling true cellular nodules. Three stages of development of these nodules could be observed: formation of the cellular nodules between days 1 and 3; nodular growth, with their maximal at day 5; and nodular regression beginning at day 8. Ultrastructural analysis of the extracellular matrix of these cellular nodules was assessed on days 3, 5 and 8. At the formation stage, we could observe striated collagen fibrils and small bundles of tubular microfibrils either interspersed with very low quantities of amorphous elastin, being morphologically identical to elaunin fibers, or without only trace of elastin, being morphologically identical to oxytalan fibers. By day 5, fibrillar elements with 100 nm periodic ladder-like collagen VI fibrillar aggregates could also be detected. At day 8, the striated collagen fibrils and oxytalan fibers could not be observed. During this same period, there was an increase of a dense matrix comprised of collagen VI and mature elastic fibers. Chondroitin/dermatan sulfate proteoglycans were synthesized and became essential for the arrangement of collagen type VI, since chondroitinase ABC treatment of the culture disrupted collagen VI assembly, associated with the large spaces near the cell surface. In addition, the cells lost their fusiform morphology and changed into rounded cells. The results show that primary cultures of rabbit meniscus fibrochondrocytes maintain their capacity to form chondro-like structures in vitro. The organization process was rapid and uniform throughout the entire culture presuming that the normal signal transduction pathways are maintained intact and that essential factors in some phases of tissue organization are present. 34 3 335 343 Aagaard, H., Verdonk, Function of the normal meniscus and consequences of meniscal resection (1999) Scand. J. Med. Sports, 9, pp. 134-140 Bidanset, D.J., Guidry, C., Rosenberg, L.C., Choi, H.U., Timpl, R., Hook, M., Binding of the proteoglycan decorin to collagen type VI (1992) J. Biol. Chem., 267, pp. 5250-5256 Burg, M.A., Nishiyama, A., Stallcup, W.B., A central segment of the NG2 proteoglycan is critical for the ability of glioma cells to bind and migrate toward type VI collagen (1997) Exp. Cell. Res., 235, pp. 254-264 Calvo, E., Palacios, I., Delgado, E., Ruiz-Cabello, J., Hernandez, P., Sanchez-Pernaute, O., Egido, J., Herrero-Beaumont, G., High-resolution MRI detects cartilage swelling at the early stages of experimental osteoarthritis (2001) Osteoarthr. Cartil., 9, pp. 463-472 Cotta-Pereira, G., Rodrigo, F.G., Fereira, D.J.F., The elastic system fibers (1977) Adv. Exp. Med. Biol., 79, pp. 10-30 Culav, E.M., Clark, C.H., Merrilees, M.J., Connective tissues: Composition and its relevance to physical therapy (1999) Phys. Ther., 79, pp. 308-319 Eyre, D.R., Wu, J.J., Collagen of fibrocartilage: A distinctive molecular phenotype in bovine meniscus (1983) FEBS Lett., 25, pp. 265-270 Finnis, M.L., Gibson, M.A., Microfibril-associated glycoproteins-1 (MAGP-1) binds to the pepsin-resistant domain of die α3(VI) chain of type VI (1997) J. Biol. Chem., 272, pp. 22817-22823 Ghadially, F.N., Thomas, I., Yong, N., Lalonde, J.M., Ultrastructure of rabbit semilunar cartilages (1978) J. Anat., 125, pp. 499-517 Heise, N., Toledo, O.M.S., Rabbit-knee-joint meniscal proteoglycans (1994) Biochem. Mol. Biol. Int., 32, pp. 491-499 Hunziker, E.B., Hermann, W., Schenk, R.K., Ruthenium hexammine trichloride (RHT) mediated interaction between plasmalemmal components and pericellular matrix proteoglycans is responsible for the preservation of chondrocytic plasma membranes in situ during cartilage fixation (1983) J. Histochem. Cytochem., 31, pp. 717-727 Isoda, K., Saito, S., In vitro and in vivo fibrochondrocytes growth behavior in fibrin gel: An immunohistochemical study in the rabbit (1998) Am. J. Knee Surg., 11, pp. 209-216 Jones, R.E., Smith, E.C., Reisch, J.S., Effects of medial meniscectomy in patients older than forty years (1978) J. Bone Joint Surg. Am., 60, pp. 783-786 Keene, D.R., Ridgway, C.C., Iozzo, R.V., Type VI microfilaments interact with a specific region of banded collagen fibrils in skin (1998) J. Histochem. Cytochem., 46, pp. 215-220 Kiraly, K., Hyttinen, M.M., Parkkinen, J.J., Arokoski, J.A., Lapvetelainen, T., Torronen, K., Kiviranta, I., Helminen, H.J., Articular cartilage collagen birefringence is altered concurrent with changes in proteoglycan synthesis during dynamic in vitro loading (1998) Anat. Rec., 251, pp. 28-36 Klein, G., Muller, C.A., Tillet, E., Chu, M.L., Timpl, R., Collagen type VI in the human bone marrow microenvironment: A strong cytoadhesive component (1995) Blood, 86, pp. 1740-1748 Knee, D.R., Engvall, E., Glanville, R.W., Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous nerwork (1988) J. Cell. Biol., 107, pp. 1995-2006 McDevitt, C.A., Webber, R.J., The ultrastructure and biochemistry of meniscal cartilage (1990) Clin. Orthop., 252, pp. 8-18 Nakamura, M., Kimura, S., Kobayashi, M., Hirano, K., Hoshino, T., Awaya, S., Type VI collagen bound to collagen fibrils by chondroitin/dermaran sulfate glycosammoglycan in mouse corneal stroma (1997) Jpn. J. Ophthalmol., 41, pp. 71-76 Nishiyama, A., Stallcup, W.B., Expression of NG2 proteoglycan causes retention of type VI collagen on the cell surface (1993) Mol. Biol. Cell., 4, pp. 1097-1108 Okada, Y., Naka, K., Minamoto, T., Ueda, Y., Oda, Y., Nakanishi, I., Timpl, R., Localization of type VI collagen in the lining cell layer of normal and rheumatoid synovium (1990) Lab. Invest., 63, pp. 647-656 Poole, C.A., Ayad, S., Gilbert, R.T., Chondrons from articular cartilage. V. Immunohistochemical evaluation of type VI collagen organisation in isolated chondrons by light, confocal and electron microscopy (1992) J. Cell. Sci., 103, pp. 1101-1110 Reinboth, B.J., Finnis, M.L., Gibson, M.A., Sandberg, L.B., Cleary, E.G., Development expression of dermatan sulfate proteoglycans in the elastic bovine nuchal ligament (2000) Matrix Biol., 19, pp. 149-162 Roughley, P.J., White, R.J., The dermatan sulfate proteoglycans of the adult human meniscus (1992) J. Orthop. Res., 10, pp. 621-630 Roughley, P.J., McNicol, D., Santer, V., Buckwalter, J., The presence of a cartilage-like proteoglycan in the adult human meniscus (1981) Biochem. J., 197, pp. 77-83 Saamanen, A.M., Puustjarvi, K., Ilves, K., Lammi, M., Kiviranta, I., Jurvelin, J., Helminen, H.J., Tammi, M., Effect of running exercise on proteoglycans and collagen content in the intervertebral disc of young dogs (1993) Int. J. Sports Med., 14, pp. 48-51 Smith, R.L., Trindade, M.C., Ikenoue, T., Mohtai, M., Das, P., Carter, D.R., Goodman, S.B., Schurman, D.J., Effects of shear stress on articular chondrocyte metabolism (2000) Biorheology, 37, pp. 95-107 Tanaka, T., Fujii, K., Kumagae, Y., Compaction of biochemical charactetistics of cultured fibrochondrocytes isolated from the inner and outer regions of human meniscus (1999) Knee Surg. Sports. Traumatol. Arthrosc., 7, pp. 75-80 Toledo, O.M.S., Taniwaki, N.N., Saldiva, P.H.N., Montes, G.S., Effect of aqueous and nonaqueous fixatives on the quantitative estimation of collagen-proteoglycan interaction in tissue sections (1996) Biotech. Histochem., 71, pp. 109-114 Trask, B.C., Trask, T.M., Broekelmann, T., Mecham, R.P., The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin (2000) Mol. Biol. Cell., 11, pp. 1499-1507 Webber, R.J., Harris, M.G., Hough Jr., A.J., Cell culture of rabbit meniscal fibrochondrocytes: Proliferative and synthetic response to growth factors and ascorbare (1985) J. Orthop. Res., 3, pp. 36-42 Webber, R.J., Norby, D.P., Malemud, C.J., Goldberg, V.M., Moskowitz, R.W., Characterization of newly synthesized proteoglycans from rabbit menisci in organ culture (1984) Biochem. J., 221, pp. 875-884 Wu, X.X., Gordon, R.E., Glanville, R.W., Kuo, H.J., Uson, R.R., Rand, J.H., Morphological reladonships of von Willebrand factor, type VI collagen, and fibrillin in human vascular subendothelium (1996) Am. J. Pathol., 149, pp. 283-291 Yamada, K., The effect of digestion with Streptomyces hyaluronidase upon certain histochemical reactions of hyaluronic acid-containing tissues (1973) J. Histochem. Cytochem., 21, pp. 794-803 Yasue, K., Kobayashi, M., Hattori, H., Teramoto, T., Senga, K., Mizutani, H., Ueda, M., Hoshino, T., An ultrastructural study of extracellular fibrillar components of developing mouse mandibular condyle with special reference to type VI collagen (1994) Arch. Oral Biol., 39, pp. 689-694