Artículos de revistas
Ultrastructural, Immunohistochemical And Biochemical Analysis Of Glycosaminoglycans And Proteoglycans In The Mouse Pubic Symphysis During Pregnancy
Registro en:
Cell Biology International. , v. 29, n. 6, p. 458 - 471, 2005.
10656995
10.1016/j.cellbi.2004.11.025
2-s2.0-23044495802
Autor
Pinheiro M.C.
Mora O.A.
Caldini E.G.
Battlehner C.N.
Joazeiro P.P.
Toledo O.M.S.
Institución
Resumen
During pregnancy, an interpubic ligament is formed in the mouse pubic symphysis. In late stages, this ligament undergoes "relaxation" to allow proper delivery, which is expected on the 19th day. Proteoglycans and hyaluronic acid play an important role in the remodeling of the extracellular matrix in these tissues. Glycosaminoglycans and proteoglycans were studied by electron microscopic, immunohistochemical and biochemical methods in samples of mouse pubic symphysis from the 12th to 18th day of pregnancy. At the ultrastructural level, using cuprolinic blue and enzymatic digestion by chondroitin lyases, two types of proteoglycan filaments were observed in the fibrocartilage on the 12th day, as well as in D15, D17 and D18 pubic ligaments. The only sulfated glycosaminoglycan in these filaments was chondroitin sulfate, as shown by chondroitin lyase treatment. Their electrophoretic mobility, before and after enzymatic degradation, corroborated this inference. The ratio of chondroitin sulfate/dry weight of symphysis showed two phases of increase: between D12 and D15, and between D17 and D18. We suggest that the first corresponds mainly to an increase in decorin when the ligament is formed, and the second to versican, during "relaxation". Versican and hyaluronic acid, working as water holding molecules would be responsible for the hydration of the ligament at the end of pregnancy, allowing an increase in resiliency. The presence of hyaluronic acid was confirmed by labeling with HA-probe in the perichondrium, fibrocartilage and ligament. The role of collagen fibers as physical restrictors of the complete expansion of glycosaminoglycans and hyaluronic acid in tissue is discussed. © 2005 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved. 29 6 458 471 Caterson, B., Baker, J.R., Christner, J.E., Couchman, J.R., Immunological methods for the detection and determination of connective tissue proteoglycans (1982) J Invest Dermatol, 79, pp. 45-50 Crelin, E.S., Newton, E.V., The pelvis of the free-tailed bat: Sexual dimorphism and pregnancy changes (1969) Anat Rec, 164, pp. 349-357 Cribb, A.M., Scott, J.E., Tendon response to tensile stress: An ultrastructural investigation of collagen:proteoglycan interactions in stressed tendon (1995) J Anat, 187, pp. 423-428 Culav, E.M., Clark, C.H., Merrilees, M.J., Connective tissues: Matrix composition and its relevance to physical therapy (1999) Phys Ther, 79, pp. 308-319 Dietrich, C.P., Dietrich, S.M., Electrophoretic behavior of acidic mucopolysaccharides in diamine buffers (1976) Anal Biochem, 70, pp. 645-647 Fleischmajer, R., Fisher, L.W., MacDonald, E.D., Jacobs Jr., L., Perslish, J.S., Termine, J.D., Decorin interacts with fibrillar collagen of embryonic and adult human skin (1991) J Struct Biol, 106, pp. 82-90 Frieden, E.H., Hisaw, F.L., The mechanism of symphyseal relaxation. the distribution of reducing groups, hexosamine, and proteins in symphyses of normal and relaxed guinea pigs (1951) Endocrinology, 48, pp. 88-97 Gamble, J.C., Simmons, S.C., Freedman, M., The symphisis pubis. Anatomic and pathologic considerations (1986) Clin Orthop, 203, pp. 261-272 Grabbe, K.J., Shelton, J.M., Richardson, J.A., Hascall, V.C., Mahendroo, M.S., Regulation of hyaluronan expression during cervical ripening (2004) Glycobiology Grande-Allen, K.J., Calabro, A., Gupta, V., Wight, T.N., Hascall, V.C., Vesely, I., Glycosaminoglycans and proteoglycans in normal mitral valve leaflets and chordae: Association with regions of tensile and compressive loading (2004) Glycobiology, 14, pp. 621-633 Hall, K., The effects of pregnancy and relaxin on the histology of the pubic symphysis in the mouse (1947) J Endocrinol, 5, pp. 174-182 Hardinghan, T.E., Fosang, A.J., Proteoglycans: Many forms and many functions (1992) FASEB J, 6, pp. 861-870 Horn, E.H., Interpubic ligament regression in relaxin-treated virgin and primiparous, post-partum mice (1960) Endocrinology, 67, pp. 668-673 Huijing, P.A., Muscle as a collagen fiber reinforced composite: A review of force transmission in muscle and whole limb (1999) J Biomech, 32, pp. 329-345 Iozzo, R.V., Matrix proteoglycans: From molecular design to cellular function (1998) Annu Rev Biochem, 67, pp. 609-652 Kaneko, S., Ohashi, K., Soma, K., Yanagishita, M., Occlusal hypofunction causes changes of proteoglycan content in the rat periodontal ligament (2001) J Periodontal Res, 36, pp. 9-17 Manning, J.P., Steinetz, B.G., Butler, M.C., Priester, S., The effect of steroids and relaxin on acid phosphatase in the pubic symphysis of the ovariectomized mouse (1965) J Endocrinol, 33, pp. 501-506 Neame, P.J., Kay, C.J., McQuillan, D.J., Beales, M.P., Hassel, J.R., Independent modulation of collagen fibrillogenesis by decorin and lumican (2000) Cell Mol Life Sci, 57, pp. 859-863 Ohya, T., Kaneko, Y., Novel hyaluronidase from streptomyces (1970) Biochim Biophys Acta, 198, pp. 607-609 Ortega, H.H., Joazeiro, P.P., Muñoz-De-Toro, M.M., Luque, E.H., Montes, G.S., Differential distribution of the fibers of the collagenous and elastic systems and of glycosaminoglycans in the rat pubic joint (2001) J Submicrosc Cytol Pathol, 33, pp. 463-472 Parry, D.A.D., Craig, A.S., Collagen fibrils during development and maturation and their contribution to the mechanical attributes of connective tissue (1988) Collagen, 2, pp. 1-23. , M.E. Nimni CRC Press Boca-Raton Perl, E., Catchpole, H.R., Changes induced in the connective tissue of the pubic symphysis of the guinea pig with estrogen and relaxin (1950) Arch Pathol, 50, pp. 223-239 Pinheiro, M.C., Joazeiro, P.P., Mora, O.A., Toledo, O.M., Ultrastructural and immunohistochemical analysis of proteoglycans in mouse pubic symphysis (2003) Cell Biol Int, 27, pp. 647-655 Pinheiro, M.C., Moraes, D.G., Battlehner, C.N., Caldini, E.G., Toledo, O.M.S., Joazeiro, P.P., Histochemical and ultrastructural study of collagen fibers in mouse pubic symphysis during pregnancy (2004) Micron, 35, pp. 685-693 Pins, G.D., Christiansen, D.L., Patel, R., Silver, F.H., Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties (1997) Biophys J, 73, pp. 2164-2172 Ruth, E.B., Metamorphosis of the pubic symphysis III. Histological changes in the symphysis of the pregnant guinea pig (1937) Anat Rec, 67, pp. 409-421 Saito, N., Yamagata, T., Suzuki, S., Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfate (1968) J Biol Chem, 243, pp. 1536-1544 Samuel, C.S., Coghlan, J.P., Bateman, J.F., Effects of relaxin, pregnancy and parturition on collagen metabolism in the rat pubic symphysis (1980) J Endocrinol, 159, pp. 117-125 Schwabe, C., Steinetz, B., Weiss, G., Segaloff, A., MacDonald, J.K., O'Byrne, E., Relaxin (1978) Recent Prog Horm Res, 34, pp. 123-211 Scott, J.E., Collagen-proteoglycan interaction. Localization of proteoglycans in tendon by electron microscopy (1980) Biochem J, 187, pp. 877-891 Scott, J.E., Haigh, M., Proteoglycan-collagen interactions in intervertebral disc. a chondroitin sulphate proteoglycan associates with collagen fibrils in rabbit annulus fibrosus at the d-e bands (1986) Biosci Rep, 6, pp. 879-888 Sherwood, O.D., Relaxin (1994) The Physiology of Reproduction, 2, pp. 861-1009. , E. Knobil J.D. Neill Raven Press New York Steinetz, B.G., Manning, J.P., Butler, M., Beach, V.L., Relationships of growth hormones, steroids and relaxin in the transformation of pubic joint cartilage to ligament in hypophysectomized mice (1965) Endocrinology, 76, pp. 876-882 Storey, E., Relaxation in the pubic symphysis of the mouse during pregnancy and after relaxin administration, with special reference to the behavior of collagen (1957) J Pathol Bacteriol, 74, pp. 147-162 Talmage, R.V., Changes produced in the symphyseal pubis of guinea pig by the sex steroids and relaxin (1947) Anat Rec, 99, pp. 91-113 Talmage, R.V., A histological study of the effects of relaxin on the symphysis pubis of the guinea pig (1947) J Exp Zool, 106, pp. 281-292 Toledo, O.M.S., Marquezini, M.V., Jia, K.B., Pinheiro, M.C., Mora, O.A., Biochemical and cytochemical characterization of extracellular proteoglycans in the inner circular smooth muscle layer of dog small intestine (2002) IUBMB Life, 54, pp. 19-25 Toledo, O.M.S., Mourão, P.A.S., Sulfated glycosaminoglycans of human aorta: Chondroitin 6-sulfate increase with age (1979) Biochem Biophys Res Commun, 89, pp. 50-55 Viell, B., Struck, H., Effects of the hormone relaxin on the metabolism of glycosaminoglycans in the mouse symphysis pubis (1987) Horm Metab Res, 19, pp. 415-418 Young, M.F., Bi, Y., Ameye, L., Chen, X.-D., Biglycan knockout mice: New models for musculoskeletal diseases (2003) Glycoconj J, 19, pp. 257-262 Zhao, L., Samuel, C.S., Tregear, G.W., Bech, F., Wintour, E.M., Collagen studies in late pregnant relaxin null mice (2000) Biol Reprod, 63, pp. 697-703