Structure and proteoglycan composition of specialized regions of the elastic tendon of the chicken wing

dc.creatorCarvalho, HF
dc.creatorFelisbino, SL
dc.creatorCovizi, DZ
dc.creatorDella Colleta, HHM
dc.creatorGomes, L
dc.date2000
dc.dateJUN
dc.date2014-12-02T16:30:19Z
dc.date2015-11-26T16:44:09Z
dc.date2014-12-02T16:30:19Z
dc.date2015-11-26T16:44:09Z
dc.date.accessioned2018-03-28T23:29:24Z
dc.date.available2018-03-28T23:29:24Z
dc.identifierCell And Tissue Research. Springer Verlag, v. 300, n. 3, n. 435, n. 446, 2000.
dc.identifier0302-766X
dc.identifierWOS:000088183200009
dc.identifier10.1007/s004410000220
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/75365
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/75365
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/75365
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1273826
dc.descriptionThe elastic tendon(1) of the avian wing has been described by others as a unique structure with elastic properties due to the predominance of elastic fibers in the midsubstance. Further analyses of the tendon have shown it to possess five anatomically distinct regions. Besides the major elastic region, a distally located fibrocartilage and three tendinous regions are present. The tendinous regions connect: (1) the muscle to the elastic region, (2) the elastic region to the fibrocartilage and (3) the latter to the insertion site. The elastic region possesses thick and abundant elastic fibers and Very thin, interconnecting collagen fibers. The collagen fibers in the sesamoid fibrocartilage are thick and interwoven, defining spaces occupied by fibrochondrocytes embedded in a non-fibrillar and highly metachromatic matrix. Biochemical analyses have shown that the fibrocartilage has about tenfold the amount of glycosaminoglycans (GAGs) found in the other regions. The main GAG in this region was chondroitin sulfate (CS) (plus keratan sulfate as detected immunocytochemically), while the other regions showed variable amounts of CS, dermatan sulfate (DS) and heparan sulfate. Further analyses have shown that a large CS-bearing proteoglycan is found in the fibrocartilage. The elastic region possesses two main proteoglycans, a large CS-bearing proteoglycan (which reacted with an antibody against keratan sulfate after chondroitinase ABC treatment) and a predominant DS-bearing proteoglycan, which showed immunoreactivity when assayed with an anti-biglycan antibody. The results demonstrate that the elastic tendon is a complex structure with complex regional structural and compositional adaptations, suited to different biomechanical roles.
dc.description300
dc.description3
dc.description435
dc.description446
dc.languageen
dc.publisherSpringer Verlag
dc.publisherNew York
dc.publisherEUA
dc.relationCell And Tissue Research
dc.relationCell Tissue Res.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectelastic tendon
dc.subjectelastin
dc.subjectfibrocartilage
dc.subjectproteoglycans
dc.subjecttendon structure
dc.subjectchicken
dc.subjectDigitorum Profundus Tendon
dc.subjectAdult Bovine Tendon
dc.subjectSulfated Glycosaminoglycans
dc.subjectAcidic Mucopolysaccharides
dc.subjectFibroblast-cultures
dc.subjectMechanical Forces
dc.subjectTannic-acid
dc.subjectAge
dc.subjectFibrocartilages
dc.subjectIdentification
dc.titleStructure and proteoglycan composition of specialized regions of the elastic tendon of the chicken wing
dc.typeArtículos de revistas


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