Publicação:
Extracellular matrix of porcine pericardium: Biochemistry and collagen architecture

dc.contributor.authorSachsida Braga-Vilela, Antonella
dc.contributor.authorRosa Pimentel, Edson
dc.contributor.authorMarangoni, Sergio
dc.contributor.authorHikari Toyama, Marcos [UNESP]
dc.contributor.authorde Campos Vidal, Benedicto
dc.contributor.institutionUniversidade Federal de Alfenas (UNIFAL)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:30:33Z
dc.date.available2014-05-20T15:30:33Z
dc.date.issued2008-01-01
dc.description.abstractPericardial tissue has been used to construct bioprostheses employed in the repair of different kinds of injuries, mostly cardiac. However, calcification and mechanical failure have been the main causes of the limited durability of cardiac bioprostheses constructed with bovine pericardium. In the course of this work, a study was conducted on porcine fibrous pericardium, its microscopic structure and biochemical nature. The general morphology and architecture of collagen were studied under conventional light and polarized light microscopy. The biochemical study of the pericardial matrix was conducted according to the following procedures: swelling test, hydroxyproline and collagen dosage, quantification of amino acids in soluble collagen, component extraction of the extracellular matrix of the right and left ventral regions of pericardium with different molarities of guanidine chloride, protein and glycosaminoglycan (GAG) dosage, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and total GAG analysis. Microscopic analysis showed collagen fibers arranged in multidirectionally oriented layers forming a closely knit web, with a larger number of fibers obliquely oriented, initiating at the lower central region toward the upper left lateral relative to the heart. No qualitative differences were found between proteins extracted from the right and left regions. Likewise, no differences were found between fresh and frozen material. Protein dosages from left frontal and right frontal pericardium regions showed no significant differences. The quantities of extracted GAGs were too small for detection by the method used. Enzymatic digestion and electrophoretic analysis showed that the GAG found is possibly dermatan sulfate. The proteoglycan showed a running standard very similar to the small proteoglycan decorin.en
dc.description.affiliationUNIFAL, Dept Biol Sci, BR-37130000 Alfenas, Minas Gerais, Brazil
dc.description.affiliationUniv Estadual Campinas, Dept Cell Biol, São Paulo, Brazil
dc.description.affiliationUniv Estadual Campinas, Dept Biochem, São Paulo, Brazil
dc.description.affiliationUniv Estadual Paulista, CLP SV, Dept Biochem, São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, CLP SV, Dept Biochem, São Paulo, Brazil
dc.format.extent15-25
dc.identifierhttp://dx.doi.org/10.1007/s00232-007-9081-5
dc.identifier.citationJournal of Membrane Biology. New York: Springer, v. 221, n. 1, p. 15-25, 2008.
dc.identifier.doi10.1007/s00232-007-9081-5
dc.identifier.issn0022-2631
dc.identifier.urihttp://hdl.handle.net/11449/39896
dc.identifier.wosWOS:000252279100003
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofJournal of Membrane Biology
dc.relation.ispartofjcr1.638
dc.relation.ispartofsjr0,567
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectextracellular matrixen
dc.subjectporcine pericardiumen
dc.subjectcollagenen
dc.subjectproteoglycan glycosaminoglycanen
dc.subjectbioprosthesisen
dc.titleExtracellular matrix of porcine pericardium: Biochemistry and collagen architectureen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer
dspace.entity.typePublication

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