Increase in expression of Hsp47 and collagen in hereditary gingival fibromatosis is modulated by stress and terminal procollagen N-propeptides

dc.creatorDella Coletta, R
dc.creatorAlmeida, OP
dc.creatorFerreira, LR
dc.creatorReynolds, MA
dc.creatorSauk, JJ
dc.date1999
dc.date2014-07-30T14:33:07Z
dc.date2015-11-26T16:32:01Z
dc.date2014-07-30T14:33:07Z
dc.date2015-11-26T16:32:01Z
dc.date.accessioned2018-03-28T23:13:17Z
dc.date.available2018-03-28T23:13:17Z
dc.identifierConnective Tissue Research. Gordon Breach Sci Publ Ltd, v. 40, n. 4, n. 237, n. +, 1999.
dc.identifier0300-8207
dc.identifierWOS:000083939900001
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/59997
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/59997
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1270368
dc.descriptionHGF is a rare oral condition characterized by a slow, progressive enlargement of the gingiva, involving both the maxilla and mandible. HGF provides a model for the study of regulatory features of conditions characterized by connective tissue hyperplasia, In this study, the culture characteristics of gingival fibroblasts derived from patients of the same family with HGF (n = 4) were similar with regard to cell cycle analysis. Flow cytometric DNA content analysis revealed uniform DNA diploidy for fibroblasts cultured from NG and HGF. NG cells showed a low S-phase fraction (19.8%) and G(2)/M fraction (5.8%) and a relatively high G(1) phase fraction (74%), In contrast, HGF cells from all members of the tested kindred, exhibited diploid cells with a higher S-phase (40.9%) and G2/M (10.1%) fraction and a relatively low G1 phase fraction (40.9%). Furthermore, we demonstrated that the expression and production of Hsp47 parallels the increased levels of collagen secretion observed in HGF. In addition, we show that Hsp47 and collagen are coordinately regulated following stress via a feedback mechanism mediated by N-terminal procollagen propeptides. Utilizing confocal microscopy and antibodies directed against GST-fusion proteins encompassing the pro alpha 1(I) N-propeptide globular domain (NP1) (residues 23-108), it was apparent that this regulatory mechanism does not involve significant interaction with Hsp47's chaperoning of procollagen.
dc.description40
dc.description4
dc.description237
dc.description+
dc.languageen
dc.publisherGordon Breach Sci Publ Ltd
dc.publisherReading
dc.publisherInglaterra
dc.relationConnective Tissue Research
dc.relationConnect. Tissue Res.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectHsp47
dc.subjectcollagen
dc.subjecthereditary gingival fibromatosis
dc.subjectN-terminal propeptides
dc.subjectstress
dc.subjectShock Protein Hsp47
dc.subjectEndoplasmic-reticulum
dc.subjectMolecular Chaperones
dc.subjectBinding Protein
dc.subjectI Collagen
dc.subjectFibroblasts
dc.subjectGene
dc.subjectRat
dc.subjectHeat-shock-protein-47
dc.subjectGlomerulonephritis
dc.titleIncrease in expression of Hsp47 and collagen in hereditary gingival fibromatosis is modulated by stress and terminal procollagen N-propeptides
dc.typeArtículos de revistas


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