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Author(s): |
Hercílio Martelli Junior
Total Authors: 1
|
Document type: | Master's Dissertation |
Press: | Piracicaba, SP. |
Institution: | Universidade Estadual de Campinas (UNICAMP). Faculdade de Odontologia de Piracicaba |
Defense date: | 2000-02-29 |
Examining board members: |
Luciano Resende Ferreira;
Heitor Panzeri;
Ricardo Della Coletta
|
Advisor: | Luciano Resende Ferreira |
Abstract | |
Study of the sinthesis of Hsp47 and Sec61??during the events of translacions/translocations of collagen type I in fibroblasts from hereditary gingival fibromatosis Hereditary Gingival Fibromatosis (HGF) represents an uncommon oral condition (l :750,000) characterized fibrous gingival enlargement. HGF can manifest as an isolated clinical entity or as part of a syndrome. The gingiva of patients with HGF produce excessive amount of collagen and other extracellular matrix. Hsp47 is an endoplasmic reticulun (ER) resident chaperone which binds specifically to collagen molecules, and Sec61? represents a transmembranous protein with active role in conducting of nascent polypeptide chain into the ER. This study describes the role of Hsp47 and Sec61? during the events of translationltranslocation of collagen type I in fibroblasts from patients with HGF and patients presenting normal gingiva (NG). Western blot assays demonstrated an increased production of Hsp47 in fibroblasts HGF as compared to NG cells under stress and unstressed conditions. In addition, Sec61? was evenly found in both cell types showing no marked variations in quantity in both stressed or unstressed situations. The more increased production of Hsp47 may related to a collagen degradation protective mechanism inside the ER. This can be one of the factors responsible for the fibrous features of HGF. Although the exact biological mechanisms involved in HGF are still unknown, the study of these ER proteins role in regulating collagen biosynthesis may be important for understanding hereditary conditions such as HGF (AU) |