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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/69536
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dc.contributor.authorDelella, Flávia K.-
dc.contributor.authorJustulin Jr., Luis A.-
dc.contributor.authorFelisbino, Sérgio L.-
dc.date.accessioned2014-05-27T11:22:24Z-
dc.date.accessioned2016-10-25T18:23:36Z-
dc.date.available2014-05-27T11:22:24Z-
dc.date.available2016-10-25T18:23:36Z-
dc.date.issued2007-03-01-
dc.identifierhttp://dx.doi.org/10.1016/j.cellbi.2006.10.004-
dc.identifier.citationCell Biology International, v. 31, n. 3, p. 229-234, 2007.-
dc.identifier.issn1065-6995-
dc.identifier.urihttp://hdl.handle.net/11449/69536-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/69536-
dc.description.abstractMatrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) play a major role in extracellular matrix component degradation in several normal and abnormal tissue situations; they are also found in human seminal plasma. MMPs have been found in rat prostate secretions and are nearly lobe specific in expression pattern. The aim of this study was to evaluate whether TIMP-2, like other semen components, is expressed differently from different rat prostatic lobes. Immunohistochemical staining was performed in both young and adult rat ventral (VP), lateral (LP), dorsal (DP), and anterior (AP) prostatic lobes and confirmed by western blotting. TIMP-2 expression was found in the epithelial cells in the following sequence: LP > AP > DP > VP, in both young and adult rats. In this study, 100% of adult LP presented histological signs of prostatitis, where TIMP-2 immunostaining was positive in normal epithelium even with intraluminal neutrophils, but was reduced or absent in the epithelium with intraepithelial leukocytes or with periductal stroma disorganization associated with mononuclear cell infiltration. However, TIMP-2 expression in LP was not induced by prostatitis, since younger rat LPs were also strongly TIMP-2 positive. The distal and intermediate VP regions were TIMP-2 negative, but the proximal regions were strongly stained. Western blotting results confirmed the high TIMP-2 expression in the LP lobe. Thus, TIMP-2 is expressed differently between the prostatic lobes and is another nearly lobe-specific protein, which plays a role in the regulation of MMP activity in seminal plasma and glandular homeostasis. TIMP-2 is also another regional ductal variation of VP. Further studies should address whether TIMP-2 expression is related to the highest incidence of rat LP prostatitis and adenocarcinoma. © 2006 International Federation for Cell Biology.en
dc.format.extent229-234-
dc.language.isoeng-
dc.sourceScopus-
dc.subjectCollagen fiber-
dc.subjectMetalloproteinase-
dc.subjectProstate-
dc.subjectProstatitis-
dc.subjectSeminal plasma-
dc.subjectTissue inhibitor of metalloproteinase-
dc.subjectmatrix metalloproteinase-
dc.subjecttissue inhibitor of metalloproteinase 2-
dc.subjectadenocarcinoma-
dc.subjectanimal tissue-
dc.subjectcell separation-
dc.subjectcontrolled study-
dc.subjectenzyme regulation-
dc.subjecthomeostasis-
dc.subjectimmunohistochemistry-
dc.subjectleukocyte-
dc.subjectmale-
dc.subjectmononuclear cell-
dc.subjectneutrophil-
dc.subjectnonhuman-
dc.subjectprostate-
dc.subjectprostate anterior lobe-
dc.subjectprostate dorsal lobe-
dc.subjectprostate epithelium-
dc.subjectprostate lateral lobe-
dc.subjectprostate ventral lobe-
dc.subjectprostatitis-
dc.subjectprotein analysis-
dc.subjectprotein content-
dc.subjectprotein expression-
dc.subjectprotein induction-
dc.subjectprotein localization-
dc.subjectrat-
dc.subjectregulatory mechanism-
dc.subjectseminal plasma-
dc.subjectstroma cell-
dc.subjectWestern blotting-
dc.subjectAging-
dc.subjectAnimals-
dc.subjectBlotting, Western-
dc.subjectImmunohistochemistry-
dc.subjectMale-
dc.subjectRats-
dc.subjectRats, Wistar-
dc.subjectTissue Inhibitor of Metalloproteinase-2-
dc.subjectRattus-
dc.titleTissue inhibitor of metalloproteinase-2 (TIMP-2) location in the ventral, lateral, dorsal and anterior lobes of rat prostate by immunohistochemistryen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationDepartment of Cell Biology Institute of Biology State University of Campinas (UNICAMP), Campinas, SP-
dc.description.affiliationDepartment of Morphology Institute of Biosciences São Paulo State University (UNESP), Box 510, 18618-000 Botucatu, SP-
dc.description.affiliationUnespDepartment of Morphology Institute of Biosciences São Paulo State University (UNESP), Box 510, 18618-000 Botucatu, SP-
dc.identifier.doi10.1016/j.cellbi.2006.10.004-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofCell Biology International-
dc.identifier.scopus2-s2.0-33847022254-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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