4.4 Article

Expression of the Small Heat Shock Protein alphaB-Crystallin in Term Human Placenta

期刊

AMERICAN JOURNAL OF REPRODUCTIVE IMMUNOLOGY
卷 60, 期 5, 页码 440-448

出版社

WILEY
DOI: 10.1111/j.1600-0897.2008.00642.x

关键词

AlphaB-crystallin; human placenta; sHsp

资金

  1. Ernst Mach Scholarship
  2. National Ministry of Education and Science [L1511/ 2005]

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Problem Expression of heat shock proteins has been described in different tissues relevant to human reproduction, including placenta. AlphaB-crystallin is a member of the small heat shock protein family (sHsp) exerting biologically important chaperon functions. Method of study Immunofluorescence; immunoblot analysis; quantitative real-time-PCR; CpG island methylation analysis. Results In this study, we once again describe the expression of alphaB-crystallin in the stroma of the placental villi and in the cytoplasm of decidual cells by immunofluorescence. In contrast, Hsp27 - another sHsp family member - was detected exclusively in the syncytiotrophoblast layer. This varying expression pattern provides additional support to earlier reports of functional differences between both proteins. Semi-quantitative immunoblot analysis of placenta tissue specimens (n = 6) revealed Hsp27 expression exceeding that of alphaB-crystallin, albeit with inter-individual variations. Inter-individual alphaB-crystallin expression variations were confirmed by quantitative RT-PCR. CpG island methylation was ruled out as the underlying cause for the inter-individual alphaB-crystallin expression variations. However, the expression extent of GATA3, which is a transcription factor with corresponding elements within the alphaB-crystallin gene (CRYAB) promoter, paralleled that of alphaB-crystallin. We demonstrated remarkable GATA3 expression in placental tissue, exceeding that of other endocrine organs. Conclusion We can conclude that the differential expression patterns of alphaB-crystallin and Hsp27 indicate functional differences between these highly related proteins in placental tissues.

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