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Immunohistochemical analysis of phospho-BAD protein and mutational analysis of BAD gene in gastric carcinomas.

Abstract
Mounting evidence indicates that deregulation of apoptosis contributes to the development of human cancers. BAD, a proapoptotic Bcl-2 family protein, regulates the intrinsic apoptosis pathway. The aim of this study was to explore whether alterations of phospho-BAD (p-BAD) protein that antagonizes apoptosis function of BAD and mutation of BAD gene are characteristics of human gastric cancers. We analyzed expression of p-BAD in 60 gastric adenocarcinomas by immunohistochemistry. Also, we analyzed BAD gene for detection of somatic mutations by single-strand conformation polymorphism (SSCP) assay. p-BAD expression was detected well in normal gastric mucosal epithelial cells, whereas it was detected in only 51% (31 of the 60) of the cancers. There was no somatic mutation of BAD gene in the 60 gastric cancer samples. The decreased expression of p-BAD in malignant gastric epithelial cells compared to normal mucosal epithelial cells suggested that loss of p-BAD expression may play a role in gastric tumorigenesis. The data also suggest that BAD mutation may not be a direct target of inactivation in gastric tumorigenesis.
AuthorsEun Goo Jeong, Sung Hak Lee, Sung Soo Kim, Chang Hyeok Ahn, Nam Jin Yoo, Sug Hyung Lee
JournalAPMIS : acta pathologica, microbiologica, et immunologica Scandinavica (APMIS) Vol. 115 Issue 8 Pg. 976-81 (Aug 2007) ISSN: 0903-4641 [Print] Denmark
PMID17696955 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • BAD protein, human
  • bcl-Associated Death Protein
Topics
  • Humans
  • Immunohistochemistry
  • Mutation
  • Phosphorylation
  • Polymorphism, Single-Stranded Conformational
  • Stomach Neoplasms (chemistry, genetics)
  • Tissue Array Analysis
  • bcl-Associated Death Protein (analysis, genetics)

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