Immunohistochemical analysis of phospho-BAD protein and mutational analysis of BAD gene in gastric carcinomas.
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.
Jeong
Eun Goo
EG
Department of Pathology, College of Medicine, The Catholic University of Korea, Seoul, Korea.
Lee
Sung Hak
SH
Kim
Sung Soo
SS
Ahn
Chang Hyeok
CH
Yoo
Nam Jin
NJ
Lee
Sug Hyung
SH
D006801:Humans; D007150:Immunohistochemistry; D009154:Mutation; D010766:Phosphorylation; D018807:Polymorphism, Single-Stranded Conformational; D013274:Stomach Neoplasms / Q000737:chemistry* / Q000235:genetics; D046888:Tissue Array Analysis; D051025:bcl-Associated Death Protein / Q000032:analysis* / Q000235:genetics*
C494819:BAD protein, human; D051025:bcl-Associated Death Protein