Journal article
Regulation of Acidification and Apoptosis by SHP-1 and Bcl-2*
Abstract
Recruitment of the SH2 domain containing cytoplasmic protein-tyrosine phosphatase SHP-1 to the membrane by somatostatin (SST) is an early event in its antiproliferative signaling that induces intracellular acidification-dependent apoptosis in breast cancer cells. Fas ligation also induces acidification-dependent apoptosis in a manner requiring the presence of SHP-1 at the membrane. Moreover, we have recently reported that SHP-1 is required not …
Authors
Thangaraju M; Sharma K; Leber B; Andrews DW; Shen S-H; Srikant CB
Journal
Journal of Biological Chemistry, Vol. 274, No. 41, pp. 29549–29557
Publisher
Elsevier
Publication Date
October 1999
DOI
10.1074/jbc.274.41.29549
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Sustainable Development Goals (SDG)
Medical Subject Headings (MeSH)
AmilorideApoptosisCyclin D1Fas Ligand ProteinHumansHydrogen-Ion ConcentrationIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMembrane ProteinsMutationOctreotideProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2Receptors, SomatostatinSH2 Domain-Containing Protein Tyrosine PhosphatasesSignal TransductionSomatostatinTime FactorsTransfectionTumor Cells, CulturedTumor Suppressor Protein p53bcl-2-Associated X Proteinsrc Homology Domains