The Protein-tyrosine Phosphatase SHP-2 Is Required during Angiotensin II-mediated Activation of Cyclin D1 Promoter in CHO-AT1A Cells

Autor: Arlette Levy, Bernard Rothhut, Laurent Guillemot, Zhizhuang Joe Zhao, Gilbert Béréziat
Rok vydání: 2000
Předmět:
Transcriptional Activation
MAPK/ERK pathway
SH2 Domain-Containing Protein Tyrosine Phosphatases
Cyclin D
Cyclin A
Protein Tyrosine Phosphatase
Non-Receptor Type 11

CHO Cells
Biology
Biochemistry
Catalysis
Receptor
Angiotensin
Type 1

S Phase
Proto-Oncogene Proteins p21(ras)
src Homology Domains
Phosphatidylinositol 3-Kinases
chemistry.chemical_compound
Cyclin D1
Cricetinae
Animals
Humans
Promoter Regions
Genetic

Molecular Biology
Protein Tyrosine Phosphatase
Non-Receptor Type 1

Receptors
Angiotensin

Angiotensin II
Protein Tyrosine Phosphatase
Non-Receptor Type 6

G1 Phase
Intracellular Signaling Peptides and Proteins
Tyrosine phosphorylation
Cell Biology
Molecular biology
Rats
Proto-Oncogene Proteins c-raf
Gene Expression Regulation
chemistry
biology.protein
Cyclin-dependent kinase complex
Mitogen-Activated Protein Kinases
Protein Tyrosine Phosphatases
Cyclin A2
Zdroj: Journal of Biological Chemistry. 275:26349-26358
ISSN: 0021-9258
DOI: 10.1074/jbc.m001614200
Popis: Angiotensin II (Ang II) binds to specific G protein-coupled receptors and is mitogenic in Chinese hamster ovary (CHO) cells stably expressing a rat vascular angiotensin II type 1A receptor (CHO-AT(1A)). Cyclin D1 protein expression is regulated by mitogens, and its assembly with the cyclin-dependent kinases induces phosphorylation of the retinoblastoma protein pRb, a critical step in G(1) to S phase cell cycle progression contributing to the proliferative responses. In the present study, we found that in CHO-AT(1A) cells, Ang II induced a rapid and reversible tyrosine phosphorylation of various intracellular proteins including the protein-tyrosine phosphatase SHP-2. Ang II also induced cyclin D1 protein expression in a phosphatidylinositol 3-kinase and mitogen-activated protein kinase/extracellular signal-regulated kinase (MAPK/ERK)-dependent manner. Using a pharmacological and a co-transfection approach, we found that p21(ras), Raf-1, phosphatidylinositol 3-kinase and also the catalytic activity of SHP-2 and its Src homology 2 domains are required for cyclin D1 promoter/reporter gene activation by Ang II through the regulation of MAPK/ERK activity. Our findings suggest for the first time that SHP-2 could play an important role in the regulation of a gene involved in the control of cell cycle progression resulting from stimulation of a G protein-coupled receptor independently of epidermal growth factor receptor transactivation.
Databáze: OpenAIRE