S. Bardhan
Vanderbilt University
16 Papers
269 Citations
S. Bardhan is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Angiotensin receptor & Angiotensin II. The author has an hindex of 13, co-authored 16 publications.
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Papers
Cloning and expression of a complementary DNA encoding a bovine adrenal angiotensin II type-1 receptor
Kazuyuki Sasaki,Yamano Y,S. Bardhan,Naoharu Iwai,Murray Jj,M. Hasegawa,Y. Matsuda,Tadashi Inagami +7 more
TL;DR: The expression cloning of a complementary DNA encoding a bovine angiotensin II receptor is reported to overcome the difficulties faced in purifying the receptor owing to its instability and low concentration.
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Cloning, expression and regulation of angiotensin II receptors.
Tadashi Inagami,Naoharu Iwai,Katsutoshi Sasaki,Yoshiaki Yamamo,S. Bardhan,Shigeyuki Chaki,Deng-Fu Guo,Hiroaki Furuta +7 more
TL;DR: Angiotensin II type 1 receptor isoforms AT1A and AT1B were cloned by expression cloning from bovine adrenal and rat vascular smooth muscles and the isoform, AT2, was also expression cloned from rat pheochromocytoma cells, and it is a seven transmembrane domain receptor with unique signalling and regulatory mechanisms.
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Cloning of the cDNA and the genomic DNA of the mouse angiotensin II type 2 receptor
TL;DR: The amino acid sequence of the mouse AT2 (363 residues) deduced from a mouse cDNA clone showed seven membrane-spanning domains, and Amino acid identity of the mice AT2 with mouse AT1 is 37%, and 98% with rat AT2.
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Peptide growth factors markedly decrease the ligand binding of angiotensin II type 2 receptor in rat cultured vascular smooth muscle cells.
TL;DR: This study indicated that the expression of AT2 is downregulated in cultured vascular smooth muscle cells by growth factors in contrast to that of AT1, which was slightly upregulated.
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Protein tyrosine phosphatase inhibition by angiotensin II in rat pheochromocytoma cells through type 2 receptor, AT2.
TL;DR: It is found that angiotensin II inhibits phosphotyrosine phosphatase activity in vivo as measured by the inhibition of hydrolysis of [32P]-phosphate from the 32P-labeled synthetic peptide substrate, Raytide.
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