Zobrazeno 1 - 10
of 63
pro vyhledávání: '"Mitchel L. Villereal"'
Autor:
Masatsugu Oh-hora, Gopal Thinakaran, Daisuke Ito, William A. Zeiger, Carol Swetlik, Mitchel L. Villereal
Publikováno v:
Molecular and Cellular Biology. 31:3710-3722
The regulation of cellular Ca(2+) homeostasis is essential for innumerable physiological and pathological processes. Stanniocalcin 1, a secreted glycoprotein hormone originally described in fish, is a well-established endocrine regulator of gill Ca(2
Autor:
Mitchel L. Villereal
Publikováno v:
Seminars in Cell & Developmental Biology. 17:618-629
Ca(2+) signaling regulates many important physiological events within a diverse set of living organisms. In particular, sustained Ca(2+) signals play an important role in controlling cell proliferation, cell differentiation and the activation of immu
Autor:
Xiaoyan Wu, Mitchel L. Villereal, Fernando Z. Zamudio, Andree Shalabi, Andrea Scaloni, Lourival D. Possani
Publikováno v:
Journal of Biological Chemistry. 279:1040-1049
Venoms from 14 snakes and four scorpions were screened for inhibitory activities toward store-operated Ca2+ entry (SOCE) in human embryonic kidney-293 cells. An inhibitory activity was found in venom from the African scorpion Pandinus imperator. The
Publikováno v:
American Journal of Physiology-Cell Physiology. 278:C526-C536
The Drosophila trp (transient receptor potential) gene appears to encode the Drosophilastore-operated channel (SOC), and some mammalian trp homologues have been proposed to encode mammalian SOCs. This study provides evidence for the expression of thr
Autor:
Phuong Nguyen, Kulandaivelu S. Vetrivel, Mitchel L. Villereal, Steven L. Wagner, Virginie Buggia-Prevot, William A. Zeiger, Gopal Thinakaran
Publikováno v:
The Journal of biological chemistry, vol 288, iss 37
Alzheimer disease (AD), the leading cause of dementia, is characterized by the accumulation of β-amyloid peptides (Aβ) in senile plaques in the brains of affected patients. Many cellular mechanisms are thought to play important roles in the develop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0bf4d3283da9058bc3c2c0008c9f155
https://escholarship.org/uc/item/8fd8v7h3
https://escholarship.org/uc/item/8fd8v7h3
Publikováno v:
Journal of Cellular Physiology. 168:8-17
It has been suggested that Ca2+ transients, acting through calmodulin-binding proteins, play a role in the activation of the Na+/H+ exchanger isoform NHE1 (Owen and Villereal, 1982a, Biochem. Biophys. Res. Commun., 109:762-768; 1982b, Proc. Natl. Aca
Autor:
Kyung Mi Lee, Mitchel L. Villereal
Publikováno v:
American Journal of Physiology-Cell Physiology. 270:C1430-C1437
Bradykinin (BK) stimulates protein tyrosine phosphorylation in human foreskin fibroblasts (K.-M. Lee, K. Toscas, and M. L. Villereal, J. Biol. Chem. 268:9945-9948, 1993). The major tyrosine phosphorylation occurs in proteins of a molecular mass of 13
Publikováno v:
Cell Calcium. 17:41-52
Previously, we have used the classical approach to examine intracellular calcium stores in human foreskin fibroblasts (HSWP) cells. In this classical protocol cells are first permeabilized and then allowed to fill their Ca 2+ reservoirs with 45 Ca 2+
Autor:
Yue Xie, Crescence Bookstein, Mrinalini C. Rao, Mitchel L. Villereal, Mark W. Musch, Eugene B. Chang, Alex M. DePaoli
Publikováno v:
Journal of Biological Chemistry. 269:29704-29709
Membrane sodium-hydrogen exchangers (NHEs), found in virtually all cell types, appear to have diverse and essential roles in regulating cellular pH and mediating vectorial transport by epithelial cells. However, the functional and physiological role
Autor:
Manoocher Soleimani, Yolanda J. Hattabaugh, Crescence Bookstein, Randy L. Howard, Mrinalini C. Rao, James A. McAteer, Gwen L. Bizal, Eugene B. Chang, Mitchel L. Villereal, Mark W. Musch
Publikováno v:
Journal of Biological Chemistry. 269:15613-15618
Na+/H+ exchanger isoform and the effect of high osmolality on its function was studied in cultured renal epithelial cells (LLC-PK1 and OK). Using NHE-3-specific antibody, immunoblots of luminal membranes from LLC-PK1 and OK cells specifically labeled