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Autor:
Patrick M. Sexton, Denise Wootten, Emilia Elizabeth Savage, Laurence J. Miller, Arthur Christopoulos, Cassandra Koole
Publikováno v:
Molecular Endocrinology. 27:1234-1244
The glucagon-like peptide-1 receptor (GLP-1R) controls the physiological responses to the incretin hormone glucagon-like peptide-1 and is a major therapeutic target for the treatment of type 2 diabetes, owing to the broad range of effects that are me
Autor:
Grant Buchanan, Luke A. Selth, Tiffany J. Harris, Stephen N. Birrell, Wayne D. Tilley, Eleanor F. Need
Publikováno v:
Molecular Endocrinology. 26:1941-1952
The cellular response to circulating sex steroids is more than the sum of individual hormone actions, instead representing an interplay between activities of the evolutionarily related steroid hormone receptors. An example of this interaction is in b
Publikováno v:
Molecular Endocrinology. 19:312-326
We evaluated the signaling pathways involved in regulating vascular endothelial growth factor (VEGF), a potent angiogenic growth factor, in response to natural and synthetic progestins in breast cancer cells. Inhibition of the phosphoinositide-3′-k
Autor:
Harumi Hattori, Koji Yoshimura, Cydney C. Brooks, Eleonora Presman, Yukio Fujisawa, Nozomi Katayama, Shigeya Kakimoto, Isao Kaieda, Paul F. Pilch, Hideaki Tojo
Publikováno v:
Molecular Endocrinology. 17:1216-1229
Insulin stimulates translocation of glucose transporter isoform type 4 (GLUT4) and the insulin-responsive aminopeptidase (IRAP) from an intracellular storage pool to the plasma membrane in muscle and fat cells. A role for the cytoskeleton in insulin
Publikováno v:
Molecular Endocrinology. 15:1993-2009
Epidemiological studies have consistently shown that an early full-term pregnancy is protective against breast cancer. We hypothesize that the hormonal milieu that is present during pregnancy results in persistent changes in the pattern of gene expre
Publikováno v:
Molecular Endocrinology. 15:1768-1780
PTP1B is a protein tyrosine phosphatase that negatively regulates insulin sensitivity by dephosphorylating the insulin receptor. Akt is a ser/thr kinase effector of insulin signaling that phosphorylates substrates at the consensus motif RXRXXS/T. Int
Autor:
Ming Ding, Tomomi Miyamoto, Paul S. Kim, Ji-Ming Cheng, Takashi Agui, Sen-ichi Furudate, Cha-Gyun Jung, Bailing Li, Shekar Menon
Publikováno v:
Molecular Endocrinology. 14:1944-1953
A convincing line of evidence is being developed that the congenital nongoitrous hypothyroidism and dwarfism observed in the WIC-rdw rat may indeed be caused by a primary defect in thyroid hormonogenesis. In support of this hypothesis, several recent
Autor:
Walter L. Miller, Richard J. Auchus
Publikováno v:
Molecular Endocrinology. 13:1169-1182
P450c17 (17alpha-hydroxylase/17,20-lyase) catalyzes steroid 17alpha-hydroxylase and 17,20-lyase activities in the biosynthesis of androgens and estrogens. These two activities are differentially regulated in a tissue-specific and developmentally prog
Publikováno v:
Molecular Endocrinology. 11:1094-1102
Homologous desensitization and internalization of the GLP-1 receptor correlate with phosphorylation of the receptor in a 33-amino acid segment of the cytoplasmic tail. Here, we identify the sites of phosphorylation as being three serine doublets loca
Publikováno v:
Molecular Endocrinology. 11:997-1007
The growth-promoting activity of GH, the principal hormonal determinant of body size, is mediated by insulin-like growth factor I (IGF-I). Most of the IGF-I in plasma circulates in a 150-kDa complex that contains IGF-binding protein-3 (IGFBP-3) and a