Zobrazeno 1 - 10
of 101
pro vyhledávání: '"Leonard R. Forte"'
Autor:
Sammy L. Eber, Richard E. Poelling, Judith A. Cole, David L. Carnes, Pamela K. Thorne, Leonard R. Forte
Publikováno v:
Journal of Bone and Mineral Research. 4:723-730
Structural alterations in the parathyroid hormone (PTH) molecule produce marked changes in biologic activity. We examined the relative sensitivity of PTH-stimulated cAMP formation and PTH-inhibitable Na+-dependent phosphate transport responses to bov
Autor:
Timothy J. Hoffman, Wynn A. Volkert, Leonard R. Forte, Michael F. Giblin, Gary L. Sieckman, Nellie K. Owen
Publikováno v:
Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms. 241:689-692
The human Escherichia coli heat-stable enterotoxin (STh, amino acid sequence N1SSNYCCELCCNPACTGCY19) binds specifically to the guanylate cyclase C (GC-C) receptor, which is present in high density on the apical surface of normal intestinal epithelial
Autor:
Leonard R. Forte
Publikováno v:
Pharmacology & Therapeutics. 104:137-162
Guanylin, uroguanylin, and the bacterial heat-stable enterotoxin (ST) peptides comprise a new family of cyclic guanosine 3'-5' monophosphate (cGMP)-regulating agonists. The discovery of guanylin and uroguanylin peptides stems from studies of cellular
Autor:
Jason J. Chang, Brian A. Jackson, Richard N. Greenberg, Elizabeth A. Mann, Congmei Sun, Rajesh G. Shah, Manassés C. Fonteles, Weiyan Cai, Ralph A. Giannella, Michael J. Hill, Stephen L. Carrithers, Leonard R. Forte, C. E. Ott, Brett R. Johnson
Publikováno v:
Kidney International. 65(1):40-53
Guanylin and uroguanylin induce natriuresis in mice lacking guanylyl cyclase-C receptor. Background Guanylin (GN) and uroguanylin (UGN) are intestinally derived peptide hormones that are similar in structure and activity to the diarrhea-causing Esche
Autor:
M. S. Santos-Neto, Leonard R. Forte, Helena Serra Azul Monteiro, Stephen L. Carrithers, Manassés C. Fonteles, André F. Carvalho, Richard N. Greenberg
Publikováno v:
Pharmacology & Toxicology. 92:114-120
Guanylin and uroguanylin are two novel peptides that activate membrane-bound guanylate cyclases found in the kidney and intestine, influencing fluid and electrolyte homeostasis by cyclic GMP. Their natriuretic and kaliuretic activities are well docum
Publikováno v:
Biology of Reproduction. 67:1975-1980
Guanylyl cyclase C (GC-C) is a membrane-associated form of guanylyl cyclase and serves as the receptor for the heat-stable enterotoxin (ST) peptide and endogenous ligands guanylin, uroguanylin, and lymphoguanylin. The major site of expression of GC-C
Autor:
David T. Chin, Hariprasad Gali, Timothy J. Hoffman, Leonard R. Forte, Wynn A. Volkert, Gary L. Sieckman, Nellie K. Owen
Publikováno v:
Nuclear Medicine and Biology. 28:903-909
In vitro competitive binding studies of In-DOTA-NCS-6-Ahx-Phe(19)-ST[1-19] vs. 125I-Tyr(5)-6-Ahx-Phe(19)-ST[1-19] with guanylate cyclase -C (GC-C) receptors on human colon cancer LS-180 cells revealed an IC(50) value of 7.7 +/- 0.1.6 nM. The in vitro
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 278:H538-H547
Uroguanylin is a small-molecular-weight peptide that activates membrane-bound receptor-guanylate cyclases in the intestine, kidney, and other epithelia. Uroguanylin has been shown to participate in the regulation of salt and water homeostasis in mamm
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1446:431-437
We report the cloning of a murine ClC-2 chloride channel cDNA from duodenal epithelium by reverse transcriptase-polymerase chain reaction (RT-PCR) using degenerate primers and by rapid amplification of cDNA ends (RACE)-PCR. Other than CFTR, this repr
Autor:
Leonard R. Forte
Publikováno v:
Regulatory Peptides. 81:25-39
The guanylin family of bioactive peptides consists of three endogenous peptides, including guanylin, uroguanylin and lymphoguanylin, and one exogenous peptide toxin produced by enteric bacteria. These small cysteine-rich peptides activate cell-surfac