Zobrazeno 1 - 10
of 84
pro vyhledávání: '"Walker H Busby"'
Autor:
Timothy C Nichols, Elizabeth P Merricks, Dwight A Bellinger, Robin A Raymer, Jing Yu, Diana Lam, Gary G Koch, Walker H Busby, David R Clemmons
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0132302 (2015)
Insulin-resistant subjects develop more severe and diffuse coronary artery atherosclerosis than insulin-sensitive controls but the mechanisms that mediate this atherosclerosis phenotype are unknown.To determine the metabolic parameters that associate
Externí odkaz:
https://doaj.org/article/fdaeeb58e3ea435d8c46bdfab0fc23c5
Autor:
Elizabeth P. Merricks, Walker H. Busby, Dwight A. Bellinger, Gang Xi, N. Gafbacik, K.P. Gollahan, W. L. Flowers, Timothy C. Nichols, Laura A. Maile, Kara R Stewart, David R. Clemmons, S. Gafbacik
Publikováno v:
Atherosclerosis. 258:40-50
Diabetes is a major risk factor for the development of atherosclerosis. Hyperglycemia stimulates vascular smooth muscle cells (VSMC) to secrete ligands that bind to the αVβ3 integrin, a receptor that regulates VSMC proliferation and migration. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a510fbf36011db2baf4c0d96c70b8b3d
https://doi.org/10.1016/j.atherosclerosis.2017.01.030
https://doi.org/10.1016/j.atherosclerosis.2017.01.030
Autor:
Dwight A. Bellinger, W. L. Flowers, Matt D. Medlin, K. Gollahon, Walker H. Busby, Kara R Stewart, Paul Dunbar, Amit Patel, Stefani Garbacik, Timothy C. Nichols, David R. Clemmons, Laura A. Maile, Nikol Garbacik
Publikováno v:
Endocrinology. 155:4665-4675
Hyperglycemia stimulates secretion of αVβ3 ligands from vascular cells, including endothelial cells, resulting in activation of the αVβ3 integrin. This study determined whether blocking ligand occupancy of αVβ3 would inhibit the development of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c225b03e9d23b34f957c64b0e56129
https://doi.org/10.1210/en.2014-1318
https://doi.org/10.1210/en.2014-1318
Publikováno v:
Journal of Biological Chemistry. 285:15682-15695
Vascular smooth muscle cells maintained in normal (5.6 mm) glucose respond to insulin-like growth factor-I (IGF-I) with increased protein synthesis but do not proliferate. In contrast, hyperglycemia alters responsiveness to IGF-I, resulting in increa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6266a3afc233c6f0b3ec45ed3837a81e
https://doi.org/10.1074/jbc.m109.092270
https://doi.org/10.1074/jbc.m109.092270
Autor:
Walker H. Busby, Sue A. Yocum, Michael A. Rowland, Debra Kellner, Lazerwith Scott E, Francis M. Sverdrup, Melissa R. Radabaugh, Matthew P. Yates, David R. Clemmons
Publikováno v:
Osteoarthritis and Cartilage. 17:547-555
Summary Insulin-like growth factor-I (IGF-I) and IGF binding proteins (IGFBPs) are trophic factors for cartilage and have been shown to be chondroprotective in animal models of osteoarthritis (OA). IGFBP-5 is degraded in joint fluid and inhibition of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff85bf38afeeec1795d8f4a09277e062
https://doi.org/10.1016/j.joca.2008.08.004
https://doi.org/10.1016/j.joca.2008.08.004
Autor:
Kevin Sitko, Elizabeth P. Merricks, Michael A. Rowland, David R. Clemmons, Walker H. Busby, Jennifer A Sipos, Timothy C. Nichols
Publikováno v:
Endocrinology. 148:5002-5010
IGF-I has been shown to play a role in the progression of atherosclerosis in experimental animal models. IGF-binding protein-4 (IGFBP-4) binds to IGF-I and prevents its association with receptors. Overexpression of a protease-resistant form of IGFBP-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d39bb095bc897f65f24c007e4773369
https://doi.org/10.1210/en.2007-0571
https://doi.org/10.1210/en.2007-0571
Autor:
Walker H. Busby, Kevin Sitko, Byron E. Capps, Yan Ling, David R. Clemmons, Jane Badley-Clarke, Tiffany Sergent, Laura A. Maile
Publikováno v:
Molecular Endocrinology. 20:881-892
We have shown that vitronectin (Vn) binding to a cysteine loop sequence within the extracellular domain of the beta3-subunit (amino acids 177-184) of alphaVbeta3 is required for the positive effects of Vn on IGF-I signaling. When Vn binding to this s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7506f712413cb4291885980d40345f8
https://doi.org/10.1210/me.2005-0382
https://doi.org/10.1210/me.2005-0382
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 90:6561-6568
Administration of IGF-binding protein-3 (IGFBP-3) with IGF-I stabilizes IGF-I concentrations and prolongs its half-life. One determinant of IGFBP-3 stability is proteolysis. Normal subjects have minimal IGFBP-3 protease activity; however, with pregna
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb7a1c52bab05b3c5232bf60229c2ba
https://doi.org/10.1210/jc.2005-1389
https://doi.org/10.1210/jc.2005-1389
Publikováno v:
Journal of Diabetes Research, Vol 2014 (2014)
Journal of Diabetes Research
Journal of Diabetes Research
This study determined if blocking ligand occupancy of theαVβ3 integrin could inhibit the pathophysiologic changes that occur in the early stages of diabetic nephropathy (DN). Diabetic rats were treated with either vehicle or a monoclonal antibody t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0720de77ee38aa160c67878329aed0ca
https://doaj.org/article/0951f397a7bd4bd98163ee2a114df569
https://doaj.org/article/0951f397a7bd4bd98163ee2a114df569
Publikováno v:
Endocrinology. 139:4182-4188
Smooth muscle cells (SMC) secrete a serine protease that cleaves insulin-like growth factor (IGF) binding protein (IGFBP)-4 into fragments that have low affinity for IGF-1. When IGFBP-4 is added to monolayer cultures of cell types that do not secrete
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec056e9727e37d9ba9f49f936ab5c77b
https://doi.org/10.1210/endo.139.10.6266
https://doi.org/10.1210/endo.139.10.6266