Zobrazeno 1 - 10
of 68
pro vyhledávání: '"John J. Egan"'
Autor:
Jean Paul Wuerth, Peter V. Vaitkevicius, George S. Roth, Michael Brines, Donald K. Ingram, John J. Egan, Harold A. Spurgeon, Edward G. Lakatta, Peter C. Ulrich, Mark A. Lane, Sara Vasan, Anthony Cerami, Dilip R. Wagle
Publikováno v:
Proceedings of the National Academy of Sciences. 98:1171-1175
Nonenzymatic glycosylation and cross-linking of proteins by glucose contributes to an age-associated increase in vascular and myocardial stiffness. Some recently sythesized thiazolium compounds selectively break these protein cross-links, reducing co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a34bf28a90870a6b3d388069273701a
https://doi.org/10.1073/pnas.98.3.1171
https://doi.org/10.1073/pnas.98.3.1171
Breakers of advanced glycation end products restore large artery properties in experimental diabetes
Autor:
Sara Vasan, Francy R. L. Crijns, Pierre Poitevin, John J. Egan, Chantal M. Boulanger, Anthony Cerami, Bernard I. Levy, Maya S. P. Huijberts, Geertje N. M. Swennen, Bruce H. R. Wolffenbuttel, Peter C. Ulrich
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 95(8), 4630-4634. National Academy of Sciences
Department of Endocrinology, Cardiovascular Research Institute Maastricht and University (Hospital) Maastricht, P.O. Box 5800, 6202 AZ Maastricht, The Netherlands.Glucose and other reducing sugars react with proteins by a nonenzymatic, posttranslatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a17862fbd9b61a3963bf8f71c43ba27
https://doi.org/10.1073/pnas.95.8.4630
https://doi.org/10.1073/pnas.95.8.4630
Publikováno v:
Diabetes. 45:1694-1700
Solubility of tail tendon collagen from normal, streptozotocin-induced diabetic Lewis rats, and diabetic animals treated with aminoguanidine and two novel advanced glycosylation end products (AGE)-formation inhibitors was investigated by limited peps
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2ef5fad125bd3647d55a77712cfd60e
https://doi.org/10.2337/diab.45.12.1694
https://doi.org/10.2337/diab.45.12.1694
Effect of Verapamil on the Cyclic AMP-Mediated Pathway for Amylase Secretion in Rat Pancreatic Acini
Publikováno v:
Pancreas. 8:212-219
In dispersed acini from rat pancreas, verapamil (a phenylalkylamine calcium channel blocker) potentiated amylase secretion stimulated by vasoactive intestinal peptide (VIP), secretin, peptide histidine isoleucine, helodermin, forskolin, and 8-bromocy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48e28b688d567edb546ec79ec26ab1a8
https://doi.org/10.1097/00006676-199303000-00012
https://doi.org/10.1097/00006676-199303000-00012
Autor:
Sheree A. Wek, Constantine Londos, Malcolm Moos, Andrew S. Greenberg, Min-Kun Chang, John J. Egan
Publikováno v:
Proceedings of the National Academy of Sciences. 89:8537-8541
Hormone-sensitive lipase activity (HSL), which is found in the supernatant of centrifuged homogenates of lipolytically quiet isolated rat adipocytes, was greatly reduced in or absent from the supernatant of lipolytically stimulated cells. The lipase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01d46f230a21e676379137aa48ce3963
https://doi.org/10.1073/pnas.89.18.8537
https://doi.org/10.1073/pnas.89.18.8537
Autor:
Sheree A. Wek, N B Garty, Constantine Londos, John J. Egan, E J Blanchette-Mackie, Andrew S. Greenberg
Publikováno v:
Journal of Biological Chemistry. 266:11341-11346
The lipid fraction ("fat cake") of rat epididymal adipocytes contains a prominent phosphoprotein (62 kDaapp by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) that is multiply phosphorylated by cAMP-dependent protein kinase in vivo, at whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d9172e5995dad9ec296281609fb6855
https://doi.org/10.1016/s0021-9258(18)99168-4
https://doi.org/10.1016/s0021-9258(18)99168-4
Autor:
A D Habberfield, Constantine Londos, Ian A. Simpson, Samuel W. Cushman, John J. Egan, J Saltis
Publikováno v:
Journal of Biological Chemistry. 266:261-267
The possible role of protein kinase C in the regulation of glucose transport in the rat adipose cell has been examined. Both insulin and phorbol 12-myristate 13-acetate (PMA) stimulate 3-O-methylglucose transport in the intact cell ein association wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e4cef9194ff4555e91901193aadc1a2
https://doi.org/10.1016/s0021-9258(18)52429-7
https://doi.org/10.1016/s0021-9258(18)52429-7
Publikováno v:
Journal of Biological Chemistry. 265:18769-18775
In isolated, 32Pi-loaded, rat adipocytes, we have examined phosphorylation of the major cAMP-dependent protein kinase (A-kinase) substrate, a protein that appears to be associated with the lipid storage droplet and migrates in sodium dodecyl sulfate-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3fdec3ab7be843b9661b8fca6227196d
https://doi.org/10.1016/s0021-9258(17)30578-1
https://doi.org/10.1016/s0021-9258(17)30578-1
Insulin, oxytocin, and vasopressin stimulate protein kinase C activity in adipocyte plasma membranes
Publikováno v:
Proceedings of the National Academy of Sciences. 87:1052-1056
Incubation of isolated rat adipocytes with insulin, vasopressin, or oxytocin increased plasma membrane-bound protein kinase C (PKC) activity by 100-400%. PKC activity was assayed by a procedure that is virtually background-free, thus permitting assay
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcfbd7a505885b0ba2a551c69ff93119
https://doi.org/10.1073/pnas.87.3.1052
https://doi.org/10.1073/pnas.87.3.1052
Publikováno v:
Nature Biotechnology. 13:559-561
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2519de29c8e79479b5a2b423b26e081d
https://doi.org/10.1038/nbt0695-559
https://doi.org/10.1038/nbt0695-559