Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Mary E. Maley"'
Autor:
Juan B. Ochoa, Andrew C. Bernard, Bernard R. Boulanger, Paul A. Kearney, Matthew D. Shane, Mary E. Maley, Betty J. Tsuei, Lawrence A. Shirley
Publikováno v:
Journal of Trauma and Acute Care Surgery. 51:497-502
Background: Arginase is a metabolic enzyme for the amino acid arginine that participates in the immune response to trauma. We hypothesize that surgical trauma induces arginase expression and activity in the human immune system. Methods: Peripheral mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::507bb97476d8cedd4001d440acd2bbb2
https://doi.org/10.1097/00005373-200109000-00012
https://doi.org/10.1097/00005373-200109000-00012
Autor:
William E. O'Brien, Bernard R. Boulanger, Juan B. Ochoa, Andrew C. Bernard, Paul A. Kearney, Mary E. Maley, Margaret M. Griffen, Sidney M. Morris, Betty J. Tsuei, Anna K. Rockich
Publikováno v:
Annals of Surgery. 233:393-399
To determine the effect of trauma on arginase, an arginine-metabolizing enzyme, in cells of the immune system in humans.Arginase, classically considered an enzyme exclusive to the liver, is now known to exist in cells of the immune system. Arginase e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a97eee75b257b4b3aaa4c4aaeb2a423
https://doi.org/10.1097/00000658-200103000-00014
https://doi.org/10.1097/00000658-200103000-00014
Autor:
Juan B. Ochoa, Andrew C. Bernard, Warwick A. Arden, Bernard R. Boulanger, Gloria Gellin, Mary E. Maley, Paul A. Kearney, Elizabeth A. Fitzpatrick, Betty J. Tsuei
Publikováno v:
Surgery. 127:412-418
Arginase, which metabolizes L-arginine within the urea cycle, is essential for production of polyamines and affects production of nitric oxide by depletion of L-arginine, the common substrate for both arginase and nitric oxide synthase. Having shown
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47b1ee1ab4432bf620e713f6cb0ab0f5
https://doi.org/10.1067/msy.2000.104115
https://doi.org/10.1067/msy.2000.104115
Publikováno v:
Molecular Brain Research. 44:134-138
We have studied the beneficial effects of S-adenosyl-L-methionine (SAM) tosylate on blood-brain barrier (BBB) breakdown and neuronal survival after transient cerebral ischemia in gerbils. BBB breakdown experiments were performed in pentobarbital anes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d18c41abe05e6c923a27bdff5507b454
https://doi.org/10.1016/s0169-328x(96)00245-8
https://doi.org/10.1016/s0169-328x(96)00245-8
Autor:
Bernard R. Boulanger, Gloria Gellin, Paul A. Kearney, Andrew R. Barksdale, Betty J. Tsuei, Juan B. Ochoa, Andrew C. Bernard, Mary E. Maley
Publikováno v:
Surgery. 135(5)
Background Trauma causes a release of catecholamines, transforming growth factor–β (TGF-β), and T-helper II cytokines (TH2). Individually, these substances also induce arginase in macrophages. The purpose of this study was to determine the synerg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8970579e8413a115d6f815522cfbf83
https://pubmed.ncbi.nlm.nih.gov/15118590
https://pubmed.ncbi.nlm.nih.gov/15118590
Autor:
Sidney M. Morris, Betty J. Tsuei, William E. O'Brien, Sanjay K. Mistry, Juan B. Ochoa, Andrew C. Bernard, Mary E. Maley, Lawrence A. Shirley, Bernard R. Boulanger, Paul A. Kearney
Publikováno v:
Shock (Augusta, Ga.). 15(3)
Arginine is the sole substrate for nitric oxide (NO) synthesis by NO synthases (NOS) and promotes the proliferation and maturation of human T-cells. Arginine is also metabolized by the enzyme arginase, producing urea and ornithine, the precursor for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e7adb8932a335ba9a874bdc75e32650
https://pubmed.ncbi.nlm.nih.gov/11236905
https://pubmed.ncbi.nlm.nih.gov/11236905
Autor:
Juan B. Ochoa, Andrew C. Bernard, Bernard R. Boulanger, Betty J. Tsuei, Paul A. Kearney, Patricia L. Figert, Sidney M. Morris, Sanjay K. Mistry, Mary E. Maley
Publikováno v:
Surgery. 127(4)
Background: Although expressed primarily in the liver, arginase activity also is present in extrahepatic tissues and specifically in macrophages, where it may play diverse physiologic roles in wound healing, cellular proliferation, and the regulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26a030f41f51f561ff20bbe456f8b082
https://pubmed.ncbi.nlm.nih.gov/10776433
https://pubmed.ncbi.nlm.nih.gov/10776433
Autor:
A. Muralikrishna Rao, M. Renuka Prasad, David Donaldson, Mustafa K. Baskaya, Mary E. Maley, Yingan Hu, Robert J. Dempsey
Publikováno v:
Journal of neurosurgery. 85(1)
✓ This study examined the effect of AA-861, a specific 5-lipoxygenase inhibitor, on brain levels of leukotriene C4 (LTC4) and correlated any changes with changes in edema formation and cerebral blood flow (CBF) after transient ischemia in gerbils.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61b185b3ec2d620c82124d7774f0ebda
https://pubmed.ncbi.nlm.nih.gov/8683259
https://pubmed.ncbi.nlm.nih.gov/8683259
Publikováno v:
Journal of neurochemistry. 65(6)
General anesthetic agents often affect the biochemical and physiologic changes triggered by cerebral ischemia. This study examined the regional activities of ornithine decarboxylase (ODC) in gerbils subjected to 5 min of bilateral carotid occlusion w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f66293a7d8be9d5d5e164b8ea1d21c29
https://pubmed.ncbi.nlm.nih.gov/7595561
https://pubmed.ncbi.nlm.nih.gov/7595561
Publikováno v:
Stroke. 21(6)
The dose-response relation between plasma glucose and brain lactate and the relation of these parameters to intracellular pH during severe cerebral ischemia have not been well characterized over a wide range of plasma glucose levels. Experiments to d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9112c729983bb0d7afe8485b2ee9aa8b
https://pubmed.ncbi.nlm.nih.gov/2349598
https://pubmed.ncbi.nlm.nih.gov/2349598