Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Kevin X. Z. Li"'
Publikováno v:
American Journal of Physiology-Gastrointestinal and Liver Physiology. 277:G541-G547
To evaluate the potential roles that both receptors and enzymes play in corticosteroid regulation of intestinal function, we have determined glucocorticoid receptor (GR), mineralocorticoid receptor (MR), and 11β-hydroxysteroid dehydrogenase (11β-HS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fefd0c08eb2886a85a8098bdfb5469d1
https://doi.org/10.1152/ajpgi.1999.277.3.g541
https://doi.org/10.1152/ajpgi.1999.277.3.g541
Autor:
Timothy Wiens, Kevin X. Z. Li, Maria I. New, Cedric H. L. Shackleton, Ji-Qing Wei, Swati Dave-Sharma, Varuni R. Obeyesekere, Robert C. Wilson, Paolo Ferrari, Zygmunt S. Krozowski, Leon Bradlow
Publikováno v:
Proceedings of the National Academy of Sciences. 95:10200-10205
Severe low-renin hypertension has few known causes. Apparent mineralocorticoid excess (AME) is a genetic disorder that results in severe juvenile low-renin hypertension, hyporeninemia, hypoaldosteronemia, hypokalemic alkalosis, low birth weight, fail
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cab58f57427476252de4e13071a68326
https://doi.org/10.1073/pnas.95.17.10200
https://doi.org/10.1073/pnas.95.17.10200
Publikováno v:
American Journal of Physiology-Endocrinology and Metabolism. 275:E124-E131
Recently, we identified a novel putative nuclear receptor in colonic crypt cells distinct from both mineralocorticoid receptor and glucocorticoid receptor, with high affinity for 11-dehydrocorticosterone (11-DHB) (33). In the present study, competiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b7ac895d35cf2a6293d7ab3b60c9ad5
https://doi.org/10.1152/ajpendo.1998.275.1.e124
https://doi.org/10.1152/ajpendo.1998.275.1.e124
Autor:
Cedric H. L. Shackleton, Berenice B. Mendonca, C B Whorwood, Ive J.p. Arnhold, Marcelo C. Batista, Zygmunt S. Krozowski, Kevin X. Z. Li, Suemi Marui, Airong Li, Paul M. Stewart
Publikováno v:
Journal of Hypertension. 15:1397-1402
Background Apparent mineralocorticoid excess (AME) is a cause of low-renin, low-aldosterone hypertension in which cortisol acts as a mineralocorticoid. The condition reflects an inability to inactivate cortisol to cortisone due to defective activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2e640a6d61927bb5a0f3df47bd61ed2
https://doi.org/10.1097/00004872-199715120-00005
https://doi.org/10.1097/00004872-199715120-00005
Autor:
Zygmunt S. Krozowski, Paul A. Komesaroff, Mark Lawrence, Kathy Myles, Lois A. Salamonsen, Kevin X. Z. Li, Robin E. Smith
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 82:4252-4257
The 11β-hydroxysteroid dehydrogenase type II enzyme (11βHSD2) is a potent inactivator of glucocorticoids and is present in high amounts in the placental syncytiotrophoblast and sodium-transporting epithelia. Placental 11βHSD2 is thought to protect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0524cd4a23e7e1a04f6131e753b7011d
https://doi.org/10.1210/jcem.82.12.4451
https://doi.org/10.1210/jcem.82.12.4451
Publikováno v:
Molecular and Cellular Endocrinology. 131:173-182
The 11beta-hydroxysteroid dehydrogenase type II enzyme (11betaHSD2) endows specificity on the mineralocorticoid receptor by metabolising glucocorticoids. Sequence comparisons with other microsomal proteins showed the strongly preferred topology of a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6aa51269cef9376dfd1d577fd1800ff3
https://doi.org/10.1016/s0303-7207(97)00106-8
https://doi.org/10.1016/s0303-7207(97)00106-8
Autor:
Zygmunt S. Krozowski, Kevin X. Z. Li, Paolo Ferrari, Varuni R. Obeyesekere, Robert K. Andrews
Publikováno v:
Steroids. 61:197-200
The 11 beta-hydroxysteroid dehydrogenase type II enzyme (11 beta HSD2) converts cortisol to cortisone, allowing the non-selective mineralocorticoid receptor to bind aldosterone. When the activity of this enzyme is compromised, as occurs in licorice i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52343da0dceba1d4a65f0f2192459be2
https://doi.org/10.1016/0039-128x(96)00013-x
https://doi.org/10.1016/0039-128x(96)00013-x
Autor:
Françoise Haeseleer, Ian Smith, Paul A. Komesaroff, Zygmunt Krozowski, Phillip S. Brereton, Takashi Suzuki, Krzysztof Palczewski, Hironobu Sasano, Varuni R. Obeyesekere, Kevin X. Z. Li, Carla Duarte
Publikováno v:
Molecular and cellular endocrinology. 171(1-2)
We describe a new member of the 17beta-hydroxysteroid dehydrogenase group of enzymes. Human Pan1b displays greatest activity with 5alpha-androstan-3alpha,17beta-diol (3alpha-Diol) as substrate, suggesting that it may be important in androgen metaboli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1b3e62d0215dfe33816f5d9b7cdfcd5
https://pubmed.ncbi.nlm.nih.gov/11165019
https://pubmed.ncbi.nlm.nih.gov/11165019
Publikováno v:
American journal of physiology. Gastrointestinal and liver physiology. 279(3)
When small intestinal epithelial cells are incubated with [3H]corticosterone, nuclear binding is displaced neither by aldosterone nor RU-28362, suggesting that [3H]corticosterone is binding to a site distinct from mineralocorticoid receptor and gluco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::928c9eb5e997503f21b613c90c69c0b2
https://pubmed.ncbi.nlm.nih.gov/10960352
https://pubmed.ncbi.nlm.nih.gov/10960352
Publikováno v:
Biochemical and biophysical research communications. 250(2)
Short chain alcohol dehydrogenases have an invariant YXXXK motif at the active site. Database analysis of 116 superfamily members showed that 92% also contain a Serine or Threonine residue at the Y + 1 or Y + 3 positions, a pattern we previously desc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a3e5df8f1b73ec3e3e8226afd9bceb3
https://pubmed.ncbi.nlm.nih.gov/9753655
https://pubmed.ncbi.nlm.nih.gov/9753655