Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Anissa Lambertino"'
Autor:
Mary Turyk, Terry G. Unterman, Anissa Lambertino, Sally Freels, Saria Awadalla, Henry A. Anderson, Victoria Persky
Publikováno v:
Chemosphere
BACKGROUND: The general population is exposed to the group of endocrine disrupting chemicals persistent organic pollutants (POPs), that includes polychlorinated biphenyls (PCBs), polychlorinated dibenzo-p-dioxins (PCDDs) and polychlorinated dibenzofu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f51d10f6a7f75d1805b08635eb2771d
https://pubmed.ncbi.nlm.nih.gov/33182091
https://pubmed.ncbi.nlm.nih.gov/33182091
Publikováno v:
Environmental Research. 111:565-572
Diet and endocrine disrupting persistent organic pollutants (POPs) have been associated with gynecologic conditions including uterine leiomyomata (UL), endometriosis, and ovarian cysts. Great Lakes sport fish consumption is a source of exposure to PO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a83538b846215e87e928442f5cc7b22
https://doi.org/10.1016/j.envres.2011.01.006
https://doi.org/10.1016/j.envres.2011.01.006
Publikováno v:
Journal of Asthma. 46:202-206
Background. Residents of public housing can experience socioeconomic disadvantages, inadequate access to health care, and particularly substandard indoor air quality due to inadequate building maintenance. Objective. This study investigates demograph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb71364ef27c442efb23f901a11ba4e7
https://doi.org/10.1080/02770900802627286
https://doi.org/10.1080/02770900802627286
Autor:
Sally Freels, Henry A. Anderson, Maria Pini, Victoria Persky, Davina H. Rhodes, Mary Turyk, Anissa Lambertino, Giamila Fantuzzi
Publikováno v:
Environmental research. 140
Exposure to persistent organic pollutants (POPs) is associated with increased diabetes risk, although the mechanism of action is not well delineated.We investigated established diabetes biomarkers that could implicate potential mechanistic pathways,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a45a8d1c5696583fa3767552df929b9
https://pubmed.ncbi.nlm.nih.gov/25913152
https://pubmed.ncbi.nlm.nih.gov/25913152
Autor:
Anissa Lambertino, Jonathan Learoyd, Xiangdong Zhu, Shigeharu Myou, Evan Boetticher, Angelo Y. Meliton, Masaaki Sano, Nilda M. Munoz, Alan R. Leff
Publikováno v:
American Journal of Respiratory Cell and Molecular Biology. 33:65-70
We examined the role of phosphoinositide 3-kinase (PI3K) in integrin-mediated eosinophil adhesion. Deltap85, a dominant-negative form of the class IA PI3K adaptor subunit, was fused to an HIV-TAT protein transduction domain (TAT-Deltap85). Recombinan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2414ac5eea925868d0b416e4215d00b0
https://doi.org/10.1165/rcmb.2005-0076oc
https://doi.org/10.1165/rcmb.2005-0076oc
Autor:
Nilda M. Munoz, Shigeharu Myou, Alan R. Leff, Evan Boetticher, Angelo Y. Meliton, Hiroyuki Sano, Anissa Lambertino, Benjamin Jacobs, Xiangdong Zhu
Publikováno v:
Journal of Leukocyte Biology. 72:1046-1053
We examined the mechanism by which interleukin (IL)-5 causes β2-integrin adhesion of human eosinophils. IL-5 caused time-dependent activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) and p38α in eosinophils as detected by their ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a68787f8a08ce2efb240f6b8597bb42
https://doi.org/10.1189/jlb.72.5.1046
https://doi.org/10.1189/jlb.72.5.1046
Autor:
Angelo Y. Meliton, Xiangdong Zhu, Kimm J. Hamann, Shigeharu Myou, Yimin Qin, Saori Myo, Nilda M. Munoz, Alan R. Leff, Anissa Lambertino, Evan Boetticher
Publikováno v:
Immunology. 107:77-85
We examined the role of cell surface clustering of beta2-integrin caused by protein kinase C (PKC)-activated-cPLA2 in adhesion of eosinophilic AML14.3D10 (AML) cells. Phorbol 12-myristate 13-acetate (PMA) caused time- and concentration-dependent adhe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b23b004f29dadbbb11698cf5e3a7ddc9
https://doi.org/10.1046/j.1365-2567.2002.01486.x
https://doi.org/10.1046/j.1365-2567.2002.01486.x
Publikováno v:
The Nursing clinics of North America. 48(1)
Incidence and prevalence rates of asthma can vary greatly according to population and location. The National Heart and Blood Institute of the National Institutes of Health defines asthma as a common chronic disorder of the airways that involves a com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbe7b39cacc33c74b6a223ad3937966e
https://pubmed.ncbi.nlm.nih.gov/23465442
https://pubmed.ncbi.nlm.nih.gov/23465442
Autor:
Anissa Lambertino, Nilda M. Munoz, Alan R. Leff, Angelo Y. Meliton, Faraz Sultan, Evan Boetticher, Xiangdong Zhu, Jonathan Learoyd, Wonhwa Cho
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 177(1)
We examined the mechanism by which secretory group V phospholipase A(2) (gVPLA(2)) secreted from stimulated epithelial cells activates eosinophil adhesion to ICAM-1 surrogate protein and secretion of leukotriene (LT)C(4). Exogenous human group V PLA(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3aa027046988172f1985f5a1170e6bd1
https://pubmed.ncbi.nlm.nih.gov/16785555
https://pubmed.ncbi.nlm.nih.gov/16785555
Autor:
Martha Cordoba, Evan Boetticher, Saori Myo, Angelo Y. Meliton, Jie Liu, Malcolm Johnson, Anissa Lambertino, Alan R. Leff, Xiangdong Zhu, Chang Xu, Masaaki Sano, Nilda M. Munoz, Jonathan Learoyd
Publikováno v:
The Journal of allergy and clinical immunology. 115(3)
Background Glucocorticoids attenuate the population of eosinophils and T lymphocytes in asthmatic airways. The decrease in airway eosinophilia is caused both by accelerated cell death and by induction of blockade of integrin adhesion. In this study,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8fc1d29a29c4b0decad47c83ecd789a
https://pubmed.ncbi.nlm.nih.gov/15753895
https://pubmed.ncbi.nlm.nih.gov/15753895