Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Richard C. Franson"'
Publikováno v:
Journal of Investigative Surgery. 13:95-101
In order to obtain baseline information on the secretory function of normal rat bowel for our work on intestinal graft ischemia, we studied several biochemical parameters in rat Thiry-Vella fistulas (TVF). TVFs were created in 200-g male Lewis rats (
Publikováno v:
Digestive Diseases and Sciences. 42:972-981
The time-dependent appearance of phospholipaseA2 (PLA2) activity in thepreservation media of ischemic rat intestinal grafts isdescribed. In controls, Ca2+-dependent,secretory PLA2 activity accumulated rapidly during the first 6 hr of ischemia,followe
Autor:
L.K. Harris, Miriam D. Rosenthal, Richard C. Franson, E.S. Buescher, M.N. Gordon, J.H. Slusser
Publikováno v:
Biochemical and Biophysical Research Communications. 208:650-656
Although "secretory" type II 14-kDa phospholipase A2 (sPLA2) activity has been described in neutrophils, direct evidence of enzyme secretion has been elusive. We have used immunogold electron microscopy with polyclonal and monoclonal antibodies to sP
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1177:79-86
Preincubation of human neutrophils with 1-oleoyl-2-acetylglycerol (OAG) enhances subsequent f-Met-Leu-Phe (fMLP)-stimulated arachidonate mobilization. We have recently demonstrated that preincubation of neutrophils with OAG also reverses inhibition o
Publikováno v:
Biology of Reproduction. 47:751-759
Phospholipase A2 was isolated from human sperm and its potential role in the membrane fusion events of fertilization was examined. Highly purified enzyme hydrolyzed the phospholipids of [1-14C]oleate-labeled Escherichia coli optimally at neutral to a
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1136:169-174
Sphingosine inhibits protein kinase C activity in vitro and has been used to implicate this enzyme in signal transduction and cell function. We report that sphingosine directly inhibits phospholipases A2 and D. Sphingosine inhibits Ca(2+)-dependent p
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1126:319-326
Aristolochic acid and PGBx, two structurally unrelated, protein-targeted inhibitors of isolated phospholipases A2, are effective antagonists of calcium ionophore A23187-stimulated mobilization of [3H]arachidonate from human neutrophils. We now report
Autor:
Richard C. Franson, Michael Bartolf
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1042:247-254
Soluble, cation-dependent, lysosomal phospholipase A2 in bovine adrenal medulla has been biochemically characterized and partially purified, and its unique pH-dependent modulation by cations has been investigated. Chromatographically distinct activit
Publikováno v:
Circulation. 116
Background: The low-molecular-weight, calcium-dependent type IIA secretory phospholipase A 2 (sPLA 2 ) has been implicated in irreversible cell damage following ischemia-reperfusion (I/R) injury. We examined the protective effect of PX-18, a novel sP
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781461374305
Previously we reported that PGBx, a prostaglandin oligomer with anti-inflammatory activity, inhibited 14 kDa phospholipase A2 (PLA2) activity and blocked arachidonic acid mobilization in prelabeled human neutrophils (Biochim. Biophys. Acta 1006:272-2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d4520d27cf3d6c06683d4013fa09d47
https://doi.org/10.1007/978-1-4615-5325-0_49
https://doi.org/10.1007/978-1-4615-5325-0_49