Linked Life Data

11566450

Source:http://linkedlifedata.com/resource/pubmed/id/11566450

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-9-21
pubmed:abstractText
In the present study, we investigated the possible role of oxidative stress and the modulation of phospholipid turnover in two related models of pericyte injury, i.e., treatment with high glucose or advanced glycation end products (AGEs). Growing microcapillary pericytes from bovine retinas in culture were incubated, for 3 weeks, with 20-50 mM glucose or 2-20 microM AGEs, and peroxidation parameters (malondialdehyde, conjugated diene, hydroperoxide, glutathione (GSH) levels and lactate dehydrogenase (LDH) release) were evaluated. Arachidonate (AA) and choline release from membrane phospholipids was determined in pericytes prelabeled with [1-(14)C]arachidonate and [Me-(3)H]choline, respectively, and stimulated with elevated glucose or AGEs for 30 min or 2 h. [1-(14)C]arachidonate and [Me-(3)H]choline incorporation into phospholipids, for 2 h and 3 h respectively, was also studied in conditioned and serum-starved cultures. Finally, lysates of treated and control cells were assayed for cytosolic phospholipase A(2) (cPLA(2)), acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase (AT), CTP:phosphocholine cytidylyltransferase (CT) and microsomal choline phosphotransferase (CPT) enzyme activities. We found that high glucose and AGEs caused neither significant production of reactive oxygen species nor cell toxicity or death, unlike other cell types. Both agents had no significant effect on the cellular ultrastructure, evaluated by light and electron microscopy, AA incorporation and release, cytosolic phospholipase A(2) (cPLA(2)) and AT activities. On the contrary, choline incorporation into phosphatidylcholine, CT and CPT activities were significantly reduced either by 50 mM glucose or 20 microM AGEs. Simultaneously, [Me-(3)H]choline release was significantly stimulated by both agents. We conclude that prolonged treatments with high glucose or AGEs are not able to induce oxidative injury in bovine retinal capillary pericytes. Nevertheless, they do induce phospholipid hydrolysis and phospholipid enzyme activity inhibition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
1533
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
128-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11566450-Animals, pubmed-meshheading:11566450-Arachidonic Acid, pubmed-meshheading:11566450-Caspase 3, pubmed-meshheading:11566450-Caspases, pubmed-meshheading:11566450-Cattle, pubmed-meshheading:11566450-Cell Survival, pubmed-meshheading:11566450-Cells, Cultured, pubmed-meshheading:11566450-Choline, pubmed-meshheading:11566450-Glucose, pubmed-meshheading:11566450-Glycosylation End Products, Advanced, pubmed-meshheading:11566450-L-Lactate Dehydrogenase, pubmed-meshheading:11566450-Lipid Peroxidation, pubmed-meshheading:11566450-Microscopy, Electron, pubmed-meshheading:11566450-Oxidative Stress, pubmed-meshheading:11566450-Pericytes, pubmed-meshheading:11566450-Phospholipids, pubmed-meshheading:11566450-Reactive Oxygen Species, pubmed-meshheading:11566450-Retinal Vessels, pubmed-meshheading:11566450-Serum Albumin, Bovine
pubmed:year
2001
pubmed:articleTitle
High glucose and advanced glycation end products induce phospholipid hydrolysis and phospholipid enzyme inhibition in bovine retinal pericytes.
pubmed:affiliation
Department of Biochemistry, Faculty of Medicine, University of Catania, Viale Andrea Doria 6, 95125, Catania, Italy.
pubmed:publicationType
Journal Article