Linked Life Data

11423489

Source:http://linkedlifedata.com/resource/pubmed/id/11423489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2001-6-25
pubmed:abstractText
An immunochemical and biochemical study was performed to reveal which of the endothelial plasma membrane proteins become glycated during the early phases of diabetes. The blood front of the lung microvascular endothelial plasmalemma was purified by the cationic colloidal silica method from normal and diabetic (streptozotocin-induced) rats and comparatively analyzed by two-dimensional electrophoresis. No major qualitative differences in the general spectrum of endothelial plasmalemmal proteins were recorded between normoglycemic and hyperglycemic animals. By probing with anti-glucitollysine antibodies, we found that at 1 month after the onset of diabetes, several endothelial membrane polypeptides contained glucose covalently linked to their lysyl residues. Ten days of insulin treatment restored euglycemia in the diabetic animals and completely abolished the membrane nonenzymatic glycosylation. All the glycated polypeptides of the endothelial plasma membrane belong to the peripheral type and are associated with its cytoplasmic face (cell cortex). They were solubilized by buffers of high pH and were not detected in the lung cytosolic fraction (100,000 g). By microsequencing, the major proteins labeled by the anti-glucitollysine have been identified as being actin, annexin I, annexin II, the p34 subunit of the Arp2/3 complex, and the Ras suppressor protein-1. Conversely, the intrinsic endothelial membrane proteins do not seem to be affected by hyperglycemia. This defines the internal face of the endothelial plasma membrane, particularly the cortical cytoskeleton, as a preferential target for nonenzymatic glycosylation in diabetes, with possible consequences on the fluidity of the endothelial plasmalemma and impairment of the endothelial mechanotransducing ability.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1666-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11423489-Actins, pubmed-meshheading:11423489-Amino Acid Sequence, pubmed-meshheading:11423489-Animals, pubmed-meshheading:11423489-Annexin A1, pubmed-meshheading:11423489-Annexin A2, pubmed-meshheading:11423489-Antibodies, Monoclonal, pubmed-meshheading:11423489-Blotting, Western, pubmed-meshheading:11423489-Cell Membrane, pubmed-meshheading:11423489-Diabetes Mellitus, Experimental, pubmed-meshheading:11423489-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:11423489-Endothelium, Vascular, pubmed-meshheading:11423489-Glucose, pubmed-meshheading:11423489-Hydrogen-Ion Concentration, pubmed-meshheading:11423489-Lysine, pubmed-meshheading:11423489-Male, pubmed-meshheading:11423489-Molecular Sequence Data, pubmed-meshheading:11423489-Rats, pubmed-meshheading:11423489-Rats, Sprague-Dawley
pubmed:year
2001
pubmed:articleTitle
Actin and annexins I and II are among the main endothelial plasmalemma-associated proteins forming early glucose adducts in experimental diabetes.
pubmed:affiliation
Département de Pathologie et Biologie Cellulaire, Université de Montréal, P.O. Box 6128, Succursale Centre-ville, Montréal (Québec) H3C 3J7, Canada. ghitsecd@patho.umontreal.ca
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't