Literature DB >> 3690834

Glycation of platelet protein in diabetes mellitus: lack of correlation with platelet function.

R W Yatscoff1, A Mehta, J M Gerrard, J Thliveris.   

Abstract

The relationship of nonenzymatic glycation of platelet proteins to altered platelet function was studied in 33 diabetic patients. Platelets isolated from diabetic patients were glycated to a greater extent than those isolated from nondiabetic controls. No relationship was found between the level of glycation of platelets in diabetics to parameters commonly used to monitor glycemic control (glycated hemoglobin, glycated albumin, fasting blood glucose). Platelets isolated from diabetics did not show an increased level of aggregation and Thromboxane B2 production as compared to nondiabetic controls. No significant relationship was found between the level of glycation and percent aggregation of platelets. The lack of a relationship between glycation and aggregation suggests that the former may not be responsible for the functional changes in platelets seen in diabetics.

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Year:  1987        PMID: 3690834     DOI: 10.1016/s0009-9120(87)80087-5

Source DB:  PubMed          Journal:  Clin Biochem        ISSN: 0009-9120            Impact factor:   3.281


  4 in total

Review 1.  The role of axonal cytoskeleton in diabetic neuropathy.

Authors:  W G McLean
Journal:  Neurochem Res       Date:  1997-08       Impact factor: 3.996

2.  Increased permeability across the blood-nerve barrier of albumin glycated in vitro and in vivo from patients with diabetic polyneuropathy.

Authors:  J F Poduslo; G L Curran
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-15       Impact factor: 11.205

3.  Posttranslational modifications of nerve cytoskeletal proteins in experimental diabetes.

Authors:  W G McLean; C Pekiner; N A Cullum; I F Casson
Journal:  Mol Neurobiol       Date:  1992 Summer-Fall       Impact factor: 5.590

4.  Binding and transcytosis of glycoalbumin by the microvascular endothelium of the murine myocardium: evidence that glycoalbumin behaves as a bifunctional ligand.

Authors:  D Predescu; M Simionescu; N Simionescu; G E Palade
Journal:  J Cell Biol       Date:  1988-11       Impact factor: 10.539

  4 in total

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