Increased Permeability Across the Blood-Nerve Barrier of Albumin Glycated In vitro and In vivo from Patients with Diabetic Polyneuropathy

The blood-nerve transfer of human plasma albumin glycated with D-glucose was investigated by measuring the permeability coefficient-surface area product (PS) of the blood-nerve barrier to radioiodinated albumin in normal adult rat sciatic nerve. Human albumin (ALB) from normal individuals, freshly i...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1992-03, Vol.89 (6), p.2218-2222
Main Authors: Poduslo, Joseph F., Curran, Geoffry L.
Format: Article
Language:English
Subjects:
Albs
Albumins
Animals
Associated diseases and complications
Biochemistry
Biological and medical sciences
Biopsies
Blood
Blood plasma
Chromatography
Chromatography, Affinity
Diabetes
Diabetes complications
Diabetes. Impaired glucose tolerance
Diabetic neuropathies
Diabetic Neuropathies - blood
Electrophoresis, Polyacrylamide Gel
Endocrine pancreas. Apud cells (diseases)
Endocrinopathies
Glycosylation
Humans
Male
Medical research
Medical sciences
Nerves
Nervous system
Nervous System - blood supply
Nervous System Physiological Phenomena
Permeability
Plasma Volume
Polyneuropathies
Rats
Rats, Inbred Strains
Reference Values
Serum Albumin - isolation & purification
Serum Albumin - metabolism
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Summary:The blood-nerve transfer of human plasma albumin glycated with D-glucose was investigated by measuring the permeability coefficient-surface area product (PS) of the blood-nerve barrier to radioiodinated albumin in normal adult rat sciatic nerve. Human albumin (ALB) from normal individuals, freshly isolated by CM-Affi-Gel Blue affinity chromatography, was glycated in vitro for 1, 3, 10, 19, and 30 weeks. Glycated ALB (gALB) was separated from the nonglycated form by boronate-affinity chromatography. The efficiency of this separation was assessed by chromatography of ALB glycated with14C glucose and by rechromatography of isolated ALB and gALB after radioiodination. The gALB was also shown to have a higher molecular weight and be completely separated from ALB after SDS/pore gradient electrophoresis in a Tris borate/EDTA buffer. After 1 week of glycation, the gALB PS was 2.2-fold greater than the ALB PS (0.724 ± 0.063 x 10-6vs. 0.328± 0.053 x 10-6ml·g-1·s-1; x̄ ± SD;$P
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.89.6.2218