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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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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.
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description 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;$P
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Human albumin (ALB) from normal individuals, freshly isolated by CM-Affi-Gel Blue affinity chromatography, was glycated in vitro for 1, 3, 10, 19, and 30 weeks. Glycated ALB (gALB) was separated from the nonglycated form by boronate-affinity chromatography. The efficiency of this separation was assessed by chromatography of ALB glycated with14C glucose and by rechromatography of isolated ALB and gALB after radioiodination. The gALB was also shown to have a higher molecular weight and be completely separated from ALB after SDS/pore gradient electrophoresis in a Tris borate/EDTA buffer. After 1 week of glycation, the gALB PS was 2.2-fold greater than the ALB PS (0.724 ± 0.063 x 10-6vs. 0.328± 0.053 x 10-6ml·g-1·s-1; x̄ ± SD;$P &lt;$0.0001) and it increased with the time of glycation reaching a maximum value of 16.2-fold greater at 30 weeks (4.656 ± 1.117 x 10-6vs. 0.288 ± 0.042 x 10-6ml·g-1·s-1; x̄ ± SD;$P &lt;$0.0001). No change was observed in the residual endoneurial plasma volume. In addition, the PS of gALB isolated from patients with diabetic polyneuropathy was significantly increased ($P &lt;$0.0001) compared to the PS for ALB isolated from the same patients. It is hypothesized that the increased permeability of gALB and presumably other glycated serum components across the blood-nerve barrier, as well as the observed quantitative increase in ALB, IgG, and IgM in sural nerve biopsies from patients with diabetic polyneuropathy contribute to the development of diabetic polyneuropathy over a prolonged period of time by mechanisms that might involve osmotic changes in the nerve microenvironment, direct toxic effects of glycated macromolecules on cells within the endoneurium, or nerve damage by classical immunological mechanisms due to trapping of glycated immunoglobulins within nerve.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.89.6.2218</identifier><identifier>PMID: 1549585</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Albs ; Albumins ; Animals ; Associated diseases and complications ; Biochemistry ; Biological and medical sciences ; Biopsies ; Blood ; Blood plasma ; Chromatography ; Chromatography, Affinity ; Diabetes ; Diabetes complications ; Diabetes. 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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 &lt;$0.0001) and it increased with the time of glycation reaching a maximum value of 16.2-fold greater at 30 weeks (4.656 ± 1.117 x 10-6vs. 0.288 ± 0.042 x 10-6ml·g-1·s-1; x̄ ± SD;$P &lt;$0.0001). No change was observed in the residual endoneurial plasma volume. 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Impaired glucose tolerance</topic><topic>Diabetic neuropathies</topic><topic>Diabetic Neuropathies - blood</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endocrine pancreas. Apud cells (diseases)</topic><topic>Endocrinopathies</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Male</topic><topic>Medical research</topic><topic>Medical sciences</topic><topic>Nerves</topic><topic>Nervous system</topic><topic>Nervous System - blood supply</topic><topic>Nervous System Physiological Phenomena</topic><topic>Permeability</topic><topic>Plasma Volume</topic><topic>Polyneuropathies</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Reference Values</topic><topic>Serum Albumin - isolation &amp; purification</topic><topic>Serum Albumin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Poduslo, Joseph F.</creatorcontrib><creatorcontrib>Curran, Geoffry L.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Poduslo, Joseph F.</au><au>Curran, Geoffry L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Increased Permeability Across the Blood-Nerve Barrier of Albumin Glycated In vitro and In vivo from Patients with Diabetic Polyneuropathy</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1992-03-15</date><risdate>1992</risdate><volume>89</volume><issue>6</issue><spage>2218</spage><epage>2222</epage><pages>2218-2222</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>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 &lt;$0.0001) and it increased with the time of glycation reaching a maximum value of 16.2-fold greater at 30 weeks (4.656 ± 1.117 x 10-6vs. 0.288 ± 0.042 x 10-6ml·g-1·s-1; x̄ ± SD;$P &lt;$0.0001). No change was observed in the residual endoneurial plasma volume. In addition, the PS of gALB isolated from patients with diabetic polyneuropathy was significantly increased ($P &lt;$0.0001) compared to the PS for ALB isolated from the same patients. It is hypothesized that the increased permeability of gALB and presumably other glycated serum components across the blood-nerve barrier, as well as the observed quantitative increase in ALB, IgG, and IgM in sural nerve biopsies from patients with diabetic polyneuropathy contribute to the development of diabetic polyneuropathy over a prolonged period of time by mechanisms that might involve osmotic changes in the nerve microenvironment, direct toxic effects of glycated macromolecules on cells within the endoneurium, or nerve damage by classical immunological mechanisms due to trapping of glycated immunoglobulins within nerve.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1549585</pmid><doi>10.1073/pnas.89.6.2218</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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ispartof Proceedings of the National Academy of Sciences - PNAS, 1992-03, Vol.89 (6), p.2218-2222
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1091-6490
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source JSTOR Archival Journals and Primary Sources Collection; PubMed Central
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
title Increased Permeability Across the Blood-Nerve Barrier of Albumin Glycated In vitro and In vivo from Patients with Diabetic Polyneuropathy
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