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Glycation of plasma low density lipoproteins increases interaction with arterial proteoglycans
The increased susceptibility to atherosclerosis of diabetic individuals, may result from diabetes-associated modification in plasma low density lipoproteins (LDL) which enhance their interaction with arterial extracellular matrix proteoglycans. Using a nonhuman primate model for human diabetes, stud...
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| Published in: | Diabetes research and clinical practice 1999-10, Vol.46 (1), p.9-18 |
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| container_issue | 1 |
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| container_title | Diabetes research and clinical practice |
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| creator | Edwards, I.J. Wagner, J.D. Litwak, K.N. Rudel, L.L. Cefalu, W.T. |
| description | The increased susceptibility to atherosclerosis of diabetic individuals, may result from diabetes-associated modification in plasma low density lipoproteins (LDL) which enhance their interaction with arterial extracellular matrix proteoglycans. Using a nonhuman primate model for human diabetes, studies were conducted to examine diabetes-induced changes in LDL. Plasma LDL were isolated from control (
n=4) and streptozotocin-induced diabetic (
n=3) cynomolgus macaques by differential ultracentrifugation. An in vitro binding assay was used to measure LDL interaction with arterial proteoglycans. Significantly more diabetic LDL bound to proteoglycans than control LDL (12.9±0.7 μg LDL cholesterol/μg proteoglycan versus 8.9±0.5 μg LDL cholesterol/μg proteoglycan (mean±S.E.M.),
P |
| doi_str_mv | 10.1016/S0168-8227(99)00074-1 |
| format | article |
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n=4) and streptozotocin-induced diabetic (
n=3) cynomolgus macaques by differential ultracentrifugation. An in vitro binding assay was used to measure LDL interaction with arterial proteoglycans. Significantly more diabetic LDL bound to proteoglycans than control LDL (12.9±0.7 μg LDL cholesterol/μg proteoglycan versus 8.9±0.5 μg LDL cholesterol/μg proteoglycan (mean±S.E.M.),
P<0.005). Glycation of LDL, determined by fructosamine content, was significantly enhanced in diabetic versus control animals (37±3.1 versus 20±1.5 μmol/l (mean±S.E.M.)
P<0.005). The correlation coefficient between fructosamine content of LDL and its binding to arterial proteoglycans was 0.95. No LDL compositional variables other than glycation correlated with proteoglycan binding. Removal of the glycated portion of LDL from diabetic animals returned LDL proteoglycan binding to normal. These data demonstrate that the diabetes induced glycation of LDL increases its proteoglycan binding properties: thus, a critical mechanism in atherosclerosis, enhanced LDL interaction with arterial proteoglycans, may be accelerated by the diabetic state.</description><identifier>ISSN: 0168-8227</identifier><identifier>EISSN: 1872-8227</identifier><identifier>DOI: 10.1016/S0168-8227(99)00074-1</identifier><identifier>PMID: 10580610</identifier><identifier>CODEN: DRCPE9</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Animals ; Aorta, Thoracic - physiology ; Aorta, Thoracic - physiopathology ; Associated diseases and complications ; Atherosclerosis ; Biological and medical sciences ; Diabetes ; Diabetes Mellitus, Experimental - blood ; Diabetes Mellitus, Experimental - physiopathology ; Diabetes. Impaired glucose tolerance ; Endocrine pancreas. Apud cells (diseases) ; Endocrinopathies ; Glycation ; Glycosylation ; Humans ; Kinetics ; Lipoproteins, LDL - blood ; Low density lipoproteins ; Macaca fascicularis ; Male ; Medical sciences ; Proteoglycans ; Proteoglycans - metabolism ; Reference Values</subject><ispartof>Diabetes research and clinical practice, 1999-10, Vol.46 (1), p.9-18</ispartof><rights>1999 Elsevier Science Ireland Ltd</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-9a8372516617a6fa517ee691253413dff0c5d2c85f20162b40b3d0db22c0bd63</citedby><cites>FETCH-LOGICAL-c390t-9a8372516617a6fa517ee691253413dff0c5d2c85f20162b40b3d0db22c0bd63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1182174$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10580610$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Edwards, I.J.</creatorcontrib><creatorcontrib>Wagner, J.D.</creatorcontrib><creatorcontrib>Litwak, K.N.</creatorcontrib><creatorcontrib>Rudel, L.L.</creatorcontrib><creatorcontrib>Cefalu, W.T.</creatorcontrib><title>Glycation of plasma low density lipoproteins increases interaction with arterial proteoglycans</title><title>Diabetes research and clinical practice</title><addtitle>Diabetes Res Clin Pract</addtitle><description>The increased susceptibility to atherosclerosis of diabetic individuals, may result from diabetes-associated modification in plasma low density lipoproteins (LDL) which enhance their interaction with arterial extracellular matrix proteoglycans. Using a nonhuman primate model for human diabetes, studies were conducted to examine diabetes-induced changes in LDL. Plasma LDL were isolated from control (
n=4) and streptozotocin-induced diabetic (
n=3) cynomolgus macaques by differential ultracentrifugation. An in vitro binding assay was used to measure LDL interaction with arterial proteoglycans. Significantly more diabetic LDL bound to proteoglycans than control LDL (12.9±0.7 μg LDL cholesterol/μg proteoglycan versus 8.9±0.5 μg LDL cholesterol/μg proteoglycan (mean±S.E.M.),
P<0.005). Glycation of LDL, determined by fructosamine content, was significantly enhanced in diabetic versus control animals (37±3.1 versus 20±1.5 μmol/l (mean±S.E.M.)
P<0.005). The correlation coefficient between fructosamine content of LDL and its binding to arterial proteoglycans was 0.95. No LDL compositional variables other than glycation correlated with proteoglycan binding. Removal of the glycated portion of LDL from diabetic animals returned LDL proteoglycan binding to normal. These data demonstrate that the diabetes induced glycation of LDL increases its proteoglycan binding properties: thus, a critical mechanism in atherosclerosis, enhanced LDL interaction with arterial proteoglycans, may be accelerated by the diabetic state.</description><subject>Animals</subject><subject>Aorta, Thoracic - physiology</subject><subject>Aorta, Thoracic - physiopathology</subject><subject>Associated diseases and complications</subject><subject>Atherosclerosis</subject><subject>Biological and medical sciences</subject><subject>Diabetes</subject><subject>Diabetes Mellitus, Experimental - blood</subject><subject>Diabetes Mellitus, Experimental - physiopathology</subject><subject>Diabetes. Impaired glucose tolerance</subject><subject>Endocrine pancreas. Apud cells (diseases)</subject><subject>Endocrinopathies</subject><subject>Glycation</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Lipoproteins, LDL - blood</subject><subject>Low density lipoproteins</subject><subject>Macaca fascicularis</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Proteoglycans</subject><subject>Proteoglycans - metabolism</subject><subject>Reference Values</subject><issn>0168-8227</issn><issn>1872-8227</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNqFkMFO3DAQhi1EBVvgEahyQFU5pHicxIlPVYVaqITUQzljOfaEunLiYGdB-_Z1khXl1ottjb5_ZvwRcg70M1DgV7_S0eQNY_UnIS4ppXWZwwHZQFOzpXxINq_IMXkf458E8aKsjsgx0KqhHOiGPNy4nVaT9UPmu2x0KvYqc_4lMzhEO-0yZ0c_Bj-hHWJmBx1QRZxfEwall-CLnX5nKqSCVS5bYP84tx3iKXnXKRfxbH-fkPvv3-6vb_O7nzc_rr_e5boQdMqFaoqaVcA51Ip3qoIakQtgVVFCYbqO6sow3VQdS39ibUnbwlDTMqZpa3hxQj6ubdPwpy3GSfY2anRODei3UXJRAKNCJLBaQR18jAE7OQbbq7CTQOXsVS5e5SxNCiEXrxJS7sN-wLbt0bxJrSITcLEHVNTKdUEN2sZ_HDQM6jJhX1YMk4xni0FGbXHQaGxAPUnj7X82-Qs00ZXD</recordid><startdate>19991001</startdate><enddate>19991001</enddate><creator>Edwards, I.J.</creator><creator>Wagner, J.D.</creator><creator>Litwak, K.N.</creator><creator>Rudel, L.L.</creator><creator>Cefalu, W.T.</creator><general>Elsevier Ireland Ltd</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19991001</creationdate><title>Glycation of plasma low density lipoproteins increases interaction with arterial proteoglycans</title><author>Edwards, I.J. ; Wagner, J.D. ; Litwak, K.N. ; Rudel, L.L. ; Cefalu, W.T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-9a8372516617a6fa517ee691253413dff0c5d2c85f20162b40b3d0db22c0bd63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Aorta, Thoracic - physiology</topic><topic>Aorta, Thoracic - physiopathology</topic><topic>Associated diseases and complications</topic><topic>Atherosclerosis</topic><topic>Biological and medical sciences</topic><topic>Diabetes</topic><topic>Diabetes Mellitus, Experimental - blood</topic><topic>Diabetes Mellitus, Experimental - physiopathology</topic><topic>Diabetes. Impaired glucose tolerance</topic><topic>Endocrine pancreas. Apud cells (diseases)</topic><topic>Endocrinopathies</topic><topic>Glycation</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Lipoproteins, LDL - blood</topic><topic>Low density lipoproteins</topic><topic>Macaca fascicularis</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Proteoglycans</topic><topic>Proteoglycans - metabolism</topic><topic>Reference Values</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Edwards, I.J.</creatorcontrib><creatorcontrib>Wagner, J.D.</creatorcontrib><creatorcontrib>Litwak, K.N.</creatorcontrib><creatorcontrib>Rudel, L.L.</creatorcontrib><creatorcontrib>Cefalu, W.T.</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>MEDLINE - Academic</collection><jtitle>Diabetes research and clinical practice</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Edwards, I.J.</au><au>Wagner, J.D.</au><au>Litwak, K.N.</au><au>Rudel, L.L.</au><au>Cefalu, W.T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycation of plasma low density lipoproteins increases interaction with arterial proteoglycans</atitle><jtitle>Diabetes research and clinical practice</jtitle><addtitle>Diabetes Res Clin Pract</addtitle><date>1999-10-01</date><risdate>1999</risdate><volume>46</volume><issue>1</issue><spage>9</spage><epage>18</epage><pages>9-18</pages><issn>0168-8227</issn><eissn>1872-8227</eissn><coden>DRCPE9</coden><abstract>The increased susceptibility to atherosclerosis of diabetic individuals, may result from diabetes-associated modification in plasma low density lipoproteins (LDL) which enhance their interaction with arterial extracellular matrix proteoglycans. Using a nonhuman primate model for human diabetes, studies were conducted to examine diabetes-induced changes in LDL. Plasma LDL were isolated from control (
n=4) and streptozotocin-induced diabetic (
n=3) cynomolgus macaques by differential ultracentrifugation. An in vitro binding assay was used to measure LDL interaction with arterial proteoglycans. Significantly more diabetic LDL bound to proteoglycans than control LDL (12.9±0.7 μg LDL cholesterol/μg proteoglycan versus 8.9±0.5 μg LDL cholesterol/μg proteoglycan (mean±S.E.M.),
P<0.005). Glycation of LDL, determined by fructosamine content, was significantly enhanced in diabetic versus control animals (37±3.1 versus 20±1.5 μmol/l (mean±S.E.M.)
P<0.005). The correlation coefficient between fructosamine content of LDL and its binding to arterial proteoglycans was 0.95. No LDL compositional variables other than glycation correlated with proteoglycan binding. Removal of the glycated portion of LDL from diabetic animals returned LDL proteoglycan binding to normal. These data demonstrate that the diabetes induced glycation of LDL increases its proteoglycan binding properties: thus, a critical mechanism in atherosclerosis, enhanced LDL interaction with arterial proteoglycans, may be accelerated by the diabetic state.</abstract><cop>Shannon</cop><pub>Elsevier Ireland Ltd</pub><pmid>10580610</pmid><doi>10.1016/S0168-8227(99)00074-1</doi><tpages>10</tpages></addata></record> |
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| ispartof | Diabetes research and clinical practice, 1999-10, Vol.46 (1), p.9-18 |
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| subjects | Animals Aorta, Thoracic - physiology Aorta, Thoracic - physiopathology Associated diseases and complications Atherosclerosis Biological and medical sciences Diabetes Diabetes Mellitus, Experimental - blood Diabetes Mellitus, Experimental - physiopathology Diabetes. Impaired glucose tolerance Endocrine pancreas. Apud cells (diseases) Endocrinopathies Glycation Glycosylation Humans Kinetics Lipoproteins, LDL - blood Low density lipoproteins Macaca fascicularis Male Medical sciences Proteoglycans Proteoglycans - metabolism Reference Values |
| title | Glycation of plasma low density lipoproteins increases interaction with arterial proteoglycans |
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