The effect of δ-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin
Nonenzymatic glycation of proteins and oxidative stress are considered independent factors important in the development of the complications of diabetes but may be interrelated by the process of autoxidative glycation. This pathway involves monosaccharide autoxidation to a reactive ketoaldehyde anal...
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| Veröffentlicht in: | Clinica chimica acta 1997-07, Vol.263 (2), p.239-247 |
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| creator | Lindsay, R.Mark Smith, William Lee, Wai K. Dominiczak, Marek H. Baird, Joyce D. |
| description | Nonenzymatic glycation of proteins and oxidative stress are considered independent factors important in the development of the complications of diabetes but may be interrelated by the process of autoxidative glycation. This pathway involves monosaccharide autoxidation to a reactive ketoaldehyde analogue and subsequent reaction with protein to form a ketoimine adduct. This study demonstrates that δ-gluconolactone (δ-GL), an oxidised analogue of glucose, is a potent glycating agent in vitro of haemoglobin present in blood samples from insulin-dependent diabetic and non-diabetic human subjects and from spontaneously diabetic, insulin-dependent BB/Edinburgh (BB/E) rats. The percentage glycated haemoglobin after incubation (37°C, 5 h) with δ-GL (25 mmol/l) was significantly (
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| doi_str_mv | 10.1016/S0009-8981(97)00067-3 |
| format | Article |
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P<0.002) higher than that observed using an equimolar concentration of glucose. Intravenous administration of δ-GL (1 g/kg) to non-diabetic BB/E rats also significantly increased glycation of haemoglobin (6.0±0.1% vs 4.9±0.1%,
P < 0.01) whereas intravenous injection of an identical dose of glucose had no significant effect (5.1±0.1% vs 5.0±0.2%). These results support the hypothesis that nonenzymatic glycation of proteins involves attachment by both native and oxidised monosaccharides. Further investigation of the interactions between diabetes-associated increases in oxidative stress and glycation on the development and progression of the vascular complications of diabetes is necessary.</description><identifier>ISSN: 0009-8981</identifier><identifier>EISSN: 1873-3492</identifier><identifier>DOI: 10.1016/S0009-8981(97)00067-3</identifier><identifier>PMID: 9246427</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Autoxidative glycation ; BB rat ; Diabetes mellitus ; Diabetes Mellitus, Type 1 - blood ; Diabetic Angiopathies - blood ; Diabetic Angiopathies - etiology ; Gluconates - pharmacology ; Glycated Hemoglobin A - drug effects ; Glycated Hemoglobin A - metabolism ; Glycosylation ; Haemoglobin ; Hemoglobins - drug effects ; Hemoglobins - metabolism ; Humans ; In Vitro Techniques ; Kinetics ; Lactones ; Nonenzymatic glycation ; Oxidation-Reduction ; Oxidative Stress ; Rats ; Rats, Inbred BB</subject><ispartof>Clinica chimica acta, 1997-07, Vol.263 (2), p.239-247</ispartof><rights>1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c360t-96c3b296c96aafdca7a8e82dc32409dd980ae6e4ebd18967c12aae8d8102def43</citedby><cites>FETCH-LOGICAL-c360t-96c3b296c96aafdca7a8e82dc32409dd980ae6e4ebd18967c12aae8d8102def43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0009-8981(97)00067-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9246427$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lindsay, R.Mark</creatorcontrib><creatorcontrib>Smith, William</creatorcontrib><creatorcontrib>Lee, Wai K.</creatorcontrib><creatorcontrib>Dominiczak, Marek H.</creatorcontrib><creatorcontrib>Baird, Joyce D.</creatorcontrib><title>The effect of δ-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin</title><title>Clinica chimica acta</title><addtitle>Clin Chim Acta</addtitle><description>Nonenzymatic glycation of proteins and oxidative stress are considered independent factors important in the development of the complications of diabetes but may be interrelated by the process of autoxidative glycation. This pathway involves monosaccharide autoxidation to a reactive ketoaldehyde analogue and subsequent reaction with protein to form a ketoimine adduct. This study demonstrates that δ-gluconolactone (δ-GL), an oxidised analogue of glucose, is a potent glycating agent in vitro of haemoglobin present in blood samples from insulin-dependent diabetic and non-diabetic human subjects and from spontaneously diabetic, insulin-dependent BB/Edinburgh (BB/E) rats. The percentage glycated haemoglobin after incubation (37°C, 5 h) with δ-GL (25 mmol/l) was significantly (
P<0.002) higher than that observed using an equimolar concentration of glucose. Intravenous administration of δ-GL (1 g/kg) to non-diabetic BB/E rats also significantly increased glycation of haemoglobin (6.0±0.1% vs 4.9±0.1%,
P < 0.01) whereas intravenous injection of an identical dose of glucose had no significant effect (5.1±0.1% vs 5.0±0.2%). These results support the hypothesis that nonenzymatic glycation of proteins involves attachment by both native and oxidised monosaccharides. Further investigation of the interactions between diabetes-associated increases in oxidative stress and glycation on the development and progression of the vascular complications of diabetes is necessary.</description><subject>Animals</subject><subject>Autoxidative glycation</subject><subject>BB rat</subject><subject>Diabetes mellitus</subject><subject>Diabetes Mellitus, Type 1 - blood</subject><subject>Diabetic Angiopathies - blood</subject><subject>Diabetic Angiopathies - etiology</subject><subject>Gluconates - pharmacology</subject><subject>Glycated Hemoglobin A - drug effects</subject><subject>Glycated Hemoglobin A - metabolism</subject><subject>Glycosylation</subject><subject>Haemoglobin</subject><subject>Hemoglobins - drug effects</subject><subject>Hemoglobins - metabolism</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Lactones</subject><subject>Nonenzymatic glycation</subject><subject>Oxidation-Reduction</subject><subject>Oxidative Stress</subject><subject>Rats</subject><subject>Rats, Inbred BB</subject><issn>0009-8981</issn><issn>1873-3492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKxTAQhoMoerw8gtCVKFhN2prLSkS8geBCXYc5yfScSJto04pHfCyfw2cy54JbN8kM_zf_MD8h-4yeMMr46SOlVOVSSXaoxFFquMjLNTJiUpR5WalinYz-kC2yHeNLaivK2SbZVEXFq0KMyNfTFDOsazR9Furs5zufNIMJPjRg-uDxOAOfhQ9nXUSbamjCZMA5uuBiAoLP-mTiE-0_Zy30ziRxZlKRpEROhzaZgLdZB302BWzDpAlj53fJRg1NxL3Vv0Oer6-eLm_z-4ebu8uL-9yUnPa54qYcF-lVHKC2BgRIlIU1ZVFRZa2SFJBjhWPLpOLCsAIApZWMFhbrqtwhB0vf1y68DRh73bposGnAYxiiFooJxs_KBJ4tQdOFGDus9WvnWuhmmlE9T10vUtfzSLUSepG6ns_trxYM4xbt39Qq5qSfL3VMV7477HQ0Dr1B67qUvLbB_bPhF4FXlOA</recordid><startdate>19970725</startdate><enddate>19970725</enddate><creator>Lindsay, R.Mark</creator><creator>Smith, William</creator><creator>Lee, Wai K.</creator><creator>Dominiczak, Marek H.</creator><creator>Baird, Joyce D.</creator><general>Elsevier B.V</general><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>19970725</creationdate><title>The effect of δ-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin</title><author>Lindsay, R.Mark ; Smith, William ; Lee, Wai K. ; Dominiczak, Marek H. ; Baird, Joyce D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c360t-96c3b296c96aafdca7a8e82dc32409dd980ae6e4ebd18967c12aae8d8102def43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Autoxidative glycation</topic><topic>BB rat</topic><topic>Diabetes mellitus</topic><topic>Diabetes Mellitus, Type 1 - blood</topic><topic>Diabetic Angiopathies - blood</topic><topic>Diabetic Angiopathies - etiology</topic><topic>Gluconates - pharmacology</topic><topic>Glycated Hemoglobin A - drug effects</topic><topic>Glycated Hemoglobin A - metabolism</topic><topic>Glycosylation</topic><topic>Haemoglobin</topic><topic>Hemoglobins - drug effects</topic><topic>Hemoglobins - metabolism</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Lactones</topic><topic>Nonenzymatic glycation</topic><topic>Oxidation-Reduction</topic><topic>Oxidative Stress</topic><topic>Rats</topic><topic>Rats, Inbred BB</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lindsay, R.Mark</creatorcontrib><creatorcontrib>Smith, William</creatorcontrib><creatorcontrib>Lee, Wai K.</creatorcontrib><creatorcontrib>Dominiczak, Marek H.</creatorcontrib><creatorcontrib>Baird, Joyce D.</creatorcontrib><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>Clinica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lindsay, R.Mark</au><au>Smith, William</au><au>Lee, Wai K.</au><au>Dominiczak, Marek H.</au><au>Baird, Joyce D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The effect of δ-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin</atitle><jtitle>Clinica chimica acta</jtitle><addtitle>Clin Chim Acta</addtitle><date>1997-07-25</date><risdate>1997</risdate><volume>263</volume><issue>2</issue><spage>239</spage><epage>247</epage><pages>239-247</pages><issn>0009-8981</issn><eissn>1873-3492</eissn><abstract>Nonenzymatic glycation of proteins and oxidative stress are considered independent factors important in the development of the complications of diabetes but may be interrelated by the process of autoxidative glycation. This pathway involves monosaccharide autoxidation to a reactive ketoaldehyde analogue and subsequent reaction with protein to form a ketoimine adduct. This study demonstrates that δ-gluconolactone (δ-GL), an oxidised analogue of glucose, is a potent glycating agent in vitro of haemoglobin present in blood samples from insulin-dependent diabetic and non-diabetic human subjects and from spontaneously diabetic, insulin-dependent BB/Edinburgh (BB/E) rats. The percentage glycated haemoglobin after incubation (37°C, 5 h) with δ-GL (25 mmol/l) was significantly (
P<0.002) higher than that observed using an equimolar concentration of glucose. Intravenous administration of δ-GL (1 g/kg) to non-diabetic BB/E rats also significantly increased glycation of haemoglobin (6.0±0.1% vs 4.9±0.1%,
P < 0.01) whereas intravenous injection of an identical dose of glucose had no significant effect (5.1±0.1% vs 5.0±0.2%). These results support the hypothesis that nonenzymatic glycation of proteins involves attachment by both native and oxidised monosaccharides. Further investigation of the interactions between diabetes-associated increases in oxidative stress and glycation on the development and progression of the vascular complications of diabetes is necessary.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>9246427</pmid><doi>10.1016/S0009-8981(97)00067-3</doi><tpages>9</tpages></addata></record> |
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| ispartof | Clinica chimica acta, 1997-07, Vol.263 (2), p.239-247 |
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| subjects | Animals Autoxidative glycation BB rat Diabetes mellitus Diabetes Mellitus, Type 1 - blood Diabetic Angiopathies - blood Diabetic Angiopathies - etiology Gluconates - pharmacology Glycated Hemoglobin A - drug effects Glycated Hemoglobin A - metabolism Glycosylation Haemoglobin Hemoglobins - drug effects Hemoglobins - metabolism Humans In Vitro Techniques Kinetics Lactones Nonenzymatic glycation Oxidation-Reduction Oxidative Stress Rats Rats, Inbred BB |
| title | The effect of δ-gluconolactone, an oxidised analogue of glucose, on the nonenzymatic glycation of human and rat haemoglobin |
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