Nonenzymatic glycosylation of tissue and blood proteins.
Identifieur interne : 000589 ( Main/Exploration ); précédent : 000588; suivant : 000590Nonenzymatic glycosylation of tissue and blood proteins.
Auteurs : N. Emekli [Turquie]Source :
- Journal of Marmara University Dental Faculty [ 1018-5992 ] ; 1996.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Collagène (métabolisme), Diabète (diagnostic), Gencive (métabolisme), Glycosylation (MeSH), Humains (MeSH), Produits terminaux de glycation avancée (analyse), Produits terminaux de glycation avancée (métabolisme), Protéines du sang (analyse), Protéines du sang (métabolisme), Rats (MeSH), Réaction de Maillard (MeSH).
- MESH :
- analyse : Produits terminaux de glycation avancée, Protéines du sang.
- diagnostic : Diabète.
- métabolisme : Collagène, Gencive, Produits terminaux de glycation avancée, Protéines du sang.
- Animaux, Bovins, Glycosylation, Humains, Rats, Réaction de Maillard.
English descriptors
- KwdEn :
- Animals (MeSH), Blood Proteins (analysis), Blood Proteins (metabolism), Cattle (MeSH), Collagen (metabolism), Diabetes Mellitus (diagnosis), Gingiva (metabolism), Glycation End Products, Advanced (analysis), Glycation End Products, Advanced (metabolism), Glycosylation (MeSH), Humans (MeSH), Maillard Reaction (MeSH), Rats (MeSH).
- MESH :
- chemical , analysis : Blood Proteins, Glycation End Products, Advanced.
- chemical , metabolism : Blood Proteins, Collagen, Glycation End Products, Advanced.
- diagnosis : Diabetes Mellitus.
- metabolism : Gingiva.
- Animals, Cattle, Glycosylation, Humans, Maillard Reaction, Rats.
Abstract
A brief description of the phenomenon of nonenzymatic glycosylation will be presented, some examples given from the literature and then a brief summary of the results of laboratory research conducted in this area by myself and coworkers since 1981. Excessive glycosylation causes undesirable changes in proteins. Such glycosylation also occurs to collagen in oral tissue. In a study on induced experimental diabetes in rats we observed a defective platelet aggregation curve for gingival collagen. Glycosylation of proteins is known to result in functional defects, for example hemoglobin acquires an increased affinity for oxygen. Glycosylation of rat and bovine lens crystallins has been reported as being an important genesis of cataracts in diabetes. Increased glycosylation of submandibular collagen has been shown to occur in diabetes. However collagen from normal subjects has also been found to show an age related advanced glycosylation end product pigment. Increased platelet membrane protein glycosylation has been reported and the hyperaggregation typically observed in these cases thought to be due to glycosylation. The presence of red cell membrane proteins has also been reported and the impairment of red cell function in diabetes has been reported in cases of excessive glycosylation. According to some investigators cataract formation is prevented by some specific drug which inhibits the glycosylation of lens crystallins. Vitamin C has lowering effects on nonenzymatic glycation. Dentists should take into account the possibility of glycosylation of oral proteins such as collagen in cases of impaired gingiva tooth connection.
PubMed: 9569811
Affiliations:
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Le document en format XML
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Emekli</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Dentistry, Marmara University, Istanbul, Türkiye.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Turquie</country><wicri:regionArea>Department of Biochemistry, Faculty of Dentistry, Marmara University, Istanbul</wicri:regionArea><wicri:noRegion>Istanbul</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1996">1996</date><idno type="RBID">pubmed:9569811</idno><idno type="pmid">9569811</idno><idno type="wicri:Area/Main/Corpus">000582</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000582</idno><idno type="wicri:Area/Main/Curation">000582</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000582</idno><idno type="wicri:Area/Main/Exploration">000582</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Nonenzymatic glycosylation of tissue and blood proteins.</title><author><name sortKey="Emekli, N" sort="Emekli, N" uniqKey="Emekli N" first="N" last="Emekli">N. Emekli</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Dentistry, Marmara University, Istanbul, Türkiye.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Turquie</country><wicri:regionArea>Department of Biochemistry, Faculty of Dentistry, Marmara University, Istanbul</wicri:regionArea><wicri:noRegion>Istanbul</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of Marmara University Dental Faculty</title><idno type="ISSN">1018-5992</idno><imprint><date when="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Blood Proteins (analysis)</term><term>Blood Proteins (metabolism)</term><term>Cattle (MeSH)</term><term>Collagen (metabolism)</term><term>Diabetes Mellitus (diagnosis)</term><term>Gingiva (metabolism)</term><term>Glycation End Products, Advanced (analysis)</term><term>Glycation End Products, Advanced (metabolism)</term><term>Glycosylation (MeSH)</term><term>Humans (MeSH)</term><term>Maillard Reaction (MeSH)</term><term>Rats (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Collagène (métabolisme)</term><term>Diabète (diagnostic)</term><term>Gencive (métabolisme)</term><term>Glycosylation (MeSH)</term><term>Humains (MeSH)</term><term>Produits terminaux de glycation avancée (analyse)</term><term>Produits terminaux de glycation avancée (métabolisme)</term><term>Protéines du sang (analyse)</term><term>Protéines du sang (métabolisme)</term><term>Rats (MeSH)</term><term>Réaction de Maillard (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Blood Proteins</term><term>Glycation End Products, Advanced</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Blood Proteins</term><term>Collagen</term><term>Glycation End Products, Advanced</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Produits terminaux de glycation avancée</term><term>Protéines du sang</term></keywords><keywords scheme="MESH" qualifier="diagnosis" xml:lang="en"><term>Diabetes Mellitus</term></keywords><keywords scheme="MESH" qualifier="diagnostic" xml:lang="fr"><term>Diabète</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Gingiva</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Collagène</term><term>Gencive</term><term>Produits terminaux de glycation avancée</term><term>Protéines du sang</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Glycosylation</term><term>Humans</term><term>Maillard Reaction</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Glycosylation</term><term>Humains</term><term>Rats</term><term>Réaction de Maillard</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A brief description of the phenomenon of nonenzymatic glycosylation will be presented, some examples given from the literature and then a brief summary of the results of laboratory research conducted in this area by myself and coworkers since 1981. Excessive glycosylation causes undesirable changes in proteins. Such glycosylation also occurs to collagen in oral tissue. In a study on induced experimental diabetes in rats we observed a defective platelet aggregation curve for gingival collagen. Glycosylation of proteins is known to result in functional defects, for example hemoglobin acquires an increased affinity for oxygen. Glycosylation of rat and bovine lens crystallins has been reported as being an important genesis of cataracts in diabetes. Increased glycosylation of submandibular collagen has been shown to occur in diabetes. However collagen from normal subjects has also been found to show an age related advanced glycosylation end product pigment. Increased platelet membrane protein glycosylation has been reported and the hyperaggregation typically observed in these cases thought to be due to glycosylation. The presence of red cell membrane proteins has also been reported and the impairment of red cell function in diabetes has been reported in cases of excessive glycosylation. According to some investigators cataract formation is prevented by some specific drug which inhibits the glycosylation of lens crystallins. Vitamin C has lowering effects on nonenzymatic glycation. Dentists should take into account the possibility of glycosylation of oral proteins such as collagen in cases of impaired gingiva tooth connection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9569811</PMID><DateCompleted><Year>1998</Year><Month>05</Month><Day>28</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1018-5992</ISSN><JournalIssue CitedMedium="Print"><Volume>2</Volume><Issue>2-3</Issue><PubDate><Year>1996</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of Marmara University Dental Faculty</Title><ISOAbbreviation>J Marmara Univ Dent Fac</ISOAbbreviation></Journal><ArticleTitle>Nonenzymatic glycosylation of tissue and blood proteins.</ArticleTitle><Pagination><MedlinePgn>530-4</MedlinePgn></Pagination><Abstract><AbstractText>A brief description of the phenomenon of nonenzymatic glycosylation will be presented, some examples given from the literature and then a brief summary of the results of laboratory research conducted in this area by myself and coworkers since 1981. Excessive glycosylation causes undesirable changes in proteins. Such glycosylation also occurs to collagen in oral tissue. In a study on induced experimental diabetes in rats we observed a defective platelet aggregation curve for gingival collagen. Glycosylation of proteins is known to result in functional defects, for example hemoglobin acquires an increased affinity for oxygen. Glycosylation of rat and bovine lens crystallins has been reported as being an important genesis of cataracts in diabetes. Increased glycosylation of submandibular collagen has been shown to occur in diabetes. However collagen from normal subjects has also been found to show an age related advanced glycosylation end product pigment. Increased platelet membrane protein glycosylation has been reported and the hyperaggregation typically observed in these cases thought to be due to glycosylation. The presence of red cell membrane proteins has also been reported and the impairment of red cell function in diabetes has been reported in cases of excessive glycosylation. According to some investigators cataract formation is prevented by some specific drug which inhibits the glycosylation of lens crystallins. Vitamin C has lowering effects on nonenzymatic glycation. Dentists should take into account the possibility of glycosylation of oral proteins such as collagen in cases of impaired gingiva tooth connection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Emekli</LastName><ForeName>N</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Dentistry, Marmara University, Istanbul, Türkiye.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Turkey</Country><MedlineTA>J Marmara Univ Dent Fac</MedlineTA><NlmUniqueID>9114162</NlmUniqueID><ISSNLinking>1018-5992</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001798">Blood Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017127">Glycation End Products, Advanced</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-34-5</RegistryNumber><NameOfSubstance UI="D003094">Collagen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>D</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001798" MajorTopicYN="N">Blood Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003094" MajorTopicYN="N">Collagen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003920" MajorTopicYN="N">Diabetes Mellitus</DescriptorName><QualifierName UI="Q000175" MajorTopicYN="N">diagnosis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005881" MajorTopicYN="N">Gingiva</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017127" MajorTopicYN="N">Glycation End Products, Advanced</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015416" MajorTopicYN="N">Maillard Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>43</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>5</Month><Day>7</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9569811</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Turquie</li></country></list><tree><country name="Turquie"><noRegion><name sortKey="Emekli, N" sort="Emekli, N" uniqKey="Emekli N" first="N" last="Emekli">N. 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