Effect of glycosaminoglycans accumulation on the non-oxidative sulfur metabolism in mouse model of Sanfilippo syndrome, type B.
Identifieur interne : 000157 ( Main/Exploration ); précédent : 000156; suivant : 000158Effect of glycosaminoglycans accumulation on the non-oxidative sulfur metabolism in mouse model of Sanfilippo syndrome, type B.
Auteurs : Marta Kaczor-Kami Ska [Pologne] ; Kamil Kami Ski [Pologne] ; Krystyna Stali Ska [Pologne] ; Maria Wr Bel [Pologne] ; Arleta Feldman [États-Unis]Source :
- Acta biochimica Polonica [ 1734-154X ] ; 2019.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cystathionine gamma-lyase (génétique), Foie (métabolisme), Glycosaminoglycanes (métabolisme), Humains (MeSH), Héparitine sulfate (métabolisme), Modèles animaux de maladie humaine (MeSH), Mucopolysaccharidose de type III (anatomopathologie), Mucopolysaccharidose de type III (génétique), Mucopolysaccharidose de type III (métabolisme), Myocarde (métabolisme), Rate (métabolisme), Rein (métabolisme), Soufre (métabolisme), Souris (MeSH), Stress oxydatif (génétique), Sulfurtransferases (génétique), Thiosulfate sulfurtransferase (génétique).
- MESH :
- anatomopathologie : Mucopolysaccharidose de type III.
- génétique : Cystathionine gamma-lyase, Mucopolysaccharidose de type III, Stress oxydatif, Sulfurtransferases, Thiosulfate sulfurtransferase.
- métabolisme : Foie, Glycosaminoglycanes, Héparitine sulfate, Mucopolysaccharidose de type III, Myocarde, Rate, Rein, Soufre.
- Animaux, Humains, Modèles animaux de maladie humaine, Souris.
English descriptors
- KwdEn :
- Animals (MeSH), Cystathionine gamma-Lyase (genetics), Disease Models, Animal (MeSH), Glycosaminoglycans (metabolism), Heparitin Sulfate (metabolism), Humans (MeSH), Kidney (metabolism), Liver (metabolism), Mice (MeSH), Mucopolysaccharidosis III (genetics), Mucopolysaccharidosis III (metabolism), Mucopolysaccharidosis III (pathology), Myocardium (metabolism), Oxidative Stress (genetics), Spleen (metabolism), Sulfur (metabolism), Sulfurtransferases (genetics), Thiosulfate Sulfurtransferase (genetics).
- MESH :
- chemical , genetics : Cystathionine gamma-Lyase, Sulfurtransferases, Thiosulfate Sulfurtransferase.
- chemical , metabolism : Glycosaminoglycans, Heparitin Sulfate, Sulfur.
- genetics : Mucopolysaccharidosis III, Oxidative Stress.
- metabolism : Kidney, Liver, Mucopolysaccharidosis III, Myocardium, Spleen.
- pathology : Mucopolysaccharidosis III.
- Animals, Disease Models, Animal, Humans, Mice.
Abstract
Lack of the N-alpha-acetylglucosaminidase gene is responsible for the occurrence of a rare disease - the Sanfilippo syndrome, type B. The result of this gene knock-out is accumulation of glycosaminoglycans (GAGs) - more specifically heparan sulfate - a sulfate rich macromolecule. The sulfur oxidative pathway is involved in the sulfate groups' turnover in the cells. In contrast, the non-oxidative sulfur pathway leads mostly to formation of sulfane sulfur-containing compounds. The aim of our research was to observe an interaction between MPS IIIB and non-oxidative sulfur metabolism. In this work, we examined selected tissues (livers, kidneys, hearts and spleens) of 3 month old mice with confirmed accumulation of GAGs. The activity and expression of three sulfurtransferases (components of non-oxidative sulfur metabolism): rhodanese, 3-mercaptopyruvate sulfurtransferase and cystathionine γ-lyase was determined, as well as the sulfane sulfur level and the level of other low molecular sulfur-containing compounds (reduced and oxidized glutathione, cysteine and cystine). In all tested tissues, the sulfane sulfur and/or sulfurtransferases' activities, as well as the cysteine content, underwent statistically significant changes. These correlations were also related to the sex of the tested animals. The obtained results indicated that accumulation of incompletely degraded GAGs in the tissues had affected the non-oxidative sulfur metabolism.
DOI: 10.18388/abp.2019_2880
PubMed: 31805227
Affiliations:
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11779</wicri:regionArea><wicri:noRegion>New York 11779</wicri:noRegion></affiliation></author></analytic><series><title level="j">Acta biochimica Polonica</title><idno type="eISSN">1734-154X</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cystathionine gamma-Lyase (genetics)</term><term>Disease Models, Animal (MeSH)</term><term>Glycosaminoglycans (metabolism)</term><term>Heparitin Sulfate (metabolism)</term><term>Humans (MeSH)</term><term>Kidney (metabolism)</term><term>Liver (metabolism)</term><term>Mice (MeSH)</term><term>Mucopolysaccharidosis III (genetics)</term><term>Mucopolysaccharidosis III (metabolism)</term><term>Mucopolysaccharidosis III (pathology)</term><term>Myocardium (metabolism)</term><term>Oxidative Stress (genetics)</term><term>Spleen (metabolism)</term><term>Sulfur (metabolism)</term><term>Sulfurtransferases (genetics)</term><term>Thiosulfate Sulfurtransferase (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cystathionine gamma-lyase (génétique)</term><term>Foie (métabolisme)</term><term>Glycosaminoglycanes (métabolisme)</term><term>Humains (MeSH)</term><term>Héparitine sulfate (métabolisme)</term><term>Modèles animaux de maladie humaine (MeSH)</term><term>Mucopolysaccharidose de type III (anatomopathologie)</term><term>Mucopolysaccharidose de type III (génétique)</term><term>Mucopolysaccharidose de type III (métabolisme)</term><term>Myocarde (métabolisme)</term><term>Rate (métabolisme)</term><term>Rein (métabolisme)</term><term>Soufre (métabolisme)</term><term>Souris (MeSH)</term><term>Stress oxydatif (génétique)</term><term>Sulfurtransferases (génétique)</term><term>Thiosulfate sulfurtransferase (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cystathionine gamma-Lyase</term><term>Sulfurtransferases</term><term>Thiosulfate Sulfurtransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycosaminoglycans</term><term>Heparitin Sulfate</term><term>Sulfur</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Mucopolysaccharidose de type III</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mucopolysaccharidosis III</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cystathionine gamma-lyase</term><term>Mucopolysaccharidose de type III</term><term>Stress oxydatif</term><term>Sulfurtransferases</term><term>Thiosulfate sulfurtransferase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Kidney</term><term>Liver</term><term>Mucopolysaccharidosis III</term><term>Myocardium</term><term>Spleen</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Foie</term><term>Glycosaminoglycanes</term><term>Héparitine sulfate</term><term>Mucopolysaccharidose de type III</term><term>Myocarde</term><term>Rate</term><term>Rein</term><term>Soufre</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Mucopolysaccharidosis III</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Disease Models, Animal</term><term>Humans</term><term>Mice</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Modèles animaux de maladie humaine</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lack of the N-alpha-acetylglucosaminidase gene is responsible for the occurrence of a rare disease - the Sanfilippo syndrome, type B. The result of this gene knock-out is accumulation of glycosaminoglycans (GAGs) - more specifically heparan sulfate - a sulfate rich macromolecule. The sulfur oxidative pathway is involved in the sulfate groups' turnover in the cells. In contrast, the non-oxidative sulfur pathway leads mostly to formation of sulfane sulfur-containing compounds. The aim of our research was to observe an interaction between MPS IIIB and non-oxidative sulfur metabolism. In this work, we examined selected tissues (livers, kidneys, hearts and spleens) of 3 month old mice with confirmed accumulation of GAGs. The activity and expression of three sulfurtransferases (components of non-oxidative sulfur metabolism): rhodanese, 3-mercaptopyruvate sulfurtransferase and cystathionine γ-lyase was determined, as well as the sulfane sulfur level and the level of other low molecular sulfur-containing compounds (reduced and oxidized glutathione, cysteine and cystine). In all tested tissues, the sulfane sulfur and/or sulfurtransferases' activities, as well as the cysteine content, underwent statistically significant changes. These correlations were also related to the sex of the tested animals. The obtained results indicated that accumulation of incompletely degraded GAGs in the tissues had affected the non-oxidative sulfur metabolism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31805227</PMID><DateCompleted><Year>2020</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2020</Year><Month>05</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1734-154X</ISSN><JournalIssue CitedMedium="Internet"><Volume>66</Volume><Issue>4</Issue><PubDate><Year>2019</Year><Month>Dec</Month><Day>05</Day></PubDate></JournalIssue><Title>Acta biochimica Polonica</Title><ISOAbbreviation>Acta Biochim Pol</ISOAbbreviation></Journal><ArticleTitle>Effect of glycosaminoglycans accumulation on the non-oxidative sulfur metabolism in mouse model of Sanfilippo syndrome, type B.</ArticleTitle><Pagination><MedlinePgn>567-576</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.18388/abp.2019_2880</ELocationID><Abstract><AbstractText>Lack of the N-alpha-acetylglucosaminidase gene is responsible for the occurrence of a rare disease - the Sanfilippo syndrome, type B. The result of this gene knock-out is accumulation of glycosaminoglycans (GAGs) - more specifically heparan sulfate - a sulfate rich macromolecule. The sulfur oxidative pathway is involved in the sulfate groups' turnover in the cells. In contrast, the non-oxidative sulfur pathway leads mostly to formation of sulfane sulfur-containing compounds. The aim of our research was to observe an interaction between MPS IIIB and non-oxidative sulfur metabolism. In this work, we examined selected tissues (livers, kidneys, hearts and spleens) of 3 month old mice with confirmed accumulation of GAGs. The activity and expression of three sulfurtransferases (components of non-oxidative sulfur metabolism): rhodanese, 3-mercaptopyruvate sulfurtransferase and cystathionine γ-lyase was determined, as well as the sulfane sulfur level and the level of other low molecular sulfur-containing compounds (reduced and oxidized glutathione, cysteine and cystine). In all tested tissues, the sulfane sulfur and/or sulfurtransferases' activities, as well as the cysteine content, underwent statistically significant changes. These correlations were also related to the sex of the tested animals. The obtained results indicated that accumulation of incompletely degraded GAGs in the tissues had affected the non-oxidative sulfur metabolism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kaczor-Kamińska</LastName><ForeName>Marta</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Chair of Medical Biochemistry, Jagiellonian University, Medical College, Kraków, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kamiński</LastName><ForeName>Kamil</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Faculty of Chemistry, Jagiellonian University, Kraków, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stalińska</LastName><ForeName>Krystyna</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Kraków, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wróbel</LastName><ForeName>Maria</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Chair of Medical Biochemistry, Jagiellonian University, Medical College, Kraków, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Feldman</LastName><ForeName>Arleta</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Team Sanfilippo Foundation, Ronkonkoma, New York 11779, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Poland</Country><MedlineTA>Acta Biochim Pol</MedlineTA><NlmUniqueID>14520300R</NlmUniqueID><ISSNLinking>0001-527X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006025">Glycosaminoglycans</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>9050-30-0</RegistryNumber><NameOfSubstance UI="D006497">Heparitin Sulfate</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.-</RegistryNumber><NameOfSubstance UI="D013466">Sulfurtransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.1</RegistryNumber><NameOfSubstance UI="D013884">Thiosulfate Sulfurtransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.2</RegistryNumber><NameOfSubstance UI="C021550">3-mercaptopyruvate sulphurtransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.4.1.1</RegistryNumber><NameOfSubstance UI="D003542">Cystathionine gamma-Lyase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003542" MajorTopicYN="N">Cystathionine gamma-Lyase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006025" MajorTopicYN="N">Glycosaminoglycans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006497" MajorTopicYN="N">Heparitin Sulfate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007668" MajorTopicYN="N">Kidney</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009084" MajorTopicYN="N">Mucopolysaccharidosis III</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009206" MajorTopicYN="N">Myocardium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013154" MajorTopicYN="N">Spleen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013466" MajorTopicYN="N">Sulfurtransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013884" MajorTopicYN="N">Thiosulfate Sulfurtransferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>10</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>11</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>12</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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K" first="Krystyna" last="Stali Ska">Krystyna Stali Ska</name><name sortKey="Wr Bel, Maria" sort="Wr Bel, Maria" uniqKey="Wr Bel M" first="Maria" last="Wr Bel">Maria Wr Bel</name></country><country name="États-Unis"><noRegion><name sortKey="Feldman, Arleta" sort="Feldman, Arleta" uniqKey="Feldman A" first="Arleta" last="Feldman">Arleta Feldman</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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