A disease-modifying treatment for Alzheimer's disease: focus on the trans-sulfuration pathway.
Identifieur interne : 000183 ( Main/Exploration ); précédent : 000182; suivant : 000184A disease-modifying treatment for Alzheimer's disease: focus on the trans-sulfuration pathway.
Auteurs : Thomas Berry [Australie] ; Eid Abohamza [Qatar] ; Ahmed A. Moustafa [Australie]Source :
- Reviews in the neurosciences [ 0334-1763 ] ; 2020.
Abstract
High homocysteine levels in Alzheimer's disease (AD) result from low activity of the trans-sulfuration pathway. Glutathione levels are also low in AD. L-cysteine is required for the synthesis of glutathione. The synthesis of coenzyme A (CoA) requires L-cysteine, which is synthesized via the trans-sulfuration pathway. CoA is required for the synthesis of acetylcholine and appropriate cholinergic neurotransmission. L-cysteine is required for the synthesis of molybdenum-containing proteins. Sulfite oxidase (SUOX), which is a molybdenum-containing protein, could be dysregulated in AD. SUOX detoxifies the sulfites. Glutaminergic neurotransmission could be dysregulated in AD due to low levels of SUOX and high levels of sulfites. L-cysteine provides sulfur for iron-sulfur clusters. Oxidative phosphorylation (OXPHOS) is heavily dependent on iron-sulfur proteins. The decrease in OXPHOS seen in AD could be due to dysregulations of the trans-sulfuration pathway. There is a decrease in aconitase 1 (ACO1) in AD. ACO1 is an iron-sulfur enzyme in the citric acid cycle that upon loss of an iron-sulfur cluster converts to iron regulatory protein 1 (IRP1). With the dysregulation of iron-sulfur cluster formation ACO1 will convert to IRP1 which will decrease the 2-oxglutarate synthesis dysregulating the citric acid cycle and also dysregulating iron metabolism. Selenomethionine is also metabolized by the trans-sulfuration pathway. With the low activity of the trans-sulfuration pathway in AD selenoproteins will be dysregulated in AD. Dysregulation of selenoproteins could lead to oxidant stress in AD. In this article, we propose a novel treatment for AD that addresses dysregulations resulting from low activity of the trans-sulfuration pathway and low L-cysteine.
DOI: 10.1515/revneuro-2019-0076
PubMed: 31751299
Affiliations:
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Moustafa</name><affiliation wicri:level="1"><nlm:affiliation>School of Social Sciences and Psychology, Western Sydney University, 2 Bullecourt Ave, Milperra, 2214 Sydney, New South Wales, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Social Sciences and Psychology, Western Sydney University, 2 Bullecourt Ave, Milperra, 2214 Sydney, New South Wales</wicri:regionArea><wicri:noRegion>New South Wales</wicri:noRegion></affiliation></author></analytic><series><title level="j">Reviews in the neurosciences</title><idno type="ISSN">0334-1763</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">High homocysteine levels in Alzheimer's disease (AD) result from low activity of the trans-sulfuration pathway. Glutathione levels are also low in AD. L-cysteine is required for the synthesis of glutathione. The synthesis of coenzyme A (CoA) requires L-cysteine, which is synthesized via the trans-sulfuration pathway. CoA is required for the synthesis of acetylcholine and appropriate cholinergic neurotransmission. L-cysteine is required for the synthesis of molybdenum-containing proteins. Sulfite oxidase (SUOX), which is a molybdenum-containing protein, could be dysregulated in AD. SUOX detoxifies the sulfites. Glutaminergic neurotransmission could be dysregulated in AD due to low levels of SUOX and high levels of sulfites. L-cysteine provides sulfur for iron-sulfur clusters. Oxidative phosphorylation (OXPHOS) is heavily dependent on iron-sulfur proteins. The decrease in OXPHOS seen in AD could be due to dysregulations of the trans-sulfuration pathway. There is a decrease in aconitase 1 (ACO1) in AD. ACO1 is an iron-sulfur enzyme in the citric acid cycle that upon loss of an iron-sulfur cluster converts to iron regulatory protein 1 (IRP1). With the dysregulation of iron-sulfur cluster formation ACO1 will convert to IRP1 which will decrease the 2-oxglutarate synthesis dysregulating the citric acid cycle and also dysregulating iron metabolism. Selenomethionine is also metabolized by the trans-sulfuration pathway. With the low activity of the trans-sulfuration pathway in AD selenoproteins will be dysregulated in AD. Dysregulation of selenoproteins could lead to oxidant stress in AD. In this article, we propose a novel treatment for AD that addresses dysregulations resulting from low activity of the trans-sulfuration pathway and low L-cysteine.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">31751299</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0334-1763</ISSN><JournalIssue CitedMedium="Internet"><Volume>31</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>Apr</Month><Day>28</Day></PubDate></JournalIssue><Title>Reviews in the neurosciences</Title><ISOAbbreviation>Rev Neurosci</ISOAbbreviation></Journal><ArticleTitle>A disease-modifying treatment for Alzheimer's disease: focus on the trans-sulfuration pathway.</ArticleTitle><Pagination><MedlinePgn>319-334</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1515/revneuro-2019-0076</ELocationID><ELocationID EIdType="pii" ValidYN="Y">/j/revneuro.2020.31.issue-3/revneuro-2019-0076/revneuro-2019-0076.xml</ELocationID><Abstract><AbstractText>High homocysteine levels in Alzheimer's disease (AD) result from low activity of the trans-sulfuration pathway. Glutathione levels are also low in AD. L-cysteine is required for the synthesis of glutathione. The synthesis of coenzyme A (CoA) requires L-cysteine, which is synthesized via the trans-sulfuration pathway. CoA is required for the synthesis of acetylcholine and appropriate cholinergic neurotransmission. L-cysteine is required for the synthesis of molybdenum-containing proteins. Sulfite oxidase (SUOX), which is a molybdenum-containing protein, could be dysregulated in AD. SUOX detoxifies the sulfites. Glutaminergic neurotransmission could be dysregulated in AD due to low levels of SUOX and high levels of sulfites. L-cysteine provides sulfur for iron-sulfur clusters. Oxidative phosphorylation (OXPHOS) is heavily dependent on iron-sulfur proteins. The decrease in OXPHOS seen in AD could be due to dysregulations of the trans-sulfuration pathway. There is a decrease in aconitase 1 (ACO1) in AD. ACO1 is an iron-sulfur enzyme in the citric acid cycle that upon loss of an iron-sulfur cluster converts to iron regulatory protein 1 (IRP1). With the dysregulation of iron-sulfur cluster formation ACO1 will convert to IRP1 which will decrease the 2-oxglutarate synthesis dysregulating the citric acid cycle and also dysregulating iron metabolism. Selenomethionine is also metabolized by the trans-sulfuration pathway. With the low activity of the trans-sulfuration pathway in AD selenoproteins will be dysregulated in AD. Dysregulation of selenoproteins could lead to oxidant stress in AD. In this article, we propose a novel treatment for AD that addresses dysregulations resulting from low activity of the trans-sulfuration pathway and low L-cysteine.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Berry</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>School of Social Sciences and Psychology, Western Sydney University, 2 Bullecourt Ave, Milperra, 2214 Sydney, New South Wales, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Abohamza</LastName><ForeName>Eid</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Social Sciences, College of Arts and Sciences, Qatar University, Doha, Qatar.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moustafa</LastName><ForeName>Ahmed A</ForeName><Initials>AA</Initials><AffiliationInfo><Affiliation>School of Social Sciences and Psychology, Western Sydney University, 2 Bullecourt Ave, Milperra, 2214 Sydney, New South Wales, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Rev Neurosci</MedlineTA><NlmUniqueID>8711016</NlmUniqueID><ISSNLinking>0334-1763</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Alzheimer’s disease (AD)</Keyword><Keyword MajorTopicYN="N">amyloid beta</Keyword><Keyword MajorTopicYN="N">cystathionine beta-synthase (CBS)</Keyword><Keyword MajorTopicYN="N">homocysteine</Keyword><Keyword MajorTopicYN="N">trans-sulfuration pathway</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>08</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>08</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>11</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31751299</ArticleId><ArticleId IdType="doi">10.1515/revneuro-2019-0076</ArticleId><ArticleId IdType="pii">/j/revneuro.ahead-of-print/revneuro-2019-0076/revneuro-2019-0076.xml</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>Qatar</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Berry, Thomas" sort="Berry, Thomas" uniqKey="Berry T" first="Thomas" last="Berry">Thomas Berry</name></noRegion><name sortKey="Moustafa, Ahmed A" sort="Moustafa, Ahmed A" uniqKey="Moustafa A" first="Ahmed A" last="Moustafa">Ahmed A. Moustafa</name></country><country name="Qatar"><noRegion><name sortKey="Abohamza, Eid" sort="Abohamza, Eid" uniqKey="Abohamza E" first="Eid" last="Abohamza">Eid Abohamza</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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