Shock membrane electropotential drops and limited diffusive distance of beta-amyloids in cerebral neurons are detrimental enhancement to Alzheimer's diseases.
Identifieur interne : 002007 ( PubMed/Curation ); précédent : 002006; suivant : 002008Shock membrane electropotential drops and limited diffusive distance of beta-amyloids in cerebral neurons are detrimental enhancement to Alzheimer's diseases.
Auteurs : Chi-Huan Chang [République populaire de Chine] ; Chiung-Huei Peng ; Kuan-Chou Chen ; Hsien-Bin Huang ; Wen-Ta Chiu ; Robert Y. PengSource :
- Colloids and surfaces. B, Biointerfaces [ 1873-4367 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Calcium (métabolisme), Chélateurs (pharmacologie), Diffusion, Encéphale (), Encéphale (anatomopathologie), Facteurs temps, Homéostasie (), Maladie d'Alzheimer (physiopathologie), Modèles biologiques, Neurones (), Neurones (anatomopathologie), Peptides bêta-amyloïdes (toxicité), Potentiels de membrane (), Spécificité d'organe (), Viscosité (), Électrolytes.
- MESH :
- anatomopathologie : Encéphale, Neurones.
- métabolisme : Calcium.
- pharmacologie : Chélateurs.
- physiopathologie : Maladie d'Alzheimer.
- toxicité : Peptides bêta-amyloïdes.
- Animaux, Diffusion, Encéphale, Facteurs temps, Homéostasie, Modèles biologiques, Neurones, Potentiels de membrane, Spécificité d'organe, Viscosité, Électrolytes.
English descriptors
- KwdEn :
- Alzheimer Disease (physiopathology), Amyloid beta-Peptides (toxicity), Animals, Brain (drug effects), Brain (pathology), Calcium (metabolism), Chelating Agents (pharmacology), Diffusion, Electrolytes, Homeostasis (drug effects), Membrane Potentials (drug effects), Models, Biological, Neurons (drug effects), Neurons (pathology), Organ Specificity (drug effects), Time Factors, Viscosity (drug effects).
- MESH :
- chemical , metabolism : Calcium.
- chemical , pharmacology : Chelating Agents.
- chemical , toxicity : Amyloid beta-Peptides.
- drug effects : Brain, Homeostasis, Membrane Potentials, Neurons, Organ Specificity, Viscosity.
- pathology : Brain, Neurons.
- physiopathology : Alzheimer Disease.
- Animals, Diffusion, Electrolytes, Models, Biological, Time Factors.
Abstract
Molecular physicobiochemical calculations indicated that the metallic ion binding to beta-amyloids (Abeta) may induce production of hydrogen peroxide, which triggers the Ca ion redistribution from the extracellular to the intracellular compartmentation, resulting in a transient membrane electropotential drop by at least 208.06 mV. Moreover, using the Mark and Houwink empirical equation, we predicted that the diffusible distances of all Abeta identities would be confined in a very tiny region within a radius less than 3.96 x 10(-4)cm in brain at 192h after produced. Because of the inherent tendency of aggregation behaved by the Abetas, the maximum diffusion coefficient and inherent viscosity were 8.24 x 10(-15)cm(2)s(-1) and 72.15 cps for the 12 mers (40.8 kDa), the largest soluble form of ABs. Conclusively, we have quantitatively predicted that the shock membrane potential drop (Deltaphi>208.06 mV) and limited diffusible distance (<3.96 x 10(-4)cm) in the brain would contribute the major detrimental effects to the neurons in the Alzheimer's diseases.
DOI: 10.1016/j.colsurfb.2009.06.004
PubMed: 19574031
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Peng</name></author></analytic><series><title level="j">Colloids and surfaces. 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Moreover, using the Mark and Houwink empirical equation, we predicted that the diffusible distances of all Abeta identities would be confined in a very tiny region within a radius less than 3.96 x 10(-4)cm in brain at 192h after produced. Because of the inherent tendency of aggregation behaved by the Abetas, the maximum diffusion coefficient and inherent viscosity were 8.24 x 10(-15)cm(2)s(-1) and 72.15 cps for the 12 mers (40.8 kDa), the largest soluble form of ABs. Conclusively, we have quantitatively predicted that the shock membrane potential drop (Deltaphi>208.06 mV) and limited diffusible distance (<3.96 x 10(-4)cm) in the brain would contribute the major detrimental effects to the neurons in the Alzheimer's diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19574031</PMID><DateCompleted><Year>2009</Year><Month>12</Month><Day>14</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4367</ISSN><JournalIssue CitedMedium="Internet"><Volume>73</Volume><Issue>2</Issue><PubDate><Year>2009</Year><Month>Oct</Month><Day>15</Day></PubDate></JournalIssue><Title>Colloids and surfaces. B, Biointerfaces</Title><ISOAbbreviation>Colloids Surf B Biointerfaces</ISOAbbreviation></Journal><ArticleTitle>Shock membrane electropotential drops and limited diffusive distance of beta-amyloids in cerebral neurons are detrimental enhancement to Alzheimer's diseases.</ArticleTitle><Pagination><MedlinePgn>339-45</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.colsurfb.2009.06.004</ELocationID><Abstract><AbstractText>Molecular physicobiochemical calculations indicated that the metallic ion binding to beta-amyloids (Abeta) may induce production of hydrogen peroxide, which triggers the Ca ion redistribution from the extracellular to the intracellular compartmentation, resulting in a transient membrane electropotential drop by at least 208.06 mV. Moreover, using the Mark and Houwink empirical equation, we predicted that the diffusible distances of all Abeta identities would be confined in a very tiny region within a radius less than 3.96 x 10(-4)cm in brain at 192h after produced. Because of the inherent tendency of aggregation behaved by the Abetas, the maximum diffusion coefficient and inherent viscosity were 8.24 x 10(-15)cm(2)s(-1) and 72.15 cps for the 12 mers (40.8 kDa), the largest soluble form of ABs. Conclusively, we have quantitatively predicted that the shock membrane potential drop (Deltaphi>208.06 mV) and limited diffusible distance (<3.96 x 10(-4)cm) in the brain would contribute the major detrimental effects to the neurons in the Alzheimer's diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Chi-Huan</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>Graduate Institute of Chemistry and Biochemistry, National Chung Cheng University, Chiayi 43302, Taiwan, ROC.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peng</LastName><ForeName>Chiung-Huei</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Kuan-Chou</ForeName><Initials>KC</Initials></Author><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Hsien-Bin</ForeName><Initials>HB</Initials></Author><Author ValidYN="Y"><LastName>Chiu</LastName><ForeName>Wen-Ta</ForeName><Initials>WT</Initials></Author><Author ValidYN="Y"><LastName>Peng</LastName><ForeName>Robert Y</ForeName><Initials>RY</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>06</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Colloids Surf B Biointerfaces</MedlineTA><NlmUniqueID>9315133</NlmUniqueID><ISSNLinking>0927-7765</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016229">Amyloid beta-Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002614">Chelating 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MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002614" MajorTopicYN="N">Chelating Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004058" MajorTopicYN="N">Diffusion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004573" MajorTopicYN="N">Electrolytes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008564" MajorTopicYN="N">Membrane Potentials</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName 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PubStatus="revised"><Year>2009</Year><Month>05</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>06</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>7</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>7</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>12</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19574031</ArticleId><ArticleId IdType="pii">S0927-7765(09)00242-2</ArticleId><ArticleId IdType="doi">10.1016/j.colsurfb.2009.06.004</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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