Distribution of 125I-ferrotransferrin binding sites in the mesencephalon of control subjects and patients with Parkinson's disease.
Identifieur interne : 001712 ( PubMed/Corpus ); précédent : 001711; suivant : 001713Distribution of 125I-ferrotransferrin binding sites in the mesencephalon of control subjects and patients with Parkinson's disease.
Auteurs : B A Faucheux ; E C Hirsch ; J. Villares ; F. Selimi ; A. Mouatt-Prigent ; F. Javoy-Agid ; J J Hauw ; Y. AgidSource :
- Journal of neurochemistry [ 0022-3042 ] ; 1993.
English descriptors
- KwdEn :
- Aged, Aged, 80 and over, Autoradiography, Brain Stem (metabolism), Humans, Iodine Radioisotopes, Kinetics, Mesencephalon (metabolism), Neurons (metabolism), Organ Specificity, Parkinson Disease (metabolism), Receptors, Transferrin (analysis), Receptors, Transferrin (metabolism), Reference Values, Transferrin (analogs & derivatives), Transferrin (metabolism).
- MESH :
- chemical , analogs & derivatives : Transferrin.
- chemical , analysis : Receptors, Transferrin.
- chemical , metabolism : Receptors, Transferrin, Transferrin.
- chemical : Iodine Radioisotopes.
- metabolism : Brain Stem, Mesencephalon, Neurons, Parkinson Disease.
- Aged, Aged, 80 and over, Autoradiography, Humans, Kinetics, Organ Specificity, Reference Values.
Abstract
Iron is abnormally accumulated in the substantia nigra pars compacta of patients with Parkinson's disease (PD). Because neuronal and glial iron uptake seems to be mediated by the binding of ferrotransferrin to a specific high-affinity receptor on the cell surface, the number of transferrin receptors could be altered in this disease. The regional distribution of specific binding sites for human 125I-diferric transferrin has been studied in the mesencephalon, on cryostat-cut sections from autopsy brains of control subjects and parkinsonian patients by in vitro autoradiography. Densities of binding sites were highest in the central gray substance (approximately 10 fmol/mg of tissue equivalent), intermediate in the catecholaminergic cell group A8, superior colliculus, and ventral tegmental area, and almost nonexistent in the substantia nigra. The density of 125I-transferrin binding sites was not significantly different between parkinsonian and control brains in any region analyzed. These results show that in the mesencephalon the regional density of transferrin binding sites is lowest in the dopaminergic cell groups, which are the most vulnerable to PD, and suggest that iron does not accumulate through an increased density of transferrin receptors at the level of the substantia nigra.
PubMed: 8492137
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Selimi</name></author><author><name sortKey="Mouatt Prigent, A" sort="Mouatt Prigent, A" uniqKey="Mouatt Prigent A" first="A" last="Mouatt-Prigent">A. Mouatt-Prigent</name></author><author><name sortKey="Javoy Agid, F" sort="Javoy Agid, F" uniqKey="Javoy Agid F" first="F" last="Javoy-Agid">F. Javoy-Agid</name></author><author><name sortKey="Hauw, J J" sort="Hauw, J J" uniqKey="Hauw J" first="J J" last="Hauw">J J Hauw</name></author><author><name sortKey="Agid, Y" sort="Agid, Y" uniqKey="Agid Y" first="Y" last="Agid">Y. Agid</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1993">1993</date><idno type="RBID">pubmed:8492137</idno><idno type="pmid">8492137</idno><idno type="wicri:Area/PubMed/Corpus">001712</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001712</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Distribution of 125I-ferrotransferrin binding sites in the mesencephalon of control subjects and patients with Parkinson's disease.</title><author><name sortKey="Faucheux, B A" sort="Faucheux, B A" uniqKey="Faucheux B" first="B A" last="Faucheux">B A Faucheux</name><affiliation><nlm:affiliation>Laboratoire de Médecine Expérimentale, Physiopathologie et Pathogenèse des Maladies Dégénératives du Système Nerveux, INSERM U289, Hôpital de la Salpêtrière, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hirsch, E C" sort="Hirsch, E C" uniqKey="Hirsch E" first="E C" last="Hirsch">E C Hirsch</name></author><author><name sortKey="Villares, J" sort="Villares, J" uniqKey="Villares J" first="J" last="Villares">J. Villares</name></author><author><name sortKey="Selimi, F" sort="Selimi, F" uniqKey="Selimi F" first="F" last="Selimi">F. Selimi</name></author><author><name sortKey="Mouatt Prigent, A" sort="Mouatt Prigent, A" uniqKey="Mouatt Prigent A" first="A" last="Mouatt-Prigent">A. Mouatt-Prigent</name></author><author><name sortKey="Javoy Agid, F" sort="Javoy Agid, F" uniqKey="Javoy Agid F" first="F" last="Javoy-Agid">F. Javoy-Agid</name></author><author><name sortKey="Hauw, J J" sort="Hauw, J J" uniqKey="Hauw J" first="J J" last="Hauw">J J Hauw</name></author><author><name sortKey="Agid, Y" sort="Agid, Y" uniqKey="Agid Y" first="Y" last="Agid">Y. Agid</name></author></analytic><series><title level="j">Journal of neurochemistry</title><idno type="ISSN">0022-3042</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aged</term><term>Aged, 80 and over</term><term>Autoradiography</term><term>Brain Stem (metabolism)</term><term>Humans</term><term>Iodine Radioisotopes</term><term>Kinetics</term><term>Mesencephalon (metabolism)</term><term>Neurons (metabolism)</term><term>Organ Specificity</term><term>Parkinson Disease (metabolism)</term><term>Receptors, Transferrin (analysis)</term><term>Receptors, Transferrin (metabolism)</term><term>Reference Values</term><term>Transferrin (analogs & derivatives)</term><term>Transferrin (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Transferrin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Receptors, Transferrin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Receptors, Transferrin</term><term>Transferrin</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Iodine Radioisotopes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain Stem</term><term>Mesencephalon</term><term>Neurons</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Aged</term><term>Aged, 80 and over</term><term>Autoradiography</term><term>Humans</term><term>Kinetics</term><term>Organ Specificity</term><term>Reference Values</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron is abnormally accumulated in the substantia nigra pars compacta of patients with Parkinson's disease (PD). Because neuronal and glial iron uptake seems to be mediated by the binding of ferrotransferrin to a specific high-affinity receptor on the cell surface, the number of transferrin receptors could be altered in this disease. The regional distribution of specific binding sites for human 125I-diferric transferrin has been studied in the mesencephalon, on cryostat-cut sections from autopsy brains of control subjects and parkinsonian patients by in vitro autoradiography. Densities of binding sites were highest in the central gray substance (approximately 10 fmol/mg of tissue equivalent), intermediate in the catecholaminergic cell group A8, superior colliculus, and ventral tegmental area, and almost nonexistent in the substantia nigra. The density of 125I-transferrin binding sites was not significantly different between parkinsonian and control brains in any region analyzed. These results show that in the mesencephalon the regional density of transferrin binding sites is lowest in the dopaminergic cell groups, which are the most vulnerable to PD, and suggest that iron does not accumulate through an increased density of transferrin receptors at the level of the substantia nigra.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8492137</PMID><DateCreated><Year>1993</Year><Month>06</Month><Day>15</Day></DateCreated><DateCompleted><Year>1993</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2011</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-3042</ISSN><JournalIssue CitedMedium="Print"><Volume>60</Volume><Issue>6</Issue><PubDate><Year>1993</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Journal of neurochemistry</Title><ISOAbbreviation>J. Neurochem.</ISOAbbreviation></Journal><ArticleTitle>Distribution of 125I-ferrotransferrin binding sites in the mesencephalon of control subjects and patients with Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>2338-41</MedlinePgn></Pagination><Abstract><AbstractText>Iron is abnormally accumulated in the substantia nigra pars compacta of patients with Parkinson's disease (PD). Because neuronal and glial iron uptake seems to be mediated by the binding of ferrotransferrin to a specific high-affinity receptor on the cell surface, the number of transferrin receptors could be altered in this disease. The regional distribution of specific binding sites for human 125I-diferric transferrin has been studied in the mesencephalon, on cryostat-cut sections from autopsy brains of control subjects and parkinsonian patients by in vitro autoradiography. Densities of binding sites were highest in the central gray substance (approximately 10 fmol/mg of tissue equivalent), intermediate in the catecholaminergic cell group A8, superior colliculus, and ventral tegmental area, and almost nonexistent in the substantia nigra. The density of 125I-transferrin binding sites was not significantly different between parkinsonian and control brains in any region analyzed. These results show that in the mesencephalon the regional density of transferrin binding sites is lowest in the dopaminergic cell groups, which are the most vulnerable to PD, and suggest that iron does not accumulate through an increased density of transferrin receptors at the level of the substantia nigra.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Faucheux</LastName><ForeName>B A</ForeName><Initials>BA</Initials><AffiliationInfo><Affiliation>Laboratoire de Médecine Expérimentale, Physiopathologie et Pathogenèse des Maladies Dégénératives du Système Nerveux, INSERM U289, Hôpital de la Salpêtrière, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hirsch</LastName><ForeName>E C</ForeName><Initials>EC</Initials></Author><Author ValidYN="Y"><LastName>Villares</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Selimi</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Mouatt-Prigent</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Javoy-Agid</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Hauw</LastName><ForeName>J J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Agid</LastName><ForeName>Y</ForeName><Initials>Y</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Neurochem</MedlineTA><NlmUniqueID>2985190R</NlmUniqueID><ISSNLinking>0022-3042</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007457">Iodine Radioisotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011990">Receptors, Transferrin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014168">Transferrin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C081199">iodo-ferrotransferrin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000368" MajorTopicYN="N">Aged</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000369" MajorTopicYN="N">Aged, 80 and over</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001345" MajorTopicYN="N">Autoradiography</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001933" MajorTopicYN="N">Brain Stem</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007457" MajorTopicYN="N">Iodine Radioisotopes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008636" MajorTopicYN="N">Mesencephalon</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009928" MajorTopicYN="N">Organ Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011990" MajorTopicYN="N">Receptors, 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