1. Repository of OAI
  2. ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"
  3. Σχολή Επιστημών Υγείας
  4. Τμήμα Ιατρικής
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
Ελληνικά   English  
Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/24665
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPapamarcaki, T.en
dc.contributor.authorKouklis, P. D.en
dc.contributor.authorKreis, T. E.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:42:36Z-
dc.date.available2015-11-24T19:42:36Z-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24665-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectAntibodies, Anti-Idiotypic/immunologyen
dc.subjectAntibodies, Monoclonal/immunologyen
dc.subjectEpitopesen
dc.subjectIntermediate Filament Proteins/immunology/*ultrastructureen
dc.subjectLamin Type Ben
dc.subjectLaminsen
dc.subject*Membrane Glycoproteinsen
dc.subjectMiceen
dc.subject*Nerve Tissue Proteinsen
dc.subjectNuclear Matrix/ultrastructureen
dc.subjectNuclear Proteins/immunology/*ultrastructureen
dc.subjectProtein Bindingen
dc.subjectProtein Conformationen
dc.subjectRatsen
dc.subjectVimentin/immunologyen
dc.titleThe "lamin B-fold". Anti-idiotypic antibodies reveal a structural complementarity between nuclear lamin B and cytoplasmic intermediate filament epitopesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/1718975-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1991-
heal.abstractPrevious studies have shown that nuclear lamin B binds specifically to the C-terminal domains of type III intermediate filament (IF) proteins under in vitro conditions. To further explore such site-specific interactions, we have used a two-step anti-idiotypic antibody approach. First, a monoclonal antibody disrupting the cytoplasmic IF network organization of living cells (mAb7A3) (Matteoni, R., and Kreis, T. E. (1987) J. Cell Biol. 105, 1253-1265) was characterized. Epitope mapping demonstrated that this antibody recognized a site located in the C-terminal domains of vimentin and peripherin (type III IF proteins). mAb7A3 was able to inhibit more than 80% of the in vitro binding of nuclear lamin B to PI, a synthetic peptide modeled after the C-terminal domain of peripherin that comprises a lamin B-binding site (Djabali, K., Portier, M. M., Gros, F., Blobel, G., and Georgatos, S. D. (1991) Cell 64, 109-121). In a second step, animals were immunized with mAb7A3 and the resulting anti-idiotypic sera were screened. Two of these antisera reacted specifically with nuclear lamin B but not with type A lamins or cytoplasmic IF proteins. The anti-lamin B activity of one of the antisera was isolated by affinity chromatography using a lamin B-agarose matrix. The reaction of these affinity-purified antibodies with lamin B was inhibited by mAb7A3. Furthermore, the anti-lamin B antibodies reacted with Fab fragments of mAb7A3 and abolished binding of lamin B to PI. From these data we conclude that anti-idiotypic antibodies against the paratope of mAb7A3 recognize specific epitopes of the lamin B molecule that have shapes complementary to the one of the C-terminal domain of type III IF proteins. We speculate that these (regional) conformations, which we term the "lamin B-fold," may also occur in non-lamin proteins that mediate the anchorage of IFs to various membranous organelles.en
heal.journalNameJ Biol Chemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

Show simple item record
Files in This Item:
File Description SizeFormat 
Georgatos-1991-the lamin b.pdf2.78 MBAdobe PDFView/Open
Show simple item record  


This item is licensed under a Creative Commons License Creative Commons