A potential role for the COOH-terminal domain in the lateral packing of type III intermediate filaments

Απλή σελίδα τεκμηρίου
dc.contributor.authorKouklis, P. D.en
dc.contributor.authorPapamarcaki, T.en
dc.contributor.authorMerdes, A.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:39:46Z
dc.date.available2015-11-24T19:39:46Z
dc.identifier.issn0021-9525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24271
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectAntibodies, Anti-Idiotypic/diagnostic useen
dc.subjectAntibodies, Monoclonal/diagnostic useen
dc.subjectBinding Sites, Antibodyen
dc.subjectCell Lineen
dc.subjectDesmin/metabolismen
dc.subjectEpitopes/analysisen
dc.subjectImmunoblottingen
dc.subjectIntermediate Filament Proteins/immunology/*metabolism/ultrastructureen
dc.subject*Membrane Glycoproteinsen
dc.subjectMiceen
dc.subjectMicroscopy, Immunoelectronen
dc.subject*Nerve Tissue Proteinsen
dc.subjectNeuropeptides/metabolismen
dc.subjectVimentin/metabolismen
dc.titleA potential role for the COOH-terminal domain in the lateral packing of type III intermediate filamentsen
heal.abstractTo identify sites of self-association in type III intermediate filament (IF) proteins, we have taken an "anti-idiotypic antibody" approach. A mAb (anti-Ct), recognizing a similar feature near the end of the rod domain of vimentin, desmin, and peripherin (epsilon site or epsilon epitope), was characterized. Anti-idiotypic antibodies, generated by immunizing rabbits with purified anti-Ct, recognize a site (presumably "complementary" to the epsilon epitope) common among vimentin, desmin, and peripherin (beta site or beta epitope). The beta epitope is represented in a synthetic peptide (PII) modeled after the 30 COOH-terminal residues of peripherin, as seen by comparative immunoblotting assays. Consistent with the idea of an association between the epsilon and the beta site, PII binds in vitro to intact IF proteins and fragments containing the epsilon epitope, but not to IF proteins that do not react with anti-Ct. Microinjection experiments conducted in vivo and filament reconstitution assays carried out in vitro further demonstrate that "uncoupling" of this site-specific association (by competition with PII or anti-Ct) interferes with normal IF architecture, resulting in the formation of filaments and filament bundles with diameters much greater than that of the normal IFs. These thick fibers are very similar to the ones observed previously when a derivative of desmin missing 27 COOH-terminal residues was assembled in vitro (Kaufmann, E., K. Weber, and N. Geisler. 1985. J. Mol. Biol. 185:733-742). As a molecular explanation, we propose here that the epsilon and the beta sites of type III IF proteins are "complementary" and associate during filament assembly. As a result of this association, we further postulate the formation of a surface-exposed "loop" or "hairpin" structure that may sterically prevent inappropriate filament-filament aggregation and regulate filament thickness.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/1714461-
heal.identifier.secondaryhttp://jcb.rupress.org/content/114/4/773.full.pdf-
heal.journalNameJ Cell Biolen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate1991-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

Αρχεία

Πρωτότυπος φάκελος/πακέτο

Προβολή: 1 - 1 of 1
Μικρογραφία εικόνας
Ονομα:
Kouklis-1991-A potential role for.pdf
Μέγεθος:
3.17 MB
Μορφότυπο:
Adobe Portable Document Format
Κατεβάστε

Φάκελος/Πακέτο αδειών

Προβολή: 1 - 1 of 1
Μικρογραφία εικόνας
Ονομα:
license.txt
Μέγεθος:
1.74 KB
Μορφότυπο:
Item-specific license agreed upon to submission
Περιγραφή:
Κατεβάστε

Συλλογές

Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ