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Titolo:
Isoform-specific differences in the size of desmosomal cadherin/catenin complexes
Autore:
Bannon, LJ; Cabrera, BL; Stack, MS; Green, KJ;
Indirizzi:
Northwestern Univ, Sch Med, Dept Pathol & Dermatol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 & Dermatol, Chicago, IL 60611 USA Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 & Mol Biol, Chicago, IL 60611 USA Northwestern Univ, Sch Med, Robert H Lurie Canc Ctr, Chicago, IL 60611 USANorthwestern Univ Chicago IL USA 60611 ie Canc Ctr, Chicago, IL 60611 USA
Titolo Testata:
JOURNAL OF INVESTIGATIVE DERMATOLOGY
fascicolo: 5, volume: 117, anno: 2001,
pagine: 1302 - 1306
SICI:
0022-202X(200111)117:5<1302:IDITSO>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-ORGANIZATION; EXPRESSION PATTERNS; PEMPHIGUS-VULGARIS; HUMAN EPIDERMIS; PLAKOGLOBIN; CADHERINS; IDENTIFICATION; DOMAINS; BINDING; DISTRIBUTIONS;
Keywords:
desmocollin; desmoglein; plakoglobin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Green, KJ Northwestern Univ, Sch Med, Dept Pathol, W127,303 E Chicago Ave,Chicago, IL 60611 USA Northwestern Univ W127,303 E Chicago Ave Chicago IL USA 60611 SA
Citazione:
L.J. Bannon et al., "Isoform-specific differences in the size of desmosomal cadherin/catenin complexes", J INVES DER, 117(5), 2001, pp. 1302-1306

Abstract

Via their integration of the intermediate filament cytoskeleton into the cell membrane, desmosomes facilitate the maintenance of cell shape and tissue integrity as well as intercellular communication. The transmembrane components of the desmosome, the desmogleins and desmocollins, are members of the cadherin family of cell-cell adhesion molecules. Each of these proteins exists as three distinct isoforms, which are the products of individual genes and expressed in a cell-type and differentiation-specific manner. Previous work has suggested that desmoglein 1 binds to its catenin partner, plakoglobin, in an approximately 6:1 stoichiometry. In this study, the molecular organization of complexes formed by plakoglobin and desmoglein 1, 2, or 3 are further examined through immunoprecipitation, size exclusion chromatography and sucrose density sedimentation analysis. It is shown that the complex formed between plakoglobin and desmoglein 1 has an overall molecular weight greater than that of plakoglobin/desmoglein 2 or plakoglobin/desmoglein 3; however, the stoichiometry of the plakoglobin/desmoglein I complex does not appear to exceed 2:1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 00:37:23