Literature DB >> 3332672

Evidence for heterogeneity in the 160/165 x 10(3) Mr glycoprotein components of desmosomes.

J C Jones1, K L Vikstrom, R D Goldman.   

Abstract

We have prepared both monoclonal and polyclonal antibody preparations directed against the 160/165 x 10(3) Mr glycoproteins (desmogleins) of bovine tongue epithelial desmosomes. The polyclonal antibody preparation recognizes desmosomes in a number of mouse tissues, e.g. mouse skin, heart, bladder and trachea, as determined by immunofluorescence microscopy. Furthermore, the polyclonal antibodies recognize polypeptide(s), present in the high salt, Triton-insoluble residues ('cytoskeleton preparations') of mouse skin, heart, bladder and trachea, which comigrate with the 160/165 x 10(3) Mr glycoproteins of bovine tongue epithelial desmosomes as determined by 'Western' immunoblotting. Conversely, the monoclonal 160/165 x 10(3) Mr antibody preparation recognizes desmosomes of stratified squamous epithelial tissues but not desmosomes in other tissue types. Moreover, whereas the monoclonal antibodies recognize 160/165 x 10(3) Mr polypeptides in mouse skin cell cytoskeletons they show no immunoreactivity with the cytoskeleton preparations of mouse bladder, trachea and heart following immunoblotting. These results suggest therefore that although there are conserved epitopes of the 160/165 x 10(3) Mr glycoproteins there are also epitopes of these molecules which vary from tissue to tissue. Double label immunofluorescence observations of cryostat sections of mouse skin using the monoclonal antibodies and antibodies directed against desmoplakin, a plaque component of desmosomes, reveal that the monoclonal antibodies do not recognize certain desmosomes in basal cells which are recognized by desmoplakin antibodies. Indeed, double label observations of cryostat sections of mouse skin using the monoclonal antibodies and human autoantibodies which react with hemidesmosomal components suggest that the monoclonal antibodies stain desmosomes located along the apical surfaces of basal cells but fail to recognize desmosomes along the lateral surfaces of these same cells.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1987        PMID: 3332672     DOI: 10.1242/jcs.88.4.513

Source DB:  PubMed          Journal:  J Cell Sci        ISSN: 0021-9533            Impact factor:   5.285


  6 in total

1.  Isolation of cDNAs encoding desmosomal plaque proteins: evidence that bovine desmoplakins I and II are derived from two mRNAs and a single gene.

Authors:  K J Green; R D Goldman; R L Chisholm
Journal:  Proc Natl Acad Sci U S A       Date:  1988-04       Impact factor: 11.205

2.  IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions.

Authors:  O Skalli; J C Jones; R Gagescu; R D Goldman
Journal:  J Cell Biol       Date:  1994-04       Impact factor: 10.539

3.  A study of desmosomes in colorectal carcinoma.

Authors:  J E Collins; I Taylor; D R Garrod
Journal:  Br J Cancer       Date:  1990-11       Impact factor: 7.640

Review 4.  Nomenclature of the desmosomal cadherins.

Authors:  R S Buxton; P Cowin; W W Franke; D R Garrod; K J Green; I A King; P J Koch; A I Magee; D A Rees; J R Stanley
Journal:  J Cell Biol       Date:  1993-05       Impact factor: 10.539

5.  Immunochemical characterization of three components of the hemidesmosome and their expression in cultured epithelial cells.

Authors:  D H Klatte; M A Kurpakus; K A Grelling; J C Jones
Journal:  J Cell Biol       Date:  1989-12       Impact factor: 10.539

6.  Formation of hemidesmosomes in vitro by a transformed rat bladder cell line.

Authors:  K S Riddelle; K J Green; J C Jones
Journal:  J Cell Biol       Date:  1991-01       Impact factor: 10.539

  6 in total

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