title: Evidence for heterogeneity in the 160/165 x 10(3) Mr glycoprotein components of desmosomes.
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)
authors.affiliation: Department of Cell Biology and Anatomy, Northwestern University Medical School, Chicago, Illinois 60611.
authors.forename: J C
authors.initials: JC
authors.lastname: Jones
authors.forename: K L
authors.initials: KL
authors.lastname: Vikstrom
authors.forename: R D
authors.initials: RD
authors.lastname: Goldman
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D002417:Cattle; D003598:Cytoskeletal Proteins; D051182:Desmogleins; D051180:Desmoplakins; D003896:Desmosomes / Q000032:analysis*; D004848:Epithelium / Q000032:analysis; D005455:Fluorescent Antibody Technique; D005629:Frozen Sections; D006023:Glycoproteins; D008562:Membrane Glycoproteins / Q000032:analysis* / Q000276:immunology; D051379:Mice; D008970:Molecular Weight; D012867:Skin / Q000032:analysis; D014059:Tongue / Q000032:analysis
chemical_list: D000911:Antibodies, Monoclonal; D003598:Cytoskeletal Proteins; D051182:Desmogleins; D051180:Desmoplakins; C495295:Dsp protein, mouse; D006023:Glycoproteins; D008562:Membrane Glycoproteins