title: Cytoskeletons of retinal pigment epithelial cells: interspecies differences of expression patterns indicate independence of cell function from the specific complement of cytoskeletal proteins.
abstract: In vertebrate tissue development a given cell differentiation pathway is usually associated with a pattern of expression of a specific set of cytoskeletal proteins, including different intermediate filament (IF) and junctional proteins, which is identical in diverse species. The retinal pigment epithelium (RPE) is a layer of polar cells that have very similar morphological features and practically identical functions in different vertebrate species. However, in biochemical and immunolocalization studies of the cytoskeletal proteins of these cells we have noted remarkable interspecies differences. While chicken RPE cells contain only IFs of the vimentin type and do not possess desmosomes and desmosomal proteins RPE cells of diverse amphibian (Rana ridibunda, Xenopus laevis) and mammalian (rat, guinea pig, rabbit, cow, human) species express cytokeratins 8 and 18 either as their sole IF proteins, or together with vimentin IFs as in guinea pig and a certain subpopulation of bovine RPE cells. Plakoglobin, a plaque protein common to desmosomes and the zonula adhaerens exists in RPE cells of all species, whereas desmoplakin and desmoglein have been identified only in RPE desmosomes of frogs and cows, including bovine RPE cell cultures in which cytokeratins have disappeared and vimentin IFs are the only IFs present. These challenging findings show that neither cytokeratin IFs nor desmosomes are necessary for the establishment and function of a polar epithelial cell layer and that the same basic cellular architecture can be achieved by different programs of expression of cytoskeletal proteins. The differences in the composition of the RPE cytoskeleton further indicate that, at least in this tissue, a specific program of expression of IF and desmosomal proteins is not related to the functions of the RPE cell, which are very similar in the various species.
authors.affiliation: Division of Membrane Biology and Biochemistry, German Cancer Research Center, Heidelberg.
authors.forename: K
authors.initials: K
authors.lastname: Owaribe
authors.forename: J
authors.initials: J
authors.lastname: Kartenbeck
authors.forename: E
authors.initials: E
authors.lastname: Rungger-Brändle
authors.forename: W W
authors.initials: WW
authors.lastname: Franke
mesh_terms: D000818:Animals; D002417:Cattle; D002645:Chickens; D003598:Cytoskeletal Proteins / Q000032:analysis* / Q000502:physiology; D003599:Cytoskeleton / Q000032:analysis / Q000502:physiology / Q000648:ultrastructure*; D005455:Fluorescent Antibody Technique; D006168:Guinea Pigs; D006801:Humans; D007365:Intercellular Junctions / Q000032:analysis / Q000648:ultrastructure; D007381:Intermediate Filament Proteins / Q000032:analysis; D007382:Intermediate Filaments / Q000648:ultrastructure; D008854:Microscopy, Electron; D010857:Pigment Epithelium of Eye / Q000032:analysis / Q000502:physiology / Q000648:ultrastructure*; D011895:Rana ridibunda; D051381:Rats; D013045:Species Specificity; D014982:Xenopus laevis
chemical_list: D003598:Cytoskeletal Proteins; D007381:Intermediate Filament Proteins