Desmosomal Proteins

Skerrow, Christine J.

doi:10.1007/978-3-662-00989-5_38

Cited by 13 publications

(5 citation statements)

References 73 publications

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“…As we and others have not detected PERP in our enriched or purified desmosomal fractions, mostly from bovine muzzle epidermis (see Skerrow and Matoltsy 1974a, 1974b; Drochmans et al 1978; Franke et al 1981, 1982; Gorbsky and Steinberg 1981; Cowin and Garrod 1983; Mueller and Franke 1983; Skerrow and Skerrow 1983; Giudice et al 1984; Cowin et al 1985b, 1986; Skerrow 1986; Godsel et al 2004), we have prepared mono- and polyclonal antibodies (mAbs and pAbs) of high specificity for and avidity to various potential epitope-bearing PERP domains. These antibodies (Abs) have allowed us to detect the PERP molecule as a general and abundant epithelial marker protein in simple, columnar, complex, transitional and stratified epithelia and in the composite junctions of the myocardial intercalated disks, in diverse tumors and in several cell cultures derived from epithelia or carcinomas.…”

Section: Introductionmentioning

confidence: 50%

Transmembrane protein PERP is a component of tessellate junctions and of other junctional and non-junctional plasma membrane regions in diverse epithelial and epithelium-derived cells

et al. 2013

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Protein PERP (p53 apoptosis effector related to PMP-22) is a small (21.4 kDa) transmembrane polypeptide with an amino acid sequence indicative of a tetraspanin character. It is enriched in the plasma membrane and apparently contributes to cell-cell contacts. Hitherto, it has been reported to be exclusively a component of desmosomes of some stratified epithelia. However, by using a series of newly generated mono- and polyclonal antibodies, we show that protein PERP is not only present in all kinds of stratified epithelia but also occurs in simple, columnar, complex and transitional epithelia, in various types of squamous metaplasia and epithelium-derived tumors, in diverse epithelium-derived cell cultures and in myocardial tissue. Immunofluorescence and immunoelectron microscopy allow us to localize PERP predominantly in small intradesmosomal locations and in variously sized, junction-like peri- and interdesmosomal regions (“tessellate junctions”), mostly in mosaic or amalgamated combinations with other molecules believed, to date, to be exclusive components of tight and adherens junctions. In the heart, PERP is a major component of the composite junctions of the intercalated disks connecting cardiomyocytes. Finally, protein PERP is a cobblestone-like general component of special plasma membrane regions such as the bile canaliculi of liver and subapical-to-lateral zones of diverse columnar epithelia and upper urothelial cell layers. We discuss possible organizational and architectonic functions of protein PERP and its potential value as an immunohistochemical diagnostic marker.

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Section: Introductionmentioning

confidence: 50%

Transmembrane protein PERP is a component of tessellate junctions and of other junctional and non-junctional plasma membrane regions in diverse epithelial and epithelium-derived cells

et al. 2013

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“…The results were markedly dependent on the specific fractionation method used, with more or less preserved plaque structures and "contaminations" by other elements, in particular IF bundle residues (e.g., Skerrow and Matoltsy 1974a,b;Drochmans et al 1978;Colaco and Evans 1981;Franke et al 1981;Gorbsky and Steinberg 1981;Mueller and Franke 1983; for review see Skerrow 1986). Although gel Immunoelectron microscopy of an ultrathin section through an epithelium, showing the immunogold decoration (5-nm particles) of desmoplakin at-or nearthe desmosomal plaque structures.…”

Section: Hard-core Anchors Of Cytoskeletal Elements: the Desmosomesmentioning

confidence: 99%

Discovering the Molecular Components of Intercellular Junctions--A Historical View

Franke

2009

Cold Spring Harbor Perspectives in Biology

165

153

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The organization of metazoa is based on the formation of tissues and on tissue-typical functions and these in turn are based on cell -cell connecting structures. In vertebrates, four major forms of cell junctions have been classified and the molecular composition of which has been elucidated in the past three decades: Desmosomes, which connect epithelial and some other cell types, and the almost ubiquitous adherens junctions are based on closely cis-packed glycoproteins, cadherins, which are associated head-to-head with those of the hemi-junction domain of an adjacent cell, whereas their cytoplasmic regions assemble sizable plaques of special proteins anchoring cytoskeletal filaments. In contrast, the tight junctions (TJs) and gap junctions (GJs) are formed by tetraspan proteins (claudins and occludins, or connexins) arranged head-to-head as TJ seal bands or as paracrystalline connexin channels, allowing intercellular exchange of small molecules. The by and large parallel discoveries of the junction protein families are reported.

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“…The cytoplasmic plaque is the binding site for cytokeratin intermediate filaments and is localized subjacent to the membrane core domain (6,10,32,36). Biochemically, the membrane core domain is composed of glycoproteins (the desmogleins [DG]) with apparent relative molecular masses of 150,000 (DGI), 120,000/110,000 (DGII/ DGIII), and 22,000 (DGIV) (2,3,5,22,26,44,45). The membrane core domain is thought to be involved in the adhesive function of the desmosome (5,6,15,34).…”

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confidence: 99%

Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain.

Pasdar¹,

Nelson²

1989

The Journal of Cell Biology

122

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Abstract. Desmosomes are composed of two morphologically and biochemically distinct domains, a cytoplasmic plaque and membrane core. We have initiated a study of the synthesis and assembly of these domains in Madin-Darby canine kidney (MDCK) epithelial cells to understand the mechanisms involved in the formation of desmosomes. Previously, we reported the kinetics of assembly of two components of the cytoplasmic plaque domain, Desmoplakin I/II (Pasdar, M., and W. J. Nelson. 1988. J. Cell Biol. 106:677-685 and 106:687-699. We have now extended this analysis to include a major glycoprotein component of the membrane core domain, Desmoglein I (DGI; M, = 150,000). Using metabolic labeling and inhibitors of glycoprotein processing and intracellular transport, we show that DGI biosynthesis is a sequential process with defined stages. In the absence of cell-cell contact, DGI enters a Triton X-100 soluble pool and is core glycosylated. The soluble DGI is then transported to the Golgi complex where it is first complex glycosylated and then titrated into an insoluble pool. The insoluble pool of DGI is subsequently transported to the plasma membrane and is degraded rapidly (t,, < 4 h). Although this biosynthetic pathway occurs independently of cell-cell contact, induction of cell-cell contact results in dramatic increases in the efficiency and rate of titration of DGI from the soluble to the insoluble pool, and its transport to the plasma membrane where DGI becomes metabolically stable (t,~ > 24 h). Taken together with our previous study of DPI/II, we conclude that newly synthesized components of the cytoplasmic plaque and membrane core domains are processed and assembled with different kinetics indicating that, at least initially, each domain is assembled separately in the cell. However, upon induction of cell-cell contact there is a rapid titration of both components into an insoluble and metabolically stable pool at the plasma membrane that is concurrent with desmosome assembly.

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Desmosomal Proteins

Cited by 13 publications

References 73 publications

Transmembrane protein PERP is a component of tessellate junctions and of other junctional and non-junctional plasma membrane regions in diverse epithelial and epithelium-derived cells

Transmembrane protein PERP is a component of tessellate junctions and of other junctional and non-junctional plasma membrane regions in diverse epithelial and epithelium-derived cells

Discovering the Molecular Components of Intercellular Junctions--A Historical View

Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain.

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