Immunocytochemical identification of epithelium-derived human tumors with antibodies to desmosomal plaque proteins.

Franke, Werner W.; Moll, Roland; Mueller, H.; Schmid, Erika Nardon; Kühn, Caecilia; Krepler, R; Artlieb, U; Denk, Helmut

doi:10.1073/pnas.80.2.543

Cited by 96 publications

(61 citation statements)

References 30 publications

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“…Therefore, it appears to be both a desmosome and a cell surface component. However, immunofluorescence observations with the antibodies to the 140-kDa GP appear to contradict this latter finding; although the antibodies generate a punctate fluorescent staining pattern similar to desmoplakin, a desmosomal plaque protein, in bovine tongue epidermis and cultured cells (2), in some instances, some interdesmosomal staining could be detected (see Fig. 6).…”

Section: Discussionmentioning

confidence: 76%

“…Several components of the cytoplasmic plaque of the desmosome have been identified and characterized (2,3). Other desmosome components have been assigned to the extracellular portion of the desmosome because they are glycosylated and are enriched in desmosomal "cores," which consist of the intercellular region of the desmosome in addition to plasma membrane and plaque remnants (4,5).…”

mentioning

confidence: 99%

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A cell surface desmosome-associated component: identification of tissue-specific cell adhesion molecule.

Jones¹,

Yokoo²,

Goldman³

1986

Proc. Natl. Acad. Sci. U.S.A.

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Autoantibodies in the serum of patients suffering the blistering skin disease pemphigus vulgaris recognize a 140-kDa glycoprotein (GP) present in enriched fractions of bovine tongue epidermal desmosomes. Immunofluorescence observations of cryostat sections of bovine tongue epidermis reveal that afflinity-purified rabbit antibodies to the 140-kDa GP generate a punctate intercellular stain that is similar to that generated by antibodies directed against a desmosome plaque component (desmoplakin). In cultured mouse keratinocytes, the antibodies against 140-kDa GP recognize desmosomes along areas of cell-cell contact. Double immunofluorescence of cultured keratinocytes with these antibodies and a desmoplakin antiserum reveals that the antibodies against the 140-kDa GP stain a single fluorescent line along areas of cell-cell contact. This single fluorescent line lies between double fluorescent lines generated by the desmoplakin antiserum. Immunogold ultrastructural localization reveals that the 140-kDa antigen is localized not only along the intercellular area of the desmosome but also is found along the whole epidermal cell surface. The antiiodies to the 140-kDa GP are able to induce a disruption of cell-cell contact in cultured keratinocytes that possess desmosomes. We propose that the 140-kDa GP is a cell adhesion molecule (CAM). Furthermore we discuss the heterogeneity of desmosomes in the light of our findings that antibodies against the 140-kDa GP recognize specific stratified squamous epithelial tissues.

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Section: Discussionmentioning

confidence: 76%

mentioning

confidence: 99%

A cell surface desmosome-associated component: identification of tissue-specific cell adhesion molecule.

Jones¹,

Yokoo²,

Goldman³

1986

Proc. Natl. Acad. Sci. U.S.A.

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“…3 a and b). This pattern reflects the typical distribution of desmosomes in epidermal tissue (13). With the anti-keratin antiserum, the cytoplasm of all cells within the epidermis is brightly stained (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Normal human serum was used as a control. A rabbit antiserum directed against the socalled "desmoplakin 2" (Mr, 220,000) component of bovine muzzle desmosomes (12,13), a rabbit antiserum directed against the 60K K2 (Mr, 60,000) mouse keratin subunit (9), and a rat monoclonal anti-mouse keratin (14) were also used.…”

Section: Methodsmentioning

confidence: 99%

Human autoantibodies against desmosomes: possible causative factors in pemphigus.

Jones¹,

Arnn²,

Staehelin³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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Pemphigus is a human disease that causes extensive blistering of the skin. This blistering is related to a loss of epidermal cell cohesion and is accompanied by circulating autoantibodies that stain epidermal cell surfaces, as shown by immunofluorescence microscopy. One of the major components involved in epidermal cell cohesion is the desmosome. The pathological changes that accompany pemphigus led us to determine whether the autoantibodies are specific for desmosomes. Incubation of cultured mouse keratinocytes in medium containing pemphigus antiserum leads to cell separation at cell-cell contact sites, which possess desmosomes. Tissue sections of mouse skin processed for indirect immunofluorescence, using pemphigus antiserum or a rabbit antiserum directed against components of desmosomes, show similar punctate cell-surface staining patterns within the epidermis. Cultured mouse keratinocytes possessing well-defined intermediate filament bundles (tonofilaments) and desmosomes were processed for double indirect immunofluorescence, using a monoclonal antibody directed against mouse skin keratin and either pemphigus antiserum or the desmosome antiserum. The keratinocytes exhibit a complex system of keratin-containing tonofilaments. Tonofilaments in contacting cells are separated by thin dark bands at the cell surface, which correspond precisely to desmosomal plaques seen by phase-contrast microscopy. These bands specifically stain with both pemphigus antiserum and the desmosome antiserum. Double indirect immunofluorescence of the cultured mouse keratinocytes, using pemphigus antiserum and the desmosome antiserum, reveals that the pemphigus autoantibodies stain the same areas of cellcell contact as the desmosome antibodies. Our evidence supports the idea that pemphigus blisters form, at least in part, from a specific antibody-induced disruption of desmosomes in the epidermis.

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“…Therefore, molecular markers for cell typing and differentiation have become almost obligatory criteria in pathological diagnoses, in particular of epithelium-derived tumors, for which reliable immunohistochemical marker antibodies are used worldwide [1][2][3][4] (for a review see Chu and Weiss 5 ). However, in the field of mesenchymally derived tumors, the armamentarium of diagnostic markers is still relatively poor and problems of correct identification of certain soft tissue tumors are obvious.…”

mentioning

confidence: 99%

A novel kind of tumor type-characteristic junction: plakophilin-2 as a major protein of adherens junctions in cardiac myxomata

et al. 2010

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Using novel antibodies of high avidity to-and specificity for-the constitutive desmosomal plaque protein, plakophilin-2 (Pkp2), in a systematic study of the molecular composition of junctions connecting the cells of soft tissue tumors, we have discovered with immunocytochemical, biochemical and electron microscopical methods, a novel type of adherens junctions in all 32 cardiac myxomata examined. These junctions contain cadherin-11 as their major transmembrane glycoprotein, which we could repeatedly show in colocalization with N-cadherin, anchored in a cytoplasmic plaque formed by a-and b-catenin, together with the further armadillo-type proteins plakoglobin, p120, p0071 and ARVCF. Surprisingly, all adherens junctions of these tumors contained, in addition, another major armadillo protein Pkp2, hitherto known as an obligatory and characteristic constituent of desmosomes in epithelium-derived tumors. We have not detected Pkp2 in a series of noncardiac myxomata studied in parallel. Therefore, we conclude that this acquisition of Pkp2, which we have recently also observed in some mesenchymally derived cells growing in culture, can also occur in tumorigenic transformations in situ. We propose to examine the marker value of Pkp2 in clinical diagnoses of cardiac myxomata and to develop Pkp2-targeted therapeutic reagents.

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Immunocytochemical identification of epithelium-derived human tumors with antibodies to desmosomal plaque proteins.

Cited by 96 publications

References 30 publications

A cell surface desmosome-associated component: identification of tissue-specific cell adhesion molecule.

A cell surface desmosome-associated component: identification of tissue-specific cell adhesion molecule.

Human autoantibodies against desmosomes: possible causative factors in pemphigus.

A novel kind of tumor type-characteristic junction: plakophilin-2 as a major protein of adherens junctions in cardiac myxomata

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