Sources/Clones
American Research Products, Biodesign (DP2.15), Boehringer Mannheim (2.15), Chemicon, Cymbus Bioscience (DP2.15), ICI (DP2.17), Progen (DP2.15) and Research Diagnostic Inc (DP2.15).
Fixation/Preparation
Current antibodies are immunoreactive only in fresh-frozen sections or cell preparations.
Background
Epithelial cells contain complexes of cytokeratin filaments (tonofilaments) associated with specific domains of the plasma membrane that appear as symmetrical junctions known as desmosomes or as asymmetrical hemidesmosomes. These regions of filament-membrane-attachment are characterized by 14-20 nm-thick dense plaque; these desmosomal plaques comprise a dense mixture of intracellular attachment proteins including plakoglobin and desmoplakins (Mueller & Franke, 1983). Transmembrane linker proteins, which belong to the cadherin family of cell-cell adhesion molecules, bind to the plaques 2+ and interact through their extracellular domains to hold the adjacent membranes together by a Cadependent mechanism. Desmoplakins I and II (DPI and DPII) are two polypeptides which make up the desmoplakins and are of molecular masses 46 and 24 kD respectively, suggesting that DPI may be a dimer in solution and DPII a monomer (O'Keefe et al, 1989).
Applications
The widespread presence of desmosomes in epithelial cells and their corresponding tumors makes the presence of desmoplakins a specific marker of epithelial differentiation. Unfortunately, these proteins are fixative sensitive, restricting the use of antibodies to desmoplakins to fresh cellular preparations or frozen sections. Applications in diagnostic pathology have therefore been limited to some studies in bullous skin diseases (Burge & Garrod, 1991; Setoyama et al, 1991). In autoimmune acantholytic diseases such as pemphigus vulgaris and pemphigus erythematosus, desmoplakins are intact even in acantholytic cells, whereas in Hailey-Haileys' disease and Dariers' disease the normal plasma membrane localization of desmoplakins is lost and the protein is internalized and present diffusely in the cytoplasm (Setoyama et al, 1991). Desmoplakins have been demonstrated in follicular dendritic cells and their corresponding tumors (Chan et al 1997).
Comments
Acetone fixation followed by plastic embedding allows the immunostaining of the desmoplakins in permanent sections. Trypsin digestion needs to be employed (Carmichael et al, 1991).
References
•Burge SM, Garrod DR 1991 An immunohistological study of desmosomes in Darier's disease and Hailey-Hailey disease. British Journal of Dermatology 124: 242-251.
•armichael RP, McCulloch CA, Zarb GA 1991 Immunohistochemical localization and quantification of desmoplakins I & II and keratins 1 and 19 in plastic-embedded sections of human gingiva. Journal of Histochemistry and Cytochemistry 39: 519-528.
•Chan JK, Fletcher CD, Nayler SJ, Cooper K 1997. Follicular dendritic cell sarcoma. Clinicopathologic analysis of 17 analysis of 17 cases suggesting a malignant potential higher than currently recognized. Cancer 79: 294-313.
•Mueller H, Fanke WW 1983. Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque. Journal of Molecular Biology 163: 647-671.
•O'Keefe EJ, Erickson HP, Bennett V 1989 Desmoplakin I and desmoplakin II. Purification and characterization. Journal of Biological Chemistry 264: 8310-8318.
•Setoyama M, Choi KC, Hashimoto K et al 1991. Desmoplakin I and II in acantholytic dermatoses: preservation in pemphigus vulgaris and pemphigus erythematosus and dissolution in Hailey-Hailey's disease and Darier's disease. Journal of Dermatological Science 1: 9-17.
Bibliografía
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
American Research Products, Biodesign (DP2.15), Boehringer Mannheim (2.15), Chemicon, Cymbus Bioscience (DP2.15), ICI (DP2.17), Progen (DP2.15) and Research Diagnostic Inc (DP2.15).
Fixation/Preparation
Current antibodies are immunoreactive only in fresh-frozen sections or cell preparations.
Background
Epithelial cells contain complexes of cytokeratin filaments (tonofilaments) associated with specific domains of the plasma membrane that appear as symmetrical junctions known as desmosomes or as asymmetrical hemidesmosomes. These regions of filament-membrane-attachment are characterized by 14-20 nm-thick dense plaque; these desmosomal plaques comprise a dense mixture of intracellular attachment proteins including plakoglobin and desmoplakins (Mueller & Franke, 1983). Transmembrane linker proteins, which belong to the cadherin family of cell-cell adhesion molecules, bind to the plaques 2+ and interact through their extracellular domains to hold the adjacent membranes together by a Cadependent mechanism. Desmoplakins I and II (DPI and DPII) are two polypeptides which make up the desmoplakins and are of molecular masses 46 and 24 kD respectively, suggesting that DPI may be a dimer in solution and DPII a monomer (O'Keefe et al, 1989).
Applications
The widespread presence of desmosomes in epithelial cells and their corresponding tumors makes the presence of desmoplakins a specific marker of epithelial differentiation. Unfortunately, these proteins are fixative sensitive, restricting the use of antibodies to desmoplakins to fresh cellular preparations or frozen sections. Applications in diagnostic pathology have therefore been limited to some studies in bullous skin diseases (Burge & Garrod, 1991; Setoyama et al, 1991). In autoimmune acantholytic diseases such as pemphigus vulgaris and pemphigus erythematosus, desmoplakins are intact even in acantholytic cells, whereas in Hailey-Haileys' disease and Dariers' disease the normal plasma membrane localization of desmoplakins is lost and the protein is internalized and present diffusely in the cytoplasm (Setoyama et al, 1991). Desmoplakins have been demonstrated in follicular dendritic cells and their corresponding tumors (Chan et al 1997).
Comments
Acetone fixation followed by plastic embedding allows the immunostaining of the desmoplakins in permanent sections. Trypsin digestion needs to be employed (Carmichael et al, 1991).
References
•Burge SM, Garrod DR 1991 An immunohistological study of desmosomes in Darier's disease and Hailey-Hailey disease. British Journal of Dermatology 124: 242-251.
•armichael RP, McCulloch CA, Zarb GA 1991 Immunohistochemical localization and quantification of desmoplakins I & II and keratins 1 and 19 in plastic-embedded sections of human gingiva. Journal of Histochemistry and Cytochemistry 39: 519-528.
•Chan JK, Fletcher CD, Nayler SJ, Cooper K 1997. Follicular dendritic cell sarcoma. Clinicopathologic analysis of 17 analysis of 17 cases suggesting a malignant potential higher than currently recognized. Cancer 79: 294-313.
•Mueller H, Fanke WW 1983. Biochemical and immunological characterization of desmoplakins I and II, the major polypeptides of the desmosomal plaque. Journal of Molecular Biology 163: 647-671.
•O'Keefe EJ, Erickson HP, Bennett V 1989 Desmoplakin I and desmoplakin II. Purification and characterization. Journal of Biological Chemistry 264: 8310-8318.
•Setoyama M, Choi KC, Hashimoto K et al 1991. Desmoplakin I and II in acantholytic dermatoses: preservation in pemphigus vulgaris and pemphigus erythematosus and dissolution in Hailey-Hailey's disease and Darier's disease. Journal of Dermatological Science 1: 9-17.
Bibliografía
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
