Absorption Studies on Antigen(s) of the Esophageal Mucosa Reactive with Autoantibodies of Pemphigus

Ablin, Richard J.; Beutner, Ernst H.

doi:10.1159/000230042

Cited by 28 publications

(7 citation statements)

References 3 publications

(4 reference statements)

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“…Since Buetner and Jordan (2) Characterization of the pemphigus antigen from numerous sources has been reported (7,8,9,10 Membrane extraction. Human skin was removed from five belowthe-knee amputations (1 m2) and trimmed of excess fat.…”

Section: Introductionmentioning

confidence: 99%

Isolation and purification of a pemphigus vulgaris antigen from human epidermis.

Peterson¹,

Wuepper²

1984

J. Clin. Invest.

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Abstract. Pemphigus vulgaris is an autoimmune disease associated with an autoantibody directed against a keratinocyte membrane antigen. The purpose ofthis study was to purify the human pemphigus vulgaris antigen, to produce an antibody to this antigen, and to use the antibody to induce pemphigus in newborn mice. Various techniques to extract the membrane-rich pellet from human epidermal homogenate were compared; 1% sodium dodecyl sulfate (SDS) and 1% dimethysulfoxide proved to be superior to extract the pemphigus vulgaris antigen. This antigen was identified by transfer blotting to nitrocellulose paper, incubated with pemphigus vulgaris serum, or 20 control sera, and detected with fluorescein labeled antisera to human IgG.Since concanavalin A inhibits the binding of pemphigus vulgaris antibody to tissue sections, we studied the binding of the extracted proteins to concanavalin A covalently coupled to Sepharose. Pemphigus vulgaris antigen bound to the concanavalin A column and was released by 0.02 M methyl a-D-mannopyranoside. The proteins thus recovered were subjected to AcA 54 gel permeation chromatography, and the pemphigus antigen was detected by the transfer blot assay. The antigen corresponded to a discrete peak at 66,000 D by gel permeation and gave one homogenous band at 33,000 D in urea-SDS-polyacrylamide gel electrophoresis. Monospecific antibody to the antigen raised in rabbits stained human epidermis in the same manner as the pemphigus vulgaris autoantibody and induced pemphigus vulgaris in newborn

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Section: Introductionmentioning

confidence: 99%

Isolation and purification of a pemphigus vulgaris antigen from human epidermis.

Peterson¹,

Wuepper²

1984

J. Clin. Invest.

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“…Pemphigus antigen has been isolated from the water-insoluble fraction of an extract of rabbit esophageal mucosa [23]. Using ethanol extraction of bovine esophageal mucosa, Ablin and Beutner [1][2][3] reported that a 12 000 dalton material bound pemphigus antibody. Extraction of human epidermis [55] and human esophagus [68] with phosphate buffered saline yielded an antigen of mol.wt./68 000 daltons.…”

Section: Pemphigus Antigen(s)mentioning

confidence: 99%

Antibody-induced proteinase activation: A proposed mechanism for pemphigus

Singer

Hashimoto

Lazarus

1981

Springer Semin Immunopathol

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The current state of understanding of pemphigus includes the following: 1. Pemphigus is an autoimmune disease. In all variants a circulating autoantibody is found which binds to epidermal cells. In vivo antibody may be found deposited in the epidermis of patients. 2. The autoantibody levels generally correlate with disease activity indicating a relationship between antibody and clinical disease. 3. Although complement components are found in lesional skin, complement does not appear to be necessary for dissolution of the epidermal cement substance. 4. The treatment of pemphigus with corticosteroids has drastically reduced mortality rates. 5. Three different groups have presented results in two different experimental systems which indicate that subsequent to binding of pemphigus antibody to epidermal cells a proteinase is activated. This proteinase(s) degrades the intercellular cement substance of epidermis which results in loss of cellular adhesion and acantholysis. There are numerous questions still remaining. What is the nature of the proteinase(s) and the surface protein(s) it cleaves? Does the binding of pemphigus antibody to the cell surface induce enzyme synthesis, specific enzyme activation, or generalized lysosomal secretion? The answers to these questions will have broad biologic relevance since they may elucidate the role of anticell surface antibodies in disease states.

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“…In contrast to this little is known about the antigen(s) involved in the production of these antibodies. Efforts to isolate and characterize the antigen had only poor results (Ablin & Beutner, 1968). Some authors suggest that these antigens may be glycoproteins localized in the intercellular areas, or in the surface coat of the epidermal cells (Beutner & Shu, 1973;Grob & Inderbitzin, 1967a;WolfF, 1971).…”

Section: Introductionmentioning

confidence: 99%

The interaction of Concanavalin A and the surface coat of stratified squamous epithelium

Lis

Kalsbeek

2006

British Journal of Dermatology

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SUMMARY The interaction of Concanavalin A (Con A) and the surface membranes of the epithelial cells of human oral mucosa, epidermis and guinea‐pig lip was studied. Two methods were used: fluorescent Con A and Con A in combination with horse radish peroxidase. With both methods the surface coat of epithelial cells was stained. The specificity of the staining methods could be demonstrated. The interaction between pemphigus antibodies and the surface membranes of epithelial cells could be blocked by Con A.

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Absorption Studies on Antigen(s) of the Esophageal Mucosa Reactive with Autoantibodies of Pemphigus

Cited by 28 publications

References 3 publications

Isolation and purification of a pemphigus vulgaris antigen from human epidermis.

Isolation and purification of a pemphigus vulgaris antigen from human epidermis.

Antibody-induced proteinase activation: A proposed mechanism for pemphigus

The interaction of Concanavalin A and the surface coat of stratified squamous epithelium

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