PubMed · 6584509
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M Shimono. 1983. [Intercellular junctions in the gingival epithelium].. https://pubmed.ncbi.nlm.nih.gov/6584509/
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The epidermic desmosomes are formed in their molecular structure by transmembrane components from the cytoplasmic plaque. These are linked up to the tonofilaments of keratin forming a continuous proteinic web which is crucial to keep the tissue integrity. The functional and structural deterioration of the desmosomes produces in human clinic a series of very typical skin diseases, the most frecuent of which is the penghigus. In them, some molecular parts of the desmosomes become strange and antigenic and trigger to an autoimmune reaction which produces a blistering disease of serious prognosis. Depending on the affected molecules the clinical manifestation are different and as Antholt says there is to make a distinction of the following varieties: phenfigus vulgaris and vegetant, phenfigus foliaceus and its varietie, phenfigus of herpes shape. For is study, it is necessary to bear in mind the clinic, the histopathology and inmunopathology (Inmunofluorescence). Some other stranger diseases are of a hereditary genetic origin because of mutations in the domains of the desmosomal molecules which produce clinical manifestations of keratodermia, hypotricosis, woolly hair, skin frailty and cardiomyopapathy. Finally, there are bacteriological staphylococcal toxins, "exfoliatin A-toxin" which produce a separation of the extracellular domain of the desmoglein 1 causing the "staphylococical scalded skin syndrome".
A case of generalized atrophic benign epidermolysis bullosa was followed from birth to 14 years of age. Electron microscopy of the blistered skin showed either the absence or greatly reduced hemidesmosomes of a very poorly developed type. In perilesional skin, the frequency of hemidesmosomes was 1/3 to 1/2 of the normal controls. These hemidesmosomes were small and lacked normal ultrastructures. Anchoring filaments did not cluster underneath them, and the anchoring fibrils were also diminished. In view of the published data correlating the genotype to the phenotype, this patient seems to have a homozygous nonsense mutation of the COL17A1 gene encoding collagen XVII. An accumulation of data may eventually enable electron microscopists to estimate the types of gene mutation.
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