Epidermolysis bullosa summary


Epidermolysis bullosa 

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Epidermolysis bullosa is an uncommon inherited skin disorder caused by a gene mutation in the integrin family of cell adhesion molecules. Integrins have adhesive receptors that are heterodimeric. The receptors have α, and β subunits joined with non-covalent bonds. Integrin α6 is found in multiple tissues except in epithelium cells. Integrin α6 interacts solely with β6 integrin, thus forming the heterodimer α6β4 (Schussler, Olivier, et al.,2021). Genetic mutations interfere with this order. The lethal form of epidermolysis bullosa is because of the occurrence of premature codons in the m-Ribonucleic Acid. Premature termination codons encode either α6 or β4 subunits, thereby triggering quick deterioration of the transcript that has been mutated and the absence of the integrin α6β4. Screening is done to check for the mutation of the α6 integrin in patients showing the absence of the α6 integrin. The missing integrin is detected to be replaced with a homozygous base-pair substitution for such patients. As a result, a serine residue is replaced with a leucine residue. The amino acid replacement, leucine, is contained within the first strand. The head of 6 has seven -propeller integrin blades (Has, Cristina, et al., 2018). The aberrant polypeptides are subjected to rapid proteolysis, including the lysosomal breakdown pathway.

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