S. Fujiwara et al., Epiplakin, a novel member of the plakin family originally identified as a 450-kDa human epidermal autoantigen - Structure and tissue localization, J BIOL CHEM, 276(16), 2001, pp. 13340-13347
A 450-kDa human epidermal autoantigen was originally identified as a protei
n that reacted with the serum from an individual with a subepidermal bliste
ring disease. Molecular cloning of this protein has now shown that it conta
ins 5065 amino acids and has a molecular mass of 552 kDa. As reported previ
ously this protein, which we call epiplakin, belongs to the plakin family,
but it has some very unusual features. Epiplakin has 13 domains that are ho
mologous to the B domain in the COOH-terminal region of desmoplakin. The la
st five of these B domains, together with their associated linker regions,
are particularly strongly conserved. However, epiplakin lacks a coiled-coil
rod domain and an amino-terminal domain, both of which are found in all ot
her known members of the plakin family. Furthermore, no dimerization motif
was found in the sequence. Thus, it is likely that epiplakin exists in vivo
as a single-chain structure. Epitope mapping experiments showed that the o
riginal patient's serum recognized a sequence unique to epiplakin, which wa
s not found in plectin. Immunofluorescence staining revealed the presence o
f epiplakin in whole sheets: of epidermis and esophagus, in glandular cells
of eccrine sweat and parotid glands and in mucous epithelial cells in the
stomach and colon.