On the cytoplasmic side of the plasma membrane of erythrocytes there i
s a dense protein filament matrix that maintains the shape of the cell
s. The-main constituents of this system, actin and spectrin, which hav
e also been detected in keratinocytes and fibroblasts, are known to be
linked in erythrocytes in a network structure by additional proteins
such as band 4.1 and adducin. The interaction between actin and spectr
in, mediated by adducin, is regulated by calmodulin and protein kinase
C. Because we have previously found adducin in cultured keratinocytes
, we investigated epidermis by immunochemical techniques. We found add
ucin to be localized at cell-cell contact sites in epidermis using aff
inity-purified antibodies against human erythrocyte adducin. Immunoflu
orescence of epidermis revealed an intense fluorescence in the basal l
ayer, whereas stratum spinosum and stratum granulosum showed moderate
staining. There was intense staining at sites of cell-cell contact in
cultured human keratinocytes. Immunoblot analysis indicated the presen
ce of adducin polypeptides of 103 kd and 97 kd in epidermis, but in cu
ltured keratinocytes only the higher molecular weight form could be de
tected. This study indicates adducin, a regulatory protein in erythroc
ytes, is also present in epidermis. Its localization suggests that it
may be involved in the formation of the microfilament matrix of the me
mbrane skeleton at cell-cell contact sites.