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J. Biol. Chem., Vol. 266, Issue 27, 17784-17790, Sep, 1991
D Sawamura, K Li, ML Chu and J Uitto
Bullous pemphigoid antigens are defined as the autoantigens in a blistering
skin disease, bullous pemphigoid. One of them, a 230-kDa protein (BPAG1),
is associated with hemidesmosomes, attachment complexes at the basal
keratinocyte-lamina lucida interface within the dermal-epidermal basement
membrane zone. The precise functions and cellular compartmentalization of
BPAG1 are unknown. In this study, a human keratinocyte lambda gt11 cDNA
library was screened for clones corresponding to BPAG1. The composite of
overlapping cDNAs delineated 8,930 base pairs of nucleotide sequences that
contained an open reading frame encoding 2,649 amino acids. Analysis of the
deduced amino acid sequences predicted a putative signal peptide of 43
amino acids and the presence of a membrane-associated sequence of 17 amino
acids. Several potential sites for N-glycosylation, as well as for protein
kinase C or cAMP- and cGMP-dependent protein kinase-mediated
phosphorylation were identified. Three peptide segments were predicted to
be highly antigenic, potentially serving as epitopes for the formation of
autoantibodies. Eight repeat segments of 38 residues each with a high
degree of homology with sequences in desmoplakin I, a component of
desmosomal cytoplasmic plaques, were detected in the carboxyl-terminal end
of the molecule. In addition, the presence of three subdomains
characterized by heptad repeats predicted an alpha-helical coiled coil
dimer structure in the central portion of the protein. These data suggest
that BPAG1 may be a membrane-associated protein that plays a role in the
attachment of basal keratinocytes to the underlying basement membrane.
Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains
Department of Dermatology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
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