Year: 1994
Type: article
Abstract: W e report here the isolation and characterization of a cDNA that encodes a novel extracellular epidermal molecule, epidermal surface antigen (ESA), which is thought to play a role in intercellular epidermal adhesion.Sequence analysis reveals that the 379 amino acid ESAhas a molecular mass of about 41.7 kDa and an a-helix-rich secondary conformation.Much of this also has an heptad substructure, consistent with the formation of several bundles of a-helices in a compact globular structure.The ESA protein appears to consist of an N H 2terminal hydrophobic region with mixed a and p structure followed by a more hydrophilic COOH-terminal region which is very rich in a-helix.The 2.5-kilobase ESA mRNA is expressed in cultured keratinocytes, melanocytes, fibroblasts, carcinoma, and melanoma cell lines.The ESA gene is conserved in all mammalian species examined and has been localized to human chromosome 17 (M17S1) in the same region as the gene for von Recklinghausen neurofibromatosis.The high level of expression of the ESA mRNA in human skin and in cultured cells derived from the epidermis, the appearance of ESA protein early in human development, and conservation of the ESA gene throughout mammalian evolution suggest that the novel ESA protein plays a vital role in epidermal structure and maintenance.Monospecific antibodies and cDNA probes are powerful tools for the isolation and characterization of proteins whose functions are unknown.It has been recognized for some time that epidermal surface proteins are important for normal epidermal maintenance and function, based on their involvement in several autoimmune bullous diseases in which autoantibodies bind to normal epidermal cell surface molecules and cause cell disadherence and ultimately blister formation (1).Recently, circulating antibodies from such patients have been used to isolate and characterize epidermal proteins involved in cell Grants AR-40970, AR-30965, AR-36546, and AR-40520.This work was
Source: Journal of Biological Chemistry
Authors: W.T. Schroeder, S. Stewart-Galetka, S. Mandavilli, D.A. Parry, L. Goldsmith, M. Duvic
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1575829284