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Journal of Histochemistry and Cytochemistry, Vol. 48, 345-354, March 2000, Copyright © 2000, The Histochemical Society, Inc.

ARTICLE

cAMP-dependent Cl- Channel Protein (CFTR) and Its mRNA Are Expressed in the Secretory Portion of Human Eccrine Sweat Gland

Fusako Satob and Kenzo Satoa
a Human Gene Therapy Research Institute, Iowa Health System, Des Moines, Iowa
b Department of Dermatology, University of Iowa College of Medicine, Iowa City, Iowa

Correspondence to: Kenzo Sato, Human Gene Therapy Research Inst., 1415 Woodland Ave., Des Moines, IA 50339-3203.

Immunoreactive cystic fibrosis transport regulator (CFTR) proteins in human sweat ducts has been documented but CFTR expression in the secretory coil has remained uncertain. Using monoclonal antibodies (MAbs) against epitopes in the R-domain and C-terminus, we observed the following: Formalin fixation masks the CFTR epitopes but the epitopes are exposed by treatment with urea and heat (antigen retrieval). Pen-Fix fixation preserves CFTR epitopes. The secretory coil also expresses CFTR epitopes for the R-domain and C-terminus. An MAb against C-terminus amino acids 1466–1480 coupled to keyhole limpet hemocyanin (MAb WC) stained dark cells predominantly. Staining by MAbs against the C-terminus was completely blocked by a C-terminus peptide. mRNA for CFTR was amplified by RT-PCR in both the duct and the secretory coil. In situ hybridization for CFTR mRNA after 3SR amplification indicates that mRNA is localized in the dark cells and perhaps also in the clear cell cytoplasm near the secretory coil. mRNA is present in both the luminal and basal duct cells. We conclude that CFTR is expressed equally well in both the duct and the secretory coil, suggesting that cAMP-dependent Cl- channels are involved in regulation of sweat secretion and duct absorption. (J Histochem Cytochem 48:345–353, 2000)

Key Words: sweat gland, cystic fibrosis, CFTR, immunohistochemistry, in situ hybridization


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