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Articles in PresS, published online ahead of print February 20, 2002
Am J Physiol Gastrointest Liver Physiol, 10.1152/ajpgi.00152.2001
Submitted on April 10, 2001
Accepted on January 10, 2002
1 Center for Cell and Molecular Signaling, Emory University, Atlanta, GA, USA
2 Department of Pathology, Emory University, Atlanta, GA, USA
3 Department of Pathology, University of California Irvine, Irvine, CA, USA
4 Department of Pediatrics, Harvard Medical School, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: gyue{at}emory.edu.
Cryptdins are antimicrobial peptides secreted by Paneth cells located at the base of intestinal crypts. In addition to their antimicrobial function, cryptdins may also regulate salt and water secretion by intestinal epithelial cells. Recent work with short circuit current measurements indicated that at least one cryptdin peptide, cryptdin 3, induces apical conductance(s) in Cl- secretory, including cystic fibrosis, epithelia. In the present study, we characterized the cryptdin 3-induced anion channel activity in human embryonic kidney (HEK) cells with single channel patch clamp techniques. The patch pipette was filled with solution containing different concentrations of cryptdin 3 and, after gigaseal formation, the channel activity was recorded with either cell-attached patch or inside-out patch modes. We found an anion selective channel with a conductance 15 pS and open probability of 0.19 regardless of cryptdin 3 concentration. The mean open time and mean closed time varied with the cryptdin 3 concentration. For cryptdin 3 concentrations of 10, 4, 1, and 0.5 mg/ml in the pipette, the corresponding mean open times (milliseconds) were 1.2, 7.0, 9.0, and 17.4, and the corresponding mean closed times (milliseconds) were 1.1, 1.6, 4.2 and 12.5. These results suggest that cryptdin 3 forms anion selective channels on the cytoplasmic membrane of HEK cells and that the kinetics of one such channel is affected by its interaction with other such channels.
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