On the Interaction of Bovine Pancreatic Trypsin Inhibitor with Maxi Ca2+-activated K + Channels A Model System for Analysis of Peptide-induced Subconductance States
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Address reprint requests to Dr. Edward Moczydlowski, Department of Pharmacology, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06510. J. GEN. PHYSIOL. © The Rockefeller University Press • 0022-1295/91/06/1295/25 $2.00 Volume 97 June 1991 1295-1319 1295 on Jne 0, 2017 D ow nladed fom Published June 1, 1991
منابع مشابه
On the interaction of bovine pancreatic trypsin inhibitor with maxi Ca(2+)-activated K+ channels. A model system for analysis of peptide- induced subconductance states
Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue basic peptide that is a representative member of a widely distributed class of serine protease inhibitors known as Kunitz inhibitors. BPTI is also homologous to dendrotoxin peptides from mamba snake venom that have been characterized as inhibitors of various types of voltage-dependent K+ channels. In this study we compared the effect of...
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In this study, we investigated the mechanism underlying the production of inwardly rectifying subconductance states induced in large conductance Ca(2+)-activated K+ channels (maxi K(Ca) channels) by the small, homologous proteins, bovine pancreatic trypsin inhibitor (BPTI) and dendrotoxin-I (DTX). Low-resolution bilayer recordings of BPTI-induced substates display excess noise that is well desc...
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The homologous Kunitz inhibitor proteins, bovine pancreatic trypsin inhibitor (BPTI) and dendrotoxin I (DTX-I), interact with large conductance Ca 2 1 -activated K 1 channels (maxi-K Ca ) by binding to an intracellular site outside of the pore to produce discrete substate events. In contrast, certain homologues of the Shaker ball peptide produce discrete blocking events by binding within the io...
متن کاملSimultaneous Binding of Basic Peptides at Intracellular Sites on a Large Conductance Ca2+-activated K+ Channel
The homologous Kunitz inhibitor proteins, bovine pancreatic trypsin inhibitor (BPTI) and dendrotoxin I (DTX-I), interact with large conductance Ca2+-activated K+ channels (maxi-KCa) by binding to an intracellular site outside of the pore to produce discrete substate events. In contrast, certain homologues of the Shaker ball peptide produce discrete blocking events by binding within the ion cond...
متن کاملTrypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2.
Proteinase-activated receptor-2 (PAR-2) is a G protein-coupled receptor that is cleaved by trypsin within the NH2-terminus, exposing a tethered ligand that binds and activates the receptor. We examined the secretory effects of trypsin, mediated through PAR-2, on well-differentiated nontransformed dog pancreatic duct epithelial cells (PDEC). Trypsin and activating peptide (AP or SLIGRL-NH2, corr...
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تاریخ انتشار 2003