Mapping a region associated with Na channel inactivation using antibodies to a synthetic peptide corresponding to a part of the channel.

H. Meiri, G. Spira, M. Sammar, M. Namir, A. Schwartz, A. Komoriya, E. M. Kosower, Y. Palti

Research output: Contribution to journalArticlepeer-review

Abstract

Antibodies to the synthetic peptide (carrier-coupled) corresponding to amino acids 210-223 of the primary sequence of eel Na channel (C1+ peptide) were generated. The antipeptide antibodies were used to identify functional roles as well as the accessibility from the external membrane surface of the C1+ domains. Rabbit antipeptide antibodies bound specifically to the C1+ synthetic peptide and to an eel membrane fraction bearing a high density of Na channels. When applied to the external surface of cultured dorsal root ganglion cells obtained from newborn rats, the antibodies modify Na channel inactivation by shifting the steady-state Na current-inactivation parameter, h infinity, curve to more negative potentials in fast and slow Na currents. The rate of inactivation of the slow channel is shown to be increased. The antibodies do not have a significant effect on activation of the channels. Part of the amino acid sequence corresponding to C1+ peptide is therefore accessible, in the mammalian Na channel, from the external membrane surface and is associated with the inactivation gate.

Original languageEnglish
Pages (from-to)5058-5062
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number14
DOIs
StatePublished - Jul 1987

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