Campus Units

Zoology

Document Type

Article

Publication Version

Published Version

Publication Date

6-1995

Journal or Book Title

The Journal of Cell Biology

Volume

129

Issue

5

First Page

1355

Last Page

1362

DOI

10.1083/jcb.129.5.1355

Abstract

The mAb lan3-6 recognizes a cytosolic antigen which is selectively expressed in the growth cones and axons of a small subset of peripheral sensory neurons fasciculating in a single tract common to all hirudinid leeches. We have used this antibody to clone a novel EF-hand calcium-binding protein, calsensin, by screening an expression vector library. A full-length clone of 1.1 kb identified by the antibody was isolated and sequenced. In situ hybridizations with calsensin probes and antibody staining using new polyclonal antisera generated against calsensin sequence demonstrate that calsensin indeed corresponds to the lan3-6 antigen. Calsensin consists of 83 residues with a calculated molecular mass of 9.1 kD that contains two helix-loop-helix domains. The calcium-binding domains are likely to be functional in vivo since a fusion protein derived from the calsensin clone binds 45Ca2+ in vitro. Immunoaffinity purification experiments with the lan3-6 antibody shows that a large 200,000 M(r) protein selectively copurifies with calsensin in two different leech species. These results suggest that calsensin may be functioning as a trigger protein which interacts with the larger protein. These data are consistent with the hypothesis that calsensin may mediate calcium-dependent signal transduction events in the growth cones and axons of this small group of sensory neurons which fasciculate in a single axon tract.

Comments

This article is published as Briggs, Kristen Kay, Andrea J. Silvers, Kristen M. Johansen, and Jørgen Johansen. "Calsensin: a novel calcium-binding protein expressed in a subset of peripheral leech neurons fasciculating in a single axon tract." The Journal of cell biology 129, no. 5 (1995): 1355-1362. doi: 10.1083/jcb.129.5.1355. Posted with permission.

Copyright Owner

The Rockefeller University Press

Language

en

File Format

application/pdf

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