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© The Rockefeller University Press, 0021-9525/1998//685 $5.00
The Journal of Cell Biology, Volume 140, Number 3, , 1998 685-698

Article

Thy-1 Is a Component Common to Multiple Populations of Synaptic Vesicles



Chung-Jiuan Jeng*, Steven A. McCarroll{ddagger}, Thomas F. J. Martin§, Erik Floor||, James Adams*, David Krantz{ddagger}, Stefan Butz, Robert Edwards{ddagger}, and Erik S. Schweitzer*

* Department of Neurobiology and Brain Research Institute, UCLA School of Medicine, Los Angeles, California 90095-1763; {ddagger} Departments of Neurology and Physiology, and Graduate Program in Neuroscience and Cell Biology, UCSF School of Medicine, San Francisco, California 94143-0435; § Department of Biochemistry, University of Wisconsin Madison, Madison, Wisconsin 53706-1569; || Department of Biochemistry, Cell & Molecular Biology, University of Kansas, Lawrence, Kansas 66045-2106; and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235

Thy-1, a glycosylphosphatidylinositol-linked integral membrane protein of the immunoglobulin superfamily, is a component of both large dense-core and small clear vesicles in PC12 cells. A majority of this protein, formerly recognized only on the plasma membrane of neurons, is localized to regulated secretory vesicles. Thy-1 is also present in synaptic vesicles in rat central nervous system. Experiments on permeabilized PC12 cells demonstrate that antibodies against Thy-1 inhibit the regulated release of neurotransmitter; this inhibition appears to be independent of any effect on the Ca2+ channel. These findings suggest Thy-1 is an integral component of many types of regulated secretory vesicles, and plays an important role in the regulated vesicular release of neurotransmitter at the synapse.

Abbreviations used in this paper: ECL, enhanced chemiluminescence; GPI, glycosylphosphatidylinositol; HBS, Hepes-buffered saline; LDCV, large dense-core vesicle; NE, norepinephrine; NMS, normal mouse serum; NSF, N-ethylmaleimide sensitive factor; SAC, staphylococcus aureus; SNAP, soluble NSF attachment protein; SNARE, SNAP receptor; SSV, small synaptic vesicle.

Address all correspondence to Erik Schweitzer, Department of Neurobiology, UCLA School of Medicine, 10833 LeConte Avenue, Los Angeles, CA 90095-1763. Tel.: (310) 206-4084. Fax: (310) 206-4066. E-mail: schweitzer{at}neurobio.medsch.ucla.edu


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