Processing, Subcellular Localization, and Function of 519 (Granulysin), a Human Late T Cell Activation Molecule with Homology to Small, Lytic, Granule Proteins

Susan V. Peña, Dennis A. Hanson, Brian A. Carr, Thomas J. Goralski, Alan M. Krensky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

223 Scopus citations

Abstract

CTL and NK cells share a common cytolytic mechanism that involves regulated exocytosis of lytic molecules stored within cytoplasmic granules. Here we describe the processing, subcellular localization, and function of a T and NK cell-specific granule protein that shares homology with small, lytic granule-associated molecules. The gene coding for this protein, 519, is expressed late after T cell activation. Antisera raised against a 519/glutathione-S-transferase fusion protein and a series of peptides derived from the 519 protein sequence permitted the identification of two small CTL protein products of 15 and 9 kDa that are exocytosed after stimulation through the TCR. The 9-kDa product is a processed form of 519 and differs from the 15-kDa product in both its amino and carboxyl terminus. While both 519 proteins are found in cytoplasmic granules, the 9-kDa form is also present in dense, highly cytolytic granules. Functional studies indicate that this protein is lytic against tumor cell targets. The cell type- and stage-specific expression pattern of 519 along with its subcellular localization are reminiscent of molecules that play a vital role in granule-mediated cytolysis by CTL and NK cells. Its lytic activity suggests the involvement of 519 in CTL effector function.

Original languageEnglish (US)
Pages (from-to)2680-2688
Number of pages9
JournalJournal of Immunology
Volume158
Issue number6
StatePublished - Mar 15 1997

ASJC Scopus subject areas

  • Immunology

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