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Comparison of Proteins Expressed on Secretory Vesicle Membranes and Plasma Membranes of Human Neutrophils¹

Silvia M. Uriarte^*, David W. Powell^*,, Gregory C. Luerman, Michael L. Merchant^*, Timothy D. Cummins^*, Neelakshi R. Jog, Richard A. Ward^* and Kenneth R. McLeish^2,*,,

^* Department of Medicine, Department of Biochemistry and Molecular Biology, and Department of Microbiology and Immunology, University of Louisville, Louisville, KY 40202; and Veterans Affairs Medical Center, Louisville, KY 40206

Secretory vesicles are neutrophil intracellular storage granules formed by endocytosis. Understanding the functional consequences of secretory vesicle exocytosis requires knowledge of their membrane proteins. The current study was designed to use proteomic technologies to develop a more complete catalog of secretory vesicle membrane proteins and to compare the proteomes of secretory vesicle and plasma membranes. A total of 1118 proteins were identified, 573 (51%) were present only in plasma membrane-enriched fractions, 418 (37%) only in secretory vesicle-enriched membrane fractions, and 127 (11%) in both fractions. Gene Ontology categorized 373 of these proteins as integral membrane proteins. Proteins typically associated with other intracellular organelles, including nuclei, mitochondria, and ribosomes, were identified in both membrane fractions. Ingenuity Pathway Knowledge Base analysis determined that the majority of canonical and functional pathways were significantly associated with proteins from both plasma membrane-enriched and secretory vesicle-enriched fractions. There were, however, some canonical signaling pathways that involved proteins only from plasma membranes or secretory vesicles. In conclusion, a number of proteins were identified that may elucidate mechanisms and functional consequences of secretory vesicle exocytosis. The small number of common proteins suggests that the hypothesis that secretory vesicles are formed from plasma membranes by endocytosis requires more critical evaluation.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ This work was supported by a Merit Review Grant from the Department of Veterans Affairs (to K.R.M.), National Institutes of Health Grants DK62389 (to R.A.W. and K.R.M.) and DK176743 (to D.W.P.), and the Office of Science Financial Assistance Program, Department of Energy (to D.W.P.).

² Address correspondence and reprint requests to Dr. Kenneth R. McLeish, Baxter I Research Building, University of Louisville, 570 South Preston Street, Louisville, KY 40202. E-mail address: k.mcleish{at}louisville.edu

³ Abbreviations used in this paper: MS, mass spectrometry; SCX, strong cation exchange; RP, reversed-phase; PAF, protein abundance factor; NCBI, National Center for Biotechnology Information; IPKB, Ingenuity Pathways Knowledge Base; SNARE, soluble NSF attachment receptor.

⁴ The online version of this article contains supplemental material.