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Science 11 July 1986:
Vol. 233. no. 4760, pp. 184 - 190
DOI: 10.1126/science.2425429

Articles

Science, Vol 233, Issue 4760, 184-190
Copyright © 1986 by American Association for the Advancement of Science


articles

The ninth component of complement and the pore-forming protein (perforin 1) from cytotoxic T cells: structural, immunological, and functional similarities

JD Young, ZA Cohn, and ER Podack

The ninth component of complement (C9) and the pore-forming protein (PFP or perforin) from cytotoxic T lymphocytes polymerize to tubular lesions having an internal diameter of 100 A and 160 A, respectively, when bound to lipid bilayers. Polymerized C9, assembled by slow spontaneous or rapid Zn2+-induced polymerization, and polyperforin, which is assembled only in the presence of Ca2+, constitute large aqueous pores that are stable, nonselective for solutes, and insensitive to changes of membrane potential. Monospecific polyclonal antibodies to purified C9 and PFP show cross-reactivity, suggesting structural homology between the two molecules. The structural and functional homologies between these two killer molecules imply an active role for pore formation during cell lysis.


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The Functional Basis for Hemophagocytic Lymphohistiocytosis in a Patient with Co-inherited Missense Mutations in the Perforin (PFN1) Gene.
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Unlocking the secrets of cytotoxic granule proteins.
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Superantigen-Driven, CD8+ T Cell-Mediated Down-Regulation: CD95 (Fas)-Dependent Down-Regulation of Human Ig Responses Despite CD95-Independent Killing of Activated B Cells.
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Cancer Vaccines: The Molecular Basis for T Cell Killing of Tumor Cells.
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Granzyme B (GraB) Autonomously Crosses the Cell Membrane and Perforin Initiates Apoptosis and GraB Nuclear Localization.
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P-glycoprotein Does Not Protect Cells against Cytolysis Induced by Pore-forming Proteins.
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J. Biol. Chem. 276, 16667-16673
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Science. ISSN 0036-8075 (print), 1095-9203 (online)