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PMID: 3419519 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Structure and function of human perforin.

Nature ·Vol. 335 ·No. 6189 ·1988-09-29 ·Pages 448-51

Lichtenheld MG, Olsen KJ, Lu P, Lowrey DM, Hameed A, Hengartner H, Podack ER

Abstract

Perforin (P1) is a cytolytic protein with similarity to complement component C9. P1 has been described as a unique component of murine cytolytic T-cell and rat natural killer cell granules Previous studies indicated that human granules and P1 differed from murine granules and P1 in that they appeared to be cytolytically less active and lacked the haemolytic activity characteristic of P1. It has been suggested that P1, like C9, is under the control of the homologous restriction factor. Here we determine the primary structure of human P1, re-examine its functional properties, and address the question of homologous restriction.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Complement C9/genetics,physiology Cytoplasmic Granules/physiology Cytotoxicity, Immunologic DNA Humans Killer Cells, Natural/physiology Membrane Glycoproteins Membrane Proteins/genetics,physiology Mice Molecular Sequence Data Perforin Pore Forming Cytotoxic Proteins Rabbits Sequence Homology, Nucleic Acid
Chemicals
Complement C9 Membrane Glycoproteins Membrane Proteins Pore Forming Cytotoxic Proteins Perforin DNA
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Lichtenheld M G
Department of Microbiology and Immunology, University of Miami, School of Medicine, Florida 33101.
Olsen K J
Lu P
Lowrey D M
Hameed A
Hengartner H
Podack E R
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1988-09-29
Pages
448-51
Language
English
Region
England
NLM ID
0410462
Subset
IM
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