Structure and function of human perforin.
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.
Department of Microbiology and Immunology, University of Miami, School of Medicine, Florida 33101.
M G
MG
Lichtenheld
K J
KJ
Olsen
P
P
Lu
D M
DM
Lowrey
A
A
Hameed
H
H
Hengartner
E R
ER
Podack
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003186:Complement C9 / Q000235:genetics / Q000502:physiology; D003594:Cytoplasmic Granules / Q000502:physiology; D003602:Cytotoxicity, Immunologic; D004247:DNA; D006801:Humans; D007694:Killer Cells, Natural / Q000502:physiology; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000235:genetics* / Q000502:physiology; D051379:Mice; D008969:Molecular Sequence Data; D054353:Perforin; D052899:Pore Forming Cytotoxic Proteins; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid
D003186:Complement C9; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D052899:Pore Forming Cytotoxic Proteins; D054353:Perforin; D004247:DNA