Structure and function of human perforin

Mathias G. Lichtenheld, Kristin J. Olsen, Ping Lu, David M. Lowrey, Arif Hameed, Hans Hengartner, Eckhard R. Podack

Research output: Contribution to journalArticlepeer-review

271 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)448-451
Number of pages4
JournalNature
Volume335
Issue number6189
DOIs
StatePublished - Jan 1 1988

ASJC Scopus subject areas

  • General

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