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Structure and function of human perforin

Nature volume 335, pages 448–451 (1988)Cite this article

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 granules1,2. Previous studies3,4 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 factor5. Here we determine the primary structure of human P1, re-examine its functional properties, and address the question of homologous restriction.

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Authors and Affiliations

  1. Department of Microbiology and Immunology, University of Miami, School of Medicine, Miami, Florida, 33101, USA

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

  2. Department of Experimental Pathology, University of Zürich, Zürich, Switzerland

    Hans Hengartner

Authors
  1. Mathias G. Lichtenheld
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  2. Kristin J. Olsen
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  3. Ping Lu
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  4. David M. Lowrey
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  5. Arif Hameed
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  6. Hans Hengartner
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  7. Eckhard R. Podack
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Lichtenheld, M., Olsen, K., Lu, P. et al. Structure and function of human perforin. Nature 335, 448–451 (1988). https://doi.org/10.1038/335448a0

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