The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Isolation and biochemical and functional characterization of perforin 1 from cytolytic T-cell granules.
Open accessAbstract
The Ca2+-dependent cytolytic activity of isolated T-lymphocyte granules was purified to apparent homogeneity by high-salt extraction, gel filtration, and ion-exchange chromatography. The lytic activity resided in a 72- to 75-kDa protein of cytolytic granules. Incubation of the isolated protein with erythrocytes in the presence of Ca2+ ions resulted in hemolysis and the formation of membrane lesions of 160 A in diameter, corresponding in size and morphology to membrane lesions formed on target cells by cloned, intact natural killer (NK) and cytolytic T lymphocytes. Hence, the 75-kDa granule protein is identified as monomeric perforin 1 (P1), postulated previously from the analysis of membrane lesions formed during NK and T-cell-mediated cytolysis. P1-mediated hemolysis is Ca2+-dependent and is inhibited by Zn2+ ions. Lysis is accompanied by the polymerization of P1 to membrane-associated tubular complexes (poly-P1) that form large transmembrane pores. P1 causes a rapid membrane depolarization of J774 cells in the presence of Ca2+. Purified P1 also induces transmembrane monovalent and divalent ion flow across lipid vesicles only in the presence of Ca2+. Whole-cell patch-clamp recordings of S49 lymphoma cells show a P1-dependent inward membrane current flow in the presence but not in the absence of Ca2+. The current increase can be dissected as a summation of discrete current events, indicative of formation of functional channels by polymerization of P1.
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Cites
Hamill, O. P., Marty, A., Neher, E., Sakmann, B., & Sigworth, F. J. (1981) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00656997 · Cited by 18,436
Cited by
Nagata, S., & Golstein, P. (1995) · Science · doi:10.1126/science.7533326 · Cited by 3,979
Perforin and granzymes: function, dysfunction and human pathology
Voskoboinik, I., Whisstock, J. C., & Trapani, J. A. (2015) · Nature Reviews Immunology · doi:10.1038/nri3839 · Cited by 1,327
Lymphocyte-Mediated Cytotoxicity
Russell, J. H., & Ley, T. J. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.100201.131730 · Cited by 1,122
Perforin-mediated target-cell death and immune homeostasis
Voskoboinik, I., Smyth, M. J., & Trapani, J. A. (2006) · Nature reviews. Immunology · doi:10.1038/nri1983 · Cited by 592
Structure and function of human perforin
Lichtenheld, M. G., Olsen, K. J., Lu, P., Lowrey, D. M., Hameed, A., Hengartner, H., & Podack, E. R. (1988) · Nature · doi:10.1038/335448a0 · Cited by 344
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Metadata
- Authors
- Podack, E. R., Young, J. D., & Cohn, Z. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-12
- Volume
- 82
- Issue
- 24
- Pages
- 8629-8633
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2170834275
- Cited by
- 398
- References
- 1
- FWCI
- 9.94
- Type
- journal article
- Language
- en
- Open access
- green
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- Podack, E. R., Young, J. D., & Cohn, Z. A. (1985). Isolation and biochemical and functional characterization of perforin 1 from cytolytic T-cell granules. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.24.8629
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