Pitsillides A A, Taylor P M, Bitensky L, Chayen J, Muir I H, Askonas B A
Division of Cellular Biology, Kennedy Institute of Rheumatology, London, GB.
Eur J Immunol. 1988 Aug;18(8):1203-8. doi: 10.1002/eji.1830180809.
Although many studies have attempted to elucidate how cytotoxic T (Tc) lymphocytes cause the death of target cells, the mechanism is still controversial. In the present study the effect on the integrity of the lysosomes of the target cell has been investigated. We show here that the specific recognition and attachment of cloned type A influenza-specific Tc cells to A/X31 influenza virus-infected target cells caused rapid change in the amount of lysosomal naphthylamidase activity that was bound within the lysosomes, indicating that the lysosomal membranes in the target cells had been totally labilized. Target cells infected with type B influenza virus served as controls. We therefore suggest that the viral specificity of Tc lymphocytes allows for recognition and intimate membrane contact with suitably infected targets. This intimate contact induces sufficient perturbation of the target cell plasma membrane so as to cause total labilization of the target cell lysosomes which could account for intracellular lysis.
尽管许多研究试图阐明细胞毒性T（Tc）淋巴细胞如何导致靶细胞死亡，但其机制仍存在争议。在本研究中，我们研究了对靶细胞溶酶体完整性的影响。我们在此表明，克隆的甲型流感特异性Tc细胞与A/X31流感病毒感染的靶细胞的特异性识别和附着导致溶酶体内结合的溶酶体萘基酰胺酶活性量迅速变化，这表明靶细胞中的溶酶体膜已完全不稳定。感染乙型流感病毒的靶细胞用作对照。因此，我们认为Tc淋巴细胞的病毒特异性允许其识别并与适当感染的靶细胞进行紧密的膜接触。这种紧密接触会引起靶细胞质膜的充分扰动，从而导致靶细胞溶酶体完全不稳定，这可能是细胞内裂解的原因。
