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The Journal of Immunology, 1999, 162: 7217-7223.
Copyright © 1999 by The American Association of Immunologists

TNF-{alpha}-Mediated Apoptosis Is Initiated in Caveolae-Like Domains1

Young-Gyu Ko2, Jae-Seon Lee, Young-Sun Kang2, Jung-Hyuck Ahn and Jeong-Sun Seo3

Ilchun Molecular Medicine Institute Medical Research Center, Cancer Research Center, and Department of Biochemistry, Seoul National University College of Medicine, Seoul, Korea

Caveolae-like domains (CLDs) have been hypothesized to mediate apoptosis, since they contain sphingomyelin and initiate the conversion of sphingomyelin to ceramide. To address whether CLDs are directly involved in apoptosis, CLDs from U937 cells were isolated, taking advantage of their detergent insolubility and low density. The CLDs contained alkaline phosphatase as well as many signaling molecules, including Fyn, protein kinase C{alpha}, Raf-1, phospholipase C{gamma}1, and tyrosine phosphoproteins. Immunoblotting and immunofluorescent data showed that TNF receptor 1 colocalized with CD36 in CLDs, suggesting that TNF-{alpha}-initiated apoptosis occurs in CLDs. When cells were incubated with lipoprotein-deficient medium, the cholesterol concentration was greatly decreased in CLDs but not in other fractions, implying that the CLDs were selectively disrupted. In the CLD-disrupted cells, the surface expression of TNF receptor 1 and CD36 was significantly reduced. Analysis of cellular morphology, percent DNA fragmentation, DNA laddering, and caspase-3 activity showed that TNF-{alpha}-mediated apoptosis was blocked in CLD-disrupted cells, whereas anti-Fas-mediated apoptosis was not. Since Fas was not found in CLDs of Jurkat cells, apoptosis by Fas ligation might not require CLDs. Taken together, these data strongly imply that TNF-{alpha}-mediated apoptosis is initiated in CLDs.




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