Evidence of redox-linked signaling for producing a giant signal complex

Journal of Cellular Biochemistry
Y KatanoI Nakashima

Abstract

Previously we showed that a thiol-reactive heavy metal, HgCl2, crosslinked multiple cell surface receptors through a ligand-independent pathway, which produced massive aggregates of phosphotyrosine (PTYR)-containing proteins beneath plasma membrane [Nakashima et al. (1994): J Immunol 152: 1064-1071]. In this study we characterized these unique aggregates at the molecular level. The lysates in Brij 96 of thymocytes treated with HgCl2 were separated into the supernatant and pellet fractions by simple centrifugation. Selected PTYR-containing proteins and p56lck appeared in the pellet fraction as quickly as 5 s after exposure to HgCl2, and were further increased in amount by 5 min. Although the mechanism of triggering these events was redox-linked, the majority of proteins in the Brij 96-insoluble aggregates were dissociated in SDS-PAGE under nonreducing condition. This suggested that PTYR-containing proteins and p56lck themselves do not form dimer or polymer directly by thiol-mediated bond. The pellet fraction was further found to include some other signal delivery elements, such as GTPase activating protein, phosphatidylinositol 3 kinase, and mitogen-activated protein kinase. Finally, all of these signal elements and selected PTY...Continue Reading

References

Apr 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·A D BeyersA F Williams
Oct 30, 1992·Cell·T Pawson, G D Gish
Jan 1, 1993·Annual Review of Immunology·R M PerlmutterJ Alberola-Ila

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Citations

Sep 7, 2002·Antioxidants & Redox Signaling·Anwarul A AkhandIzumi Nakashima
Sep 7, 2002·Antioxidants & Redox Signaling·Izumi NakashimaYoshiyuki Kawamoto
Apr 4, 2006·Aquatic Toxicology·Bruno BurlandoAldo Viarengo
Jun 16, 2005·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Barbara MarchiGabriella Gallo

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