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Volume 272, Number 51, Issue of December 19, 1997 pp. 32006-32010

Cloning and Tyrosine Phosphorylation of a Novel Invertebrate Immunocyte Protein Containing Immunoreceptor Tyrosine-based Activation Motifs

(Received for publication, June 24, 1997, and in revised form, October 9, 1997)

Hiroki Takahashi , Go Ishikawa , Kazuko Ueki , Kaoru Azumi and Hideyoshi Yokosawa

From the Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060, Japan

Immunoreceptor tyrosine-based activation motif (ITAM) plays an important role in signal transduction through mammalian T-cell and B-cell antigen receptors and Fc receptors. The ITAM has been found only in vertebrate immunocytes. Ascidians are intriguing invertebrates from the viewpoint of the evolution of immune systems because they are considered to be ancestors of the vertebrates. We have previously shown that the monoclonal antibody A74 inhibits cellular defense reactions of the ascidian. In the present studies, we found that the A74 antigen protein has two ITAMs and several motifs that are proposed to function in signal transduction. The A74 protein is tyrosine-phosphorylated and associated with other proteins in the initial stages of cellular defense reactions. The ITAMs of the A74 protein are tyrosine-phosphorylated by a c-Src kinase in vitro. The A74 protein provides a key to the understanding of the origin of vertebrate immune systems.


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