Cell adhesion molecules in invertebrate immunity.
Cell adhesion is essential in immunity in invertebrates, e.g., in the cellular immune responses of encapsulation and nodule formation. Here cell adhesion molecules shown or suggested to be involved in invertebrate immunity are reviewed. Blood cells of the crayfish, Pacifastacus leniusculus, can release a cell-adhesive and opsonic peroxidase, peroxinectin. A site containing the motif, KGD, appears to be adhesive by binding to a transmembrane receptor of the integrin family on the blood cells. Peroxinectin also binds a peripheral blood cell surface CuZn-superoxide dismutase. The peroxidase-integrin interaction appears to have evolved early and seems conserved; human myeloperoxidase supports cell adhesion via the alphaMbeta2 integrin. There is evidence for peroxinectin-like proteins in other arthropods. Effects by RGD peptides indicate that integrins mediate blood cell adhesion and cellular immunity in diverse invertebrate species. Other invertebrate blood cell molecules proposed to be involved in adhesion include the insect plasmatocyte-spreading peptide, as well as soluble and transmembrane proteins which show some similarity to vertebrate adhesive or extracellular matrix molecules. Proteins such as the Ig family member hemolin, or proteins found in insects that are hosts for parasitic wasps, inhibit cell adhesion and may regulate or block cellular immunity.
Johansson
M W
MW
Department of Comparative Physiology, Evolutionary Biology Center, Uppsala University, Sweden. mats.johansson@fysbot.uu.se
D000818:Animals; D003400:Astacoidea / Q000276:immunology; D001773:Blood Cells / Q000378:metabolism; D001798:Blood Proteins / Q000502:physiology; D002448:Cell Adhesion / Q000187:drug effects / Q000276:immunology; D015815:Cell Adhesion Molecules / Q000276:immunology / Q000378:metabolism / Q000502:physiology; D033364:Decapoda / Q000276:immunology; D006801:Humans; D007111:Immunity, Cellular; D007448:Invertebrates / Q000276:immunology*; D016177:Macrophage-1 Antigen / Q000378:metabolism; D009195:Peroxidase / Q000502:physiology; D013482:Superoxide Dismutase / Q000502:physiology
D001798:Blood Proteins; D015815:Cell Adhesion Molecules; D016177:Macrophage-1 Antigen; C096867:peroxinectin protein, Pacifastacus leniusculus; D009195:Peroxidase; D013482:Superoxide Dismutase