title: Lectin-binding receptors, Na+,K(+)-ATPase, and acetylcholinesterase on immunocyte plasma membrane of Limulus polyphemus.
abstract: Plasma membrane receptors are crucial for nonself tissue recognition. Using concanavalin A (Con A), wheat germ agglutinin, peanut agglutinin, soybean agglutinin (SBA), and winged pea agglutinin, five lectin-binding receptor molecules have been recognized on the plasma membrane of the granulocyte (immunocyte) of the horseshoe crab, Limulus polyphemus. Only Con A and SBA caused capping of surface receptors. On the basis of the known functions of these lectin-binding receptor molecules in other invertebrates and vertebrates, their roles in phagocytosis, encapsulation, signaling, and possibly in complement pathway activation are postulated. In addition to lectin-binding receptors, Na+,K(+)-ATPase and acetylcholinesterase were detected on the plasma membrane. Because Limulus dates back to some 200 million years, the antiquity of these molecules is suggested. Furthermore, some of the lectin-binding surface receptors have the potential to be used as markers to separate different kinds of hemocytes in higher arthropods and to distinguish between normal and neoplastic cells in humans.
authors.affiliation: Department of Entomology, Cook College, Rutgers University, New Brunswick, New Jersey 08903.
authors.forename: A P
authors.initials: AP
authors.lastname: Gupta
authors.forename: S D
authors.initials: SD
authors.lastname: Orenberg
authors.forename: Y T
authors.initials: YT
authors.lastname: Das
authors.forename: S K
authors.initials: SK
authors.lastname: Chattopadhyay
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism* / Q000502:physiology; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism / Q000502:physiology / Q000648:ultrastructure; D003208:Concanavalin A / Q000378:metabolism / Q000494:pharmacology; D006098:Granulocytes / Q000378:metabolism / Q000502:physiology / Q000648:ultrastructure*; D006651:Histocytochemistry / Q000379:methods; D006737:Horseshoe Crabs / Q000378:metabolism* / Q000502:physiology; D037102:Lectins / Q000378:metabolism; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence / Q000379:methods; D019887:Peanut Agglutinin; D037121:Plant Lectins; D051381:Rats; D011940:Receptor Aggregation / Q000187:drug effects; D011975:Receptors, Mitogen / Q000378:metabolism* / Q000502:physiology; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism* / Q000502:physiology; D030262:Soybean Proteins; D014909:Wheat Germ Agglutinins; D010835:Phytohemagglutinins
chemical_list: D000110:Acetylcholinesterase; D003208:Concanavalin A; D037102:Lectins; D019887:Peanut Agglutinin; D037121:Plant Lectins; D011975:Receptors, Mitogen; D000254:Sodium-Potassium-Exchanging ATPase; D030262:Soybean Proteins; D014909:Wheat Germ Agglutinins; C028824:soybean lectin; D010835:Phytohemagglutinins