. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 228 REPORTS FROM THE MBL GENERAL SCIENTIFIC MEETINGS as the lectin limulin is an important advance in our understand- ing of the mechanisms of immunity in this animal. The recog- nition of foreign cells for subsequent cytolytic destruction prob- ably depends on the presentation of sugars recognized by limulin on the surfaces of the foreign cells. Although several plasma lectins have been identified in a variety of animals, the functions of this class of proteins have been poorly characterized. To our knowledge, this is the f
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 228 REPORTS FROM THE MBL GENERAL SCIENTIFIC MEETINGS as the lectin limulin is an important advance in our understand- ing of the mechanisms of immunity in this animal. The recog- nition of foreign cells for subsequent cytolytic destruction prob- ably depends on the presentation of sugars recognized by limulin on the surfaces of the foreign cells. Although several plasma lectins have been identified in a variety of animals, the functions of this class of proteins have been poorly characterized. To our knowledge, this is the first demonstration of a cytolytic function for a plasma lectin. The ability of LAM to regulate the activity of limulin is as yet not well characterized, but it may be important in the integration of the different components of the immune defense system of Limulus. Supported by Grant No. MCB-9218460 from the National Science Foundation. Literature Cited 1 Canicatti, C. 1990. Expvrientia 46: 239-243. 2 Armstrong, P. B., , and J. P. Quigley. 1993. Moi Immunol. 30: 929-934. 3. Mandal, C., and C. Mandal. 1990. Expenenlia 46: 433-441. 4. Kehoe, J. M., and R. K. Scide. 1986. Pp. 345-358 in Hemocytic and Humoral Immunity in Arthropods. A. P. Gupta, ed. John Wiley & Sons. New York. 5 Quigley, J. P., S. Misquith, A. Surolia, S. Srimal, and P. B. Arm- strong. 1994. Biol. Bull 187: 229-230. Reference: Biol. Bull. 187: 228-229. (October, 1994) Clearance of Proteases from the Circulation of the American Horseshoe Crab, Limulus polyphemus: A Possible Function for a2-Macroglobulin Ralph Melchior (Department of Molecular and Cellular Biology, University of California. Davis, CA 95616-8755), James P. Quigley. and Peter B. Armstrong The protease inhibitor «2-macroglobulin (a2M), which is found at high concentration in the plasma of vertebrates, ar- thropods, and molluscs (1), binds proteases by a unique process that begins with the proteolytic cleavage of a2M and is completed wh
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