= D. T. Fearon
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D. T. Fearon authored a 1980 study identifying a membrane <glycoprotein> as the receptor for the <complement> fragment <C3b> on human <red blood cells>, <B cells>, <monocytes> and polymorphonuclear <leukocytes>. The molecule, called gp205 in the paper, is associated with the receptor now called <complement receptor 1>. The work connected a purified <protein>'s biochemical activity with a receptor found on several classes of blood <cells>.<Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte by D. T. Fearon>[Abstract, Journal of Experimental Medicine 152 (1980), pp. 20–30; DOI 10.1084/jem.152.1.20.]{ref}
The route to identification is instructive. The <glycoprotein> was investigated for its ability to inhibit a <C3 convertase> and to assist enzymatic inactivation of <C3b>. Those activities suggested a <C3b>-binding function, which the receptor experiments tested. Thus a <cell membrane> receptor need not merely initiate a response: recognition of a <complement> component can also help regulate the amplification system to which that component belongs.<Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte by D. T. Fearon>[Abstract: convertase destabilization, C3b-inactivator cofactor activity and receptor identification.]{ref}
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