RESUMO
Prothymosin alpha (ProTalpha) is a highly conserved and widely distributed protein whose physiological functions remain elusive. In previous work we identified high and low affinity-binding sites for ProTalpha in lymphoid cells. Here we demonstrate, by affinity cross-linking and affinity chromatography, the existence of three binding partners (31, 29, and 19 kDa) for ProTalpha in the membrane of PHA-activated lymphoblasts. These surface molecules possess the expected affinity and specificity for a ProTalpha receptor. Examination of the expression of this complex of molecules by flow cytometry reveals that they bind ProTalpha in a specific and saturable way. In addition, the distribution of the receptor on the cell surface was studied by fluorescence microscopy; a cap-like structure at one of the poles of the cells was identified. These results represent a new and promising approach in the research on ProTalpha, opening the way toward the understanding of the molecular mechanism of action of this protein.
