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A. Piñeiro, M. Begoña Bugía, M. Pilar Arias, O.J. Cordero, M. Nogueira

Identification of Receptors for Prothymosin ? on Human Lymphocytes

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

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 382, 10/2001
Pages: 1473 - 1482

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