Identification of Receptors for Prothymosin α on Human Lymphocytes
-
A. Piñeiro
Abstract
Prothymosin α (ProTα ) is a highly conserved and widely distributed protein whose physiological functions remain elusive. In previous work we identified high and low affinitybinding sites for ProTα in lymphoid cells. Here we demonstrate, by affinity crosslinking and affinity chromatography, the existence of three binding partners (31, 29, and 19kDa) for ProTα in the membrane of PHAactivated lymphoblasts. These surface molecules possess the expected affinity and specificity for a ProTα receptor. Examination of the expression of this complex of molecules by flow cytometry reveals that they bind ProTα 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 ProTα, opening the way toward the understanding of the molecular mechanism of action of this protein.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Protein-DNA Interaction and CpG Methylation at rep*/vIL-10p of Latent Epstein-Barr Virus Genomes in Lymphoid Cell Lines
- In Vitro and in Vivo Processing of Cyanelle tmRNA by RNase P
- A Eubacterial Origin for the Human tRNA Nucleotidyltransferase?
- Interaction of Thymidylate Synthase with the 5-Thiophosphates, 5-Dithiophosphates, 5-H-Phosphonates and 5-S-Thiosulfates of 2-Deoxyuridine, Thymidine and 5-Fluoro-2-Deoxyuridine
- The MKK6/p38 Mitogen-Activated Protein Kinase Pathway Is Capable of Inducing SOCS3 Gene Expression and Inhibits IL-6-Induced Transcription
- Identification of a Gephyrin-Binding Motif in the GDP/GTP Exchange Factor Collybistin
- Major Vault Protein Is a Substrate of Endogenous Protein Kinases in CHO and PC12 Cells
- Identification of Receptors for Prothymosin α on Human Lymphocytes
- Tissue Kallikrein KLK1 Is Expressed de Novo in Endothelial Cells and Mediates Relaxation of Human Umbilical Veins
- Secretion of Gelatinases and Activation of Gelatinase A (MMP-2) by Human Rheumatoid Synovial Fibroblasts
- Ferredoxins from the Archaeon Acidianus ambivalens: Overexpression and Characterization of the Non-Zinc-Containing Ferredoxin FdB
- Isolation and Characterization of a Trypsin-Like Protease from Trichoderma viride
- The N-Terminal Part of Recombinant Human Tear Lipocalin/von Ebners Gland Protein Confers Cysteine Proteinase Inhibition Depending on the Presence of the Entire Cystatin-Like Sequence Motifs
Articles in the same Issue
- Protein-DNA Interaction and CpG Methylation at rep*/vIL-10p of Latent Epstein-Barr Virus Genomes in Lymphoid Cell Lines
- In Vitro and in Vivo Processing of Cyanelle tmRNA by RNase P
- A Eubacterial Origin for the Human tRNA Nucleotidyltransferase?
- Interaction of Thymidylate Synthase with the 5-Thiophosphates, 5-Dithiophosphates, 5-H-Phosphonates and 5-S-Thiosulfates of 2-Deoxyuridine, Thymidine and 5-Fluoro-2-Deoxyuridine
- The MKK6/p38 Mitogen-Activated Protein Kinase Pathway Is Capable of Inducing SOCS3 Gene Expression and Inhibits IL-6-Induced Transcription
- Identification of a Gephyrin-Binding Motif in the GDP/GTP Exchange Factor Collybistin
- Major Vault Protein Is a Substrate of Endogenous Protein Kinases in CHO and PC12 Cells
- Identification of Receptors for Prothymosin α on Human Lymphocytes
- Tissue Kallikrein KLK1 Is Expressed de Novo in Endothelial Cells and Mediates Relaxation of Human Umbilical Veins
- Secretion of Gelatinases and Activation of Gelatinase A (MMP-2) by Human Rheumatoid Synovial Fibroblasts
- Ferredoxins from the Archaeon Acidianus ambivalens: Overexpression and Characterization of the Non-Zinc-Containing Ferredoxin FdB
- Isolation and Characterization of a Trypsin-Like Protease from Trichoderma viride
- The N-Terminal Part of Recombinant Human Tear Lipocalin/von Ebners Gland Protein Confers Cysteine Proteinase Inhibition Depending on the Presence of the Entire Cystatin-Like Sequence Motifs
