In vitro effect of thymosin alpha 1 on the expression of peanut agglutinin binding by murine thymocytes.
Thymosin alpha 1 induces the loss of PNA binding ability by subpopulation of thymic cells. This loss is probably due to an endocytic process. Nevertheless this disappearance is not a permanent one, suggesting a recycling of the PNA binding molecule. The cells that modulate their PNA binding sites after exposure to Thymosin alpha 1 are a small proportion of the total PNA+ thymocytes, indicating that not all thymocytes are susceptible to the thymic hormone Thymosin alpha 1. Conversely the exposure of thymocytes to Thymosin alpha 1 induces the disappearance of the binding sites for this ligand without further recycling, behavior expected for the receptor of a regulatory ligand. These results also indicate that the Thymosin alpha 1 and the PNA binding sites are on different molecules on the surface of the PNA+ thymocytes.
D000818:Animals; D037102:Lectins / Q000378:metabolism*; D007958:Leukocyte Count; D051379:Mice; D008810:Mice, Inbred C57BL; D019887:Peanut Agglutinin; D010641:Phenotype; D011975:Receptors, Mitogen / Q000187:drug effects*; D013601:T-Lymphocytes / Q000145:classification / Q000378:metabolism*; D000077596:Thymalfasin; D013947:Thymosin / Q000031:analogs & derivatives* / Q000494:pharmacology
D037102:Lectins; D019887:Peanut Agglutinin; D011975:Receptors, Mitogen; C038223:peanut agglutinin receptor; D013947:Thymosin; D000077596:Thymalfasin