Isolation, Biochemical Analysis, and N-Terminal Amino Acid Sequence of a Cell Surface Glycoprotein that Binds to the 'Erythrocyte Receptor' of T-Lymphocytes

Autor: T. Hünig, F. Lottspeich, G. Tiefenthaler, R. Mitnacht
Rok vydání: 1987
Předmět:
Zdroj: Haematology and Blood Transfusion / Hämatologie und Bluttransfusion ISBN: 9783540177548
DOI: 10.1007/978-3-642-72624-8_70
Popis: Recent findings have provided strong evidence in support of a functional role of the “erythrocyte receptor” of human T-lymphocytes in T-cell activation. Thus, binding of appropriate ligands (erythrocytes or monoclonal antibodies) to the CD2 molecule, as this receptor is now called, can either block (Palacios and Martinez-Maza 1982; Martin et al. 1983; Krensky et al. 1983) or stimulate (Larsson et al. 1978; Meuer et al. 1984) T-cell proliferation and expression of T-cell function. We have previously suggested that CD2 is a cell interaction molecule, the natural ligand of which is expressed on cells with which T-lymphocytes interact during immune responses (Hunig 1985, 1986). Since the CD2 molecule had previously been characterized by the T11 antigen(s), we have named this ligand T11 target structure or T11TS.
Databáze: OpenAIRE