TY - JOUR
T1 - Human peripheral blood lymphocytes bearing T cell receptor γ/δ. Expression of CD8 differentiation antigen correlates with the expression of the 55-kD, Cγ2-encoded γ chain
AU - Moretta, A.
AU - Bottino, C.
AU - Ciccone, E.
AU - Tambussi, G.
AU - Mingari, M. C.
AU - Ferrini, S.
AU - Casorati, G.
AU - Varese, P.
AU - Viale, O.
AU - Migone, N.
AU - Moretta, L.
PY - 1988
Y1 - 1988
N2 - We analyzed the CD3-associated molecules present on peripheral blood-derived TCR-γ/δ+ clones that express CD8 surface antigens. Clones was derived by limiting dilution from CD3+ WT31- FACS-purified populations derived from several donors. Eight of > 300 TCR-γ/δ+ clones analyzed expressed CD8 and reacted with δ-TCS-1 mAb. Cell numbers suitable for more detailed analyses could be obtained from four clones, including one derived from thymus. Analysis of CD3-associated TCR molecules immunoprecipitated by anti-Leu-4 (anti-CD3) mAb under conditions that preserve the CD3/TCR association (1% digitonin) showed a predominant 55-60-kD molecule both under reducing and nonreducing conditions. On the other hand, the δ-TCS-1-reactive molecules immunoprecipitated from 25 CD3+ δ-TCS-1+ CD8- clones, in all instances, displayed a 40-44-kD mol mass. In two-dimensional PAGE, TCR-γ molecules precipitated from δ-TCS-1+ CD8+ clones appeared more acidic than those of BB3+ or δ-TCS-1+ CD8+ clones. Southern analysis confirmed that this type of non-disulphide-linked TCR-γ/δ is also coded for by the Cγ2 gene segment.
AB - We analyzed the CD3-associated molecules present on peripheral blood-derived TCR-γ/δ+ clones that express CD8 surface antigens. Clones was derived by limiting dilution from CD3+ WT31- FACS-purified populations derived from several donors. Eight of > 300 TCR-γ/δ+ clones analyzed expressed CD8 and reacted with δ-TCS-1 mAb. Cell numbers suitable for more detailed analyses could be obtained from four clones, including one derived from thymus. Analysis of CD3-associated TCR molecules immunoprecipitated by anti-Leu-4 (anti-CD3) mAb under conditions that preserve the CD3/TCR association (1% digitonin) showed a predominant 55-60-kD molecule both under reducing and nonreducing conditions. On the other hand, the δ-TCS-1-reactive molecules immunoprecipitated from 25 CD3+ δ-TCS-1+ CD8- clones, in all instances, displayed a 40-44-kD mol mass. In two-dimensional PAGE, TCR-γ molecules precipitated from δ-TCS-1+ CD8+ clones appeared more acidic than those of BB3+ or δ-TCS-1+ CD8+ clones. Southern analysis confirmed that this type of non-disulphide-linked TCR-γ/δ is also coded for by the Cγ2 gene segment.
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M3 - Article
C2 - 3264327
AN - SCOPUS:0024255823
VL - 168
SP - 2349
EP - 2354
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
SN - 0022-1007
IS - 6
ER -