TY - JOUR
T1 - Activation of natural killer cells by the mAb YTA-1 that recognizes leukocyte function-associated antigen-1
AU - Sugle, Katsuji
AU - Nakamura, Kazuhiro
AU - Teshigawara, Keisuke
AU - Diamond, Michael S.
AU - Springer, Timothy A.
AU - Nakamura, Yoshiaki
AU - Leonard, Warren J.
AU - Uchida, Atsushi
AU - Yodoi, Junji
N1 - Funding Information:
Wfe thank Drs Kimishige Ishizaka, Carl H. June, Yasuhiro Minami, Amnon Altman and Toshiaki Kawakami for critical reading of the manuscript and useful advice, and Dr Atsushi Miyajima for valuable discussions. This work was supported by The Naito Foundation, OSAKA Cancer Research Fund, The Shimizu Foundation Research Grant, and a Grant-in-Aid for Scientific Research and Cancer Research from the Ministry of Education, Science and Culture, Japan
PY - 1995/5
Y1 - 1995/5
N2 - The mAb YTA-1, which brightly stains CD3-CD16+ large granular lymphocytes (LGL)/natural killer (NK) cells and CD8+ T cells by immunofluorescence, is specific for leukocyte function-associated antigen (LFA)-1. Some mAbs recognizing the LFA-1α chain (CD11a) or LFA-1β chain (CD18) inhibited the binding of YTA-1 to peripheral blood mononuclear cells. YTA-1 mAb could be chemically cross-linked to 170 and 96 kDa molecules, whose molecular weights correspond to those of LFA-1α and β respectively.YTA-1 bound to COS-7 cells co-transfected with CD11a and CD18 cDNAs, but not to untransfected cells. Reactivities of YTA-1 to K562 cells transfected with LFA-1α and β(CD11a/CD18) cDNAs and to CHO cells transfected with Mac-1 (CD11b/CD18) or p150, 95 (CD11c/CD18) cDNAs strongly suggest that YTA-1 recognizes either LFA-1α or an epitope formed by a combination of LFA-1α and β. Treatment of fresh CD3-CD16+ LGL with YTA-1 augmented cytolytic activity and induced proliferation. F(ab')2 fragments of YTA-1 augmented NK cytotoxicity, indicating that the NK activating signal was transmitted through LFA-1 without involvement of Fcγ receptor III. In contrast, the other mAbs against LFA-1 could not activate NK cells. These results collectively indicate that YTA-1 recognizes a unique epitope of LFA-1, which is involved in activation of fresh NK cells.
AB - The mAb YTA-1, which brightly stains CD3-CD16+ large granular lymphocytes (LGL)/natural killer (NK) cells and CD8+ T cells by immunofluorescence, is specific for leukocyte function-associated antigen (LFA)-1. Some mAbs recognizing the LFA-1α chain (CD11a) or LFA-1β chain (CD18) inhibited the binding of YTA-1 to peripheral blood mononuclear cells. YTA-1 mAb could be chemically cross-linked to 170 and 96 kDa molecules, whose molecular weights correspond to those of LFA-1α and β respectively.YTA-1 bound to COS-7 cells co-transfected with CD11a and CD18 cDNAs, but not to untransfected cells. Reactivities of YTA-1 to K562 cells transfected with LFA-1α and β(CD11a/CD18) cDNAs and to CHO cells transfected with Mac-1 (CD11b/CD18) or p150, 95 (CD11c/CD18) cDNAs strongly suggest that YTA-1 recognizes either LFA-1α or an epitope formed by a combination of LFA-1α and β. Treatment of fresh CD3-CD16+ LGL with YTA-1 augmented cytolytic activity and induced proliferation. F(ab')2 fragments of YTA-1 augmented NK cytotoxicity, indicating that the NK activating signal was transmitted through LFA-1 without involvement of Fcγ receptor III. In contrast, the other mAbs against LFA-1 could not activate NK cells. These results collectively indicate that YTA-1 recognizes a unique epitope of LFA-1, which is involved in activation of fresh NK cells.
KW - LFA-1
KW - Natural killer
KW - YT cell line
UR - http://www.scopus.com/inward/record.url?scp=0029008290&partnerID=8YFLogxK
U2 - 10.1093/intimm/7.5.763
DO - 10.1093/intimm/7.5.763
M3 - Article
C2 - 7547703
AN - SCOPUS:0029008290
SN - 0953-8178
VL - 7
SP - 763
EP - 769
JO - International Immunology
JF - International Immunology
IS - 5
ER -