TY - JOUR
T1 - Characterization of three new membrane structures on rat NK cells which are involved in activation of the lytic machinery
AU - Giezeman-Smits, Katinka M.
AU - Gorter, Arko
AU - Nagelkerke, J. Fred
AU - Van Vlierberghe, Ronald L.P.
AU - Van Eendenburg, Jaap
AU - Eggermont, Alexander M.M.
AU - Fleuren, Gert Jan
AU - Kuppen, Peter J.K.
N1 - Funding Information:
We thank ANDREA VAN NIEUWENHUIZEN and ANNEKE MELS for excellent technical assistance and Mrs. P. KIEVIT-TYSON for carefully reading the manuscript. This work was supported by grant RUL 95-1104 from the Dutch Cancer Society.
PY - 1997/11
Y1 - 1997/11
N2 - In this study, three membrane structures on rat NK cells which activate lysis of target cells were characterized. Furthermore, the role of adhesion molecules in this activation process, in particular the CD18-associated integrins, was investigated. Three rat NK-activation structures were identified which have not been previously described. These structures are apparently unique as they differed in molecular weight from known NK-activation structures. Cross-linking of these activation structures with specific mAbs and a FcγR-positive tumor cell line (P815) resulted in enhanced killing of these target cells by NK cells. If the CD18-associated integrins were masked by the anti-CD18 mAb WT.3, the redirected killing of P815 was completely blocked. This indicates that the CD18-associated integrins play a crucial role in activation of NK cells. Furthermore, our results show that rat NK cells possess multiple activation structures.
AB - In this study, three membrane structures on rat NK cells which activate lysis of target cells were characterized. Furthermore, the role of adhesion molecules in this activation process, in particular the CD18-associated integrins, was investigated. Three rat NK-activation structures were identified which have not been previously described. These structures are apparently unique as they differed in molecular weight from known NK-activation structures. Cross-linking of these activation structures with specific mAbs and a FcγR-positive tumor cell line (P815) resulted in enhanced killing of these target cells by NK cells. If the CD18-associated integrins were masked by the anti-CD18 mAb WT.3, the redirected killing of P815 was completely blocked. This indicates that the CD18-associated integrins play a crucial role in activation of NK cells. Furthermore, our results show that rat NK cells possess multiple activation structures.
UR - http://www.scopus.com/inward/record.url?scp=0030720262&partnerID=8YFLogxK
U2 - 10.1016/S0171-2985(97)80077-0
DO - 10.1016/S0171-2985(97)80077-0
M3 - Article
C2 - 9413744
AN - SCOPUS:0030720262
SN - 0171-2985
VL - 197
SP - 429
EP - 443
JO - Immunobiology
JF - Immunobiology
IS - 5
ER -