Why is it so hard to dissociate multivalent antigens from cell-surface antibodies?

被引:27
作者
Goldstein, B [1 ]
Wofsy, C [1 ]
机构
[1] UNIV NEW MEXICO,DEPT MATH & STAT,ALBUQUERQUE,NM 87131
来源
IMMUNOLOGY TODAY | 1996年 / 17卷 / 02期
关键词
D O I
10.1016/0167-5699(96)80583-4
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
It is often difficult to induce dissociation of multivalent antigens that are bound to cells by surface-associated immunoglobulin (sIg), even when high concentrations of monovalent hapten are used to fill all free binding sites. Here, Byron Goldstein and Carla Wofsy discuss the evidence that this appears to be due to a cellular and propose that a receptor-desensitization process is responsible for the transition of multivalent antigens to a dissociation-resistant state.
引用
收藏
页码:77 / 80
页数:4
相关论文
共 22 条
[1]  
APGAR JR, 1990, J IMMUNOL, V145, P3814
[2]   BIVALENT LIGAND DISSOCIATION KINETICS FROM RECEPTOR-BOUND IMMUNOGLOBULIN-E - EVIDENCE FOR A TIME-DEPENDENT INCREASE IN LIGAND REBINDING AT THE CELL-SURFACE [J].
ERICKSON, JW ;
POSNER, RG ;
GOLDSTEIN, B ;
HOLOWKA, D ;
BAIRD, B .
BIOCHEMISTRY, 1991, 30 (09) :2357-2363
[3]  
FEWTRELL C, 1985, CALCIUM BIOL SYSTEMS, P129
[4]   COMPETITION BETWEEN SOLUTION AND CELL-SURFACE RECEPTORS FOR LIGAND - DISSOCIATION OF HAPTEN BOUND TO SURFACE ANTIBODY IN THE PRESENCE OF SOLUTION ANTIBODY [J].
GOLDSTEIN, B ;
POSNER, RG ;
TORNEY, DC ;
ERICKSON, J ;
HOLOWKA, D ;
BAIRD, B .
BIOPHYSICAL JOURNAL, 1989, 56 (05) :955-966
[5]  
HOLOWKA D, 1990, CELLULAR MOL MECHANI, V1, P173
[6]  
LABRECQUE GF, 1989, J IMMUNOL, V142, P236
[7]  
LICHTENSTEIN LM, 1971, J IMMUNOL, V107, P1122
[8]  
MACGLASHAN D, 1983, J IMMUNOL, V130, P2337
[9]  
MACGLASHAN D, 1983, J IMMUNOL, V130, P2330
[10]  
MACGLASHAN DW, 1981, J IMMUNOL, V127, P2410