PMID- 2532552
OWN - NLM
STAT- MEDLINE
DCOM- 19900221
LR  - 20181113
IS  - 0006-3495 (Print)
IS  - 1542-0086 (Electronic)
IS  - 0006-3495 (Linking)
VI  - 56
IP  - 5
DP  - 1989 Nov
TI  - Competition between solution and cell surface receptors for ligand. Dissociation 
      of hapten bound to surface antibody in the presence of solution antibody.
PG  - 955-66
AB  - We present a joint theoretical and experimental study on the effects of 
      competition for ligand between receptors in solution and receptors on cell 
      surfaces. We focus on the following experiment. After ligand and cell surface 
      receptors equilibrate, solution receptors are introduced, and the dissociation of 
      surface bound ligand is monitored. We derive theoretical expressions for the 
      dissociation rate and compare with experiment. In a standard dissociation 
      experiment (no solution receptors present) dissociation may be slowed by 
      rebinding, i.e., at high receptor densities a ligand that dissociates from one 
      receptor may rebind to other receptors before separating from the cell. Our 
      theory predicts that rebinding will be prevented when S much greater than 
      N2Kon/(16 pi 2D a4), where S is the free receptor site concentration in solution, 
      N the number of free surface receptor sites per cell, Kon the forward rate 
      constant for ligand-receptor binding in solution, D the diffusion coefficient of 
      the ligand, and a the cell radius. The predicted concentration of solution 
      receptors needed to prevent rebinding is proportional to the square of the cell 
      surface receptor density. The experimental system used in these studies consists 
      of a monovalent ligand, 2,4-dinitrophenyl (DNP)-aminocaproyl-L-tyrosine (DCT), 
      that reversibly binds to a monoclonal anti-DNP immunoglobulin E (IgE). This IgE 
      is both a solution receptor and, when anchored to its high affinity Fc epsilon 
      receptor on rat basophilic leukemia (RBL) cells, a surface receptor. For RBL 
      cells with 6 x 10(5) binding sites per cell, our theory predicts that to prevent 
      DCT rebinding to cell surface IgE during dissociation requires S much greater 
      than 2,400 nM. We show that for S = 200-1,700 nM, the dissociation rate of DCT 
      from surface IgE is substantially slower than from solution IgE where no 
      rebinding occurs. Other predictions are also tested and shown to be consistent 
      with experiment.
FAU - Goldstein, B
AU  - Goldstein B
AD  - Theoretical Division, University of California, Los Alamos National Laboratory, 
      New Mexico 87545.
FAU - Posner, R G
AU  - Posner RG
FAU - Torney, D C
AU  - Torney DC
FAU - Erickson, J
AU  - Erickson J
FAU - Holowka, D
AU  - Holowka D
FAU - Baird, B
AU  - Baird B
LA  - eng
GR  - AI18306/AI/NIAID NIH HHS/United States
GR  - AI22449/AI/NIAID NIH HHS/United States
GR  - GM35556/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biophys J
JT  - Biophysical journal
JID - 0370626
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (Haptens)
RN  - 0 (Ligands)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - 0 (Solutions)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Animals
MH  - Antigens, Differentiation, B-Lymphocyte/*metabolism
MH  - Binding, Competitive
MH  - Cell Line
MH  - Cell Membrane/immunology
MH  - Haptens
MH  - Immunoglobulin E/*metabolism
MH  - Kinetics
MH  - Leukemia, Basophilic, Acute/immunology
MH  - Leukemia, Experimental/immunology
MH  - *Ligands
MH  - Mathematics
MH  - *Models, Theoretical
MH  - Rats
MH  - Receptors, Fc/*metabolism
MH  - Receptors, IgE
MH  - Solutions
PMC - PMC1280594
EDAT- 1989/11/01 00:00
MHDA- 1989/11/01 00:01
PMCR- 1990/11/01
CRDT- 1989/11/01 00:00
PHST- 1989/11/01 00:00 [pubmed]
PHST- 1989/11/01 00:01 [medline]
PHST- 1989/11/01 00:00 [entrez]
PHST- 1990/11/01 00:00 [pmc-release]
AID - S0006-3495(89)82741-9 [pii]
AID - 10.1016/S0006-3495(89)82741-9 [doi]
PST - ppublish
SO  - Biophys J. 1989 Nov;56(5):955-66. doi: 10.1016/S0006-3495(89)82741-9.