PMID- 2715641
OWN - NLM
STAT- MEDLINE
DCOM- 19890622
LR  - 20071114
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 142
IP  - 11
DP  - 1989 Jun 1
TI  - Regulation of formyl peptide receptor binding to rabbit neutrophil plasma 
      membranes. Use of monovalent cations, guanine nucleotides, and bacterial toxins 
      to discriminate among different states of the receptor.
PG  - 3963-70
AB  - The regulation by monovalent cations, guanine nucleotides, and bacterial toxins 
      of [3H]FMLP binding to rabbit neutrophil plasma membranes was studied by using 
      dissociation techniques to identify regulatory effects on separate receptor 
      states. Under conditions of low receptor occupancy (1 nM [3H]FMLP) and in both 
      Na+ and K+ buffers, dissociation is heterogenous, displaying two distinct, 
      statistically significant off rates. [3H]FMLP binding was enhanced by 
      substituting other monovalent cations for Na+. In particular, enhanced binding in 
      the presence of K+ relative to Na+ was caused by additional binding to both 
      rapidly and slowly dissociating receptors. Three receptor dissociation rates, two 
      of which appear to correspond to the two affinity states detected in equilibrium 
      binding studies, were defined by specific GTP and pertussis toxin (PT) 
      treatments. Neither GTP, nor PT or cholera toxins (CT) had an effect on the rate 
      of dissociation of [3H]FMLP from the rapidly dissociating form of the receptor. 
      Both 100 microM GTP and PT treatments increased the percentage of rapidly 
      dissociating receptors, correspondingly decreasing the percentage of slowly 
      dissociating receptors. The observed changes in the rapidly and slowly 
      dissociating receptors after GTP, PT, and CT treatments were caused by an 
      absolute decrease in the amount of binding to the slowly dissociating receptors. 
      However, complete inhibition of slowly dissociating receptor binding by GTP, PT, 
      or both was never observed. Both GTP and PT treatments, but not CT treatment, 
      increased by two-fold the rate of dissociation of 1 nM [3H]FMLP from the slowly 
      dissociating form of the receptor, resulting in a third dissociation rate. Thus, 
      slowly dissociating receptors comprise two different receptor states, a G 
      protein-associated guanine nucleotide and PT-sensitive state and a guanine 
      nucleotide-insensitive state.
FAU - Feltner, D E
AU  - Feltner DE
AD  - Department of Pathology, University of Michigan Medical School, Ann Arbor 48109.
FAU - Marasco, W A
AU  - Marasco WA
LA  - eng
GR  - HL-28445/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Bacterial Toxins)
RN  - 0 (Cations, Monovalent)
RN  - 0 (Guanine Nucleotides)
RN  - 0 (Receptors, Formyl Peptide)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Virulence Factors, Bordetella)
RN  - 10028-17-8 (Tritium)
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 9012-63-9 (Cholera Toxin)
RN  - EC 2.4.2.31 (Pertussis Toxin)
SB  - IM
MH  - Animals
MH  - Bacterial Toxins/*pharmacology
MH  - Binding, Competitive
MH  - Cations, Monovalent/*pharmacology
MH  - Cell Membrane/metabolism
MH  - Cholera Toxin/pharmacology
MH  - Guanine Nucleotides/*pharmacology
MH  - Guanosine Triphosphate/pharmacology
MH  - N-Formylmethionine Leucyl-Phenylalanine/*metabolism
MH  - Neutrophils/*metabolism
MH  - Pertussis Toxin
MH  - Rabbits
MH  - Receptors, Formyl Peptide
MH  - Receptors, Immunologic/*drug effects/metabolism
MH  - Tritium
MH  - Virulence Factors, Bordetella/pharmacology
EDAT- 1989/06/01 00:00
MHDA- 1989/06/01 00:01
CRDT- 1989/06/01 00:00
PHST- 1989/06/01 00:00 [pubmed]
PHST- 1989/06/01 00:01 [medline]
PHST- 1989/06/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1989 Jun 1;142(11):3963-70.