Multiple pathways from three types of sugar receptor sites to metabotropic transduction pathways of the blowfly: Study by the whole cell-clamp experiments

Author(s):  
Hideko Kan ◽  
Naoko Kataoka-Shirasugi ◽  
Taisaku Amakawa
1986 ◽  
Vol 32 (1) ◽  
pp. 80-83 ◽  
Author(s):  
A E Steiner ◽  
J L Wittliff

Abstract We used a whole-cell glucocorticoid receptor assay to examine characteristics of the glucocorticoid receptor in the lymphocytes of normal human donors. We measured binding of [3H]dexamethasone to the lymphocytes of four different donors on several different occasions; the variation about the mean for the assays was +/- 15%. Whole-cell assays in 15 normal subjects showed a mean value of 6.18 fmol/10(6) cells or 3722 sites per cell, with a somewhat higher level in men (7.67 fmol/10(6) cells, or 4620 sites per cell) than women (4.48 fmol/10(6) cells, or 2698 sites per cell). We saw no correlation between donor age and receptor values, in either group. Assays in which we used [3H]prednisolone demonstrated similar binding properties as with [3H]dexamethasone. The mean glucocorticoid receptor value for normal human T-cells from three donors was 2.52 fmol/10(6) cells, or 1518 sites per cell.


Nature ◽  
1974 ◽  
Vol 249 (5455) ◽  
pp. 311-311
Author(s):  

1981 ◽  
Vol 77 (1) ◽  
pp. 23-39 ◽  
Author(s):  
I Shimada ◽  
T Tanimura

N-Formylation and N-methylation of the alpha-amino group of L-phenylalanine result in extremely decreased responses of the labellar sugar receptor of the fleshfly, whereas the same structural alteration of L-valine hardly affects the response. Methyl esterification of the alpha-carboxyl group of phenylalanine, on the other hand, maintains the response to some extent, but similar treatment of valine completely diminishes the response. The aromatic structure in phenylalanine is not essential for stimulation. These results suggest a substantial difference in the stereospecificities and functional group specificities of the furnase (F) and aliphatic carboxylate (T) sites in the sugar receptor. The effect of small peptides on the sugar receptor was examined systematically. Their effectiveness depends mainly on the place of the constituent amino acids rather than on their composition, indicating the decisive role that certain aliphatic amino acids in the C-terminal position play in stimulation. Remarkable regularities in the stimulating effectiveness of small peptides exactly correspond to the stereospecificity of each receptor site. We propose two hypothetical models of the F and T sites, which involve three and two subsites, respectively, that are capable of hydrogen bond formation. The F and T sites also have a hydrophobic subsite that discriminates the R groups of the stimulants and a few spatial barriers.


1974 ◽  
Vol 20 (3) ◽  
pp. 605-621 ◽  
Author(s):  
Ichiro Shimada ◽  
Akio Shiraishi ◽  
Hiromasa Kijima ◽  
Hiromichi Morita

1968 ◽  
Vol 52 (4) ◽  
pp. 559-583 ◽  
Author(s):  
Hiromichi Morita ◽  
Akio Shiraishi

Responses of the labellar sugar receptor of the fleshfly, Boettcherisca peregrina, were studied over a wide range of concentrations of several sugars (sucrose, maltose, glucose, fructose, and mannose) in single solutions and in mixtures. The results suggest (a) that the receptor sites are not completely differentiated for glucose and for fructose combination, (b) that the receptor site is composed of two subunits. Such suggestions are based on the classical model, where the response is proportional to the number of the sites, two subunits of each site being simultaneously occupied with one molecule of disaccharides or two molecules of monosaccharides. It is shown, however, that an allosteric model gives a somewhat better interpretation of the experimental results.


1968 ◽  
Vol 52 (3) ◽  
pp. 559-583 ◽  
Author(s):  
Hiromichi Morita ◽  
Akio Shiraishi

Responses of the labellar sugar receptor of the fleshfly, Boettcherisca peregrina, were studied over a wide range of concentrations of several sugars (sucrose, maltose, glucose, fructose, and mannose) in single solutions and in mixtures. The results suggest (a) that the receptor sites are not completely differentiated for glucose and for fructose combination, (b) that the receptor site is composed of two subunits. Such suggestions are based on the classical model, where the response is proportional to the number of the sites, two subunits of each site being simultaneously occupied with one molecule of disaccharides or two molecules of monosaccharides. It is shown, however, that an allosteric model gives a somewhat better interpretation of the experimental results.


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