Influence of L-glutamic acid on binding of interleukin-1beta, tumour necrosis factor-alpha and interleukin-6 to HL-60 cells.
To elucidate the mechanism of differentiating activity on L-Glu to HL-60 cells, its influence on binding of human recombinant interleukine-1beta (rHuIL-1beta), tumour necrosis factor-alpha (rHuTNF-alpha) and interleukine-6 (IL-6) by HL-60 cells was studied. It was established, that L-Glu converted the high affinity binding of [125I]rHuIL-1beta (Kd = 0.32 nM) and [125I]rHuIL-6 (Kd = 0.075 nM) to HL-60 cells into low affinity (corresponding Kd values -13.3 and 2.1 nM) at concentration 0.1 microM. The preincubation for an hour of HL-60 cells with 0.1 microM L-Glu was shown to result in an increase of affinity and number of [125I]rHuTNF-alpha binding sites. Thus, L-Glu decreases the sensitivity of the HL-60 cells to IL-1beta and IL-6 and increases TNF-alpha binding at concentration 0.1 microM.
Shemyakin-Ovchinnikov Institute of Bio-organic Chemistry, Russian Academy of Sciences, Moscow.
I A
IA
Kostanyan
R I
RI
Nurieva
E V
EV
Navolotskaya
M V
MV
Astapova
S M
SM
Dranitsina
A P
AP
Bogachuk
V P
VP
Zav'yalov
V M
VM
Lipkin
D018698:Glutamic Acid / Q000378:metabolism* / Q000494:pharmacology; D018922:HL-60 Cells; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism* / Q000494:pharmacology; D015850:Interleukin-6 / Q000378:metabolism* / Q000494:pharmacology; D007457:Iodine Radioisotopes; D007553:Isotope Labeling; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism* / Q000494:pharmacology
D007375:Interleukin-1; D015850:Interleukin-6; D007457:Iodine Radioisotopes; D011994:Recombinant Proteins; D014409:Tumor Necrosis Factor-alpha; D018698:Glutamic Acid