Changes in purine metabolism in the macrophages of mice exposed to a new synthetic analog of muramyl dipeptide

It has been established that N-acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP), a new synthetic analog of muramyl dipeptide, while incubated in vitro with macrophages essentially inhibits 5'-nucleotidase (5-N) activity without any influence on the activity of adenosine deamina...

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Bibliographic Details
Published inBiulleten' eksperimental'noi biologii i meditsiny Vol. 99; no. 6; p. 685
Main Authors Umanskiĭ, V Iu, Tarakhovskiĭ, A M, Andronova, T M
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.06.1985
Subjects
5'-Nucleotidase
Acetylmuramyl-Alanyl-Isoglutamine - analogs & derivatives
Acetylmuramyl-Alanyl-Isoglutamine - pharmacology
Adenosine Deaminase - metabolism
Adjuvants, Immunologic - pharmacology
Animals
Cells, Cultured
Macrophages - drug effects
Macrophages - metabolism
Mice
Mice, Inbred BALB C
Nucleotidases - metabolism
Purines - metabolism
Time Factors
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Summary:It has been established that N-acetylglucosaminyl-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP), a new synthetic analog of muramyl dipeptide, while incubated in vitro with macrophages essentially inhibits 5'-nucleotidase (5-N) activity without any influence on the activity of adenosine deaminase in these cells. The maximal effect was recorded 24 h after co-incubation. As 0.01 = 1 microgram/ml concentration of GMDP was added, the enzyme activity gradually decreased to minimum. L-D-isomer of GMDP was shown to affect 5-N activity whereas the effect of its analog with a double peptide chain GM (DP)2 was found to be less. Inhibition of 5-N activity may be one of the mechanisms by which macrophages are activated under the influence of GMDP.
ISSN:0365-9615