| Autor: |
Mikhaleva II, Ivanov VT, Voĭtenkov VB, Vechkanov EM, Bondarenko TI |
| Jazyk: |
ruština |
| Zdroj: |
Bioorganicheskaia khimiia [Bioorg Khim] 2013 May-Jun; Vol. 39 (3), pp. 277-84. |
| DOI: |
10.1134/s1068162013030096 |
| Abstrakt: |
We have undertaken a comparative study on physiological activity of well known neuropeptide DSIP (WAGGDASG E) and new closely related peptide KND (WKGGNASGE) in vivo assays. The sequence of K2, N5-DSIP (KND) was found recently by the computer search for DSIP homologous sequences in available nucleotide and protein databases at 324-332 site of Lysine-specific demethylase 3 B (EC 1.14.11, Swiss-Prot: Q7LBC6.1, 1-1761aa). This human lysine-specific histone demethylase is a representative of the recently discovered family of so called JmjC-domain-containing histone demethylases encoded by JMJD1B gene and ubiquitously expressed in tissues of various mammalian species. Biological investigations performed in this work confirm our preliminary data that DSIP-related peptide KND exhibits the similar biological properties in comparison with DSIP. Assessed by us antioxidative, anticonvulsive and behavioral effects of KND were even more expressed than in DSIP case. These results provide the additional evidences to support our suggestion that KND can be a possible endogenous prototype of "real" DSIP. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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