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L I Sidorenko

Publications and source records attributed to L I Sidorenko.

10 recordsLinked to original sources

[Relation of the biosynthesis of intracellular and export proteins in rat liver cells during induction of proliferation by cycloheximide].

After a single injection of a sublethal dose of cycloheximide (CHI) the biosynthesis of extracellular proteins in rat hepatocytes was rapidly suppressed, the reconstitution being very slow. On the contrast, the biosynthesis of intracellular proteins (e.g., histones, and other acid-soluble liver proteins) was more resistant to CHI. The activation of biosynthesis of acid-soluble and acid-insoluble proteins was found to occur stepwise. It was assumed that the activation of synthesis and accumulation of intracellular proteins after CHI release accompanied by a decreased synthesis of extracellular proteins is one of possible causes of stimulation of DNA synthesis in the hepatocytes following a single injection of CHI.

Animals↗

[Activation of chromatin and histone proteolysis during protein synthesis inhibition in liver cells].

The initial response of rat liver chromatin to strong (up to 95%) inhibition of protein synthesis by cycloheximide consist in activation (2-3-fold) of proteolysis of weakly bound nuclear histones, especially of the acetylated histone H3, in a decrease (7-8-fold) of the rate of histone acetylation, in an increased sensitivity of chromatin to DNAase I (EC 3.1.4.5) and in transformations of the DNA-histone interactions during the first 1-2 hours after inhibition of translation. This results in a temporary activation of chromatin which manifests itself in acceleration of RNA synthesis. Within 3 hours following the inhibition of translation the rate of proteolysis in the nucleus, the amount of acetylated forms of histone H3 and other acetylated proteins, the sensitivity of chromatin to DNAase I and the rate of RNA synthesis are decreased. It is assumed that at strong inhibition of protein synthesis one of the factors controlling chromatin activity is a specific proteolysis of modified histones.

Acetylation↗

[Chromatin biogenesis in higher animal cells. Acceleration of catabolism and transport of non-histone proteins into the nucleus under conditions of protein synthesis inhibition].

Repression by 95% of protein synthesis in rat liver cells after a single injection of a sublethal dose of cycloheximide (0.3 mg per 100 g of body weight) accelerates the transport of loosely bound to chromatin NHB (sNHB), in particular, that of proteins HMG 1 and HMG 2 from the cytoplasm into the nuclei. The activation of transport of sNHB and HMG proteins is correlated in time with the increase in activity of chromatin transcription by RNA-polymerase II. Simultaneously the rate of protein proteolysis in the nucleus is increased. The half-life time of HMG proteins and some other sNHB in the nucleus is about 1-2 hrs and is close to that of the decrease in activity of chromatin transcription by RNA polymerases I and II from the 1st to the 3rd hr following cycloheximide injection. It was assumed that the proteins HMG and other sNHB with a short life-time are responsible for a rapid positive control of chromatin activity. The dynamics of nuclear chromatin activity during the first three hours of protein synthesis inhibition depend on sNHB content in the nucleus, which, in its turn, depends on the pool of the cytoplasm, correlation of sNHB transport from the cytoplasm into the nuclei and on their proteolysis in the nucleus.

Animals↗

[Biogenesis of chromatin in animal cells. Stimulation of nuclear protein and DNA synthesis in hepatocytes after brief inhibition of translation by cycloheximide].

A drastic and brief inhibition of protein synthesis (up to 95% for 3--6 hrs) by cycloheximide in the liver of rats starved for 24 hrs results in a recovery and subsequent marked stimulation of non-histone proteins, histone chromosomal proteins and DNA. The stimulation of non-histone protein synthesis was observed after 1 hr (inhibition) 12--24 hrs (recovery and stimulation of protein synthesis) and 48--60 hrs (stimulation of DNA synthesis) following the administration of cycloheximide. Two periods of histone biosynthesis were observed. The first one (24--36 hrs) was not coupled and the second one (48--60 hrs) was coupled with DNA replication. During the recovery and stimulation of protein synthesis acetylation of the histone and non-histone proteins proceeds at an increased rate. Possible applicability of the model in question for investigations of chromatin biogenesis is discussed.

Animals↗

[Stimulation of nuclear membrane components and DNA biosynthesis in rat liver cells after inhibition of translation with cycloheximide].

After a drastic inhibition of protein synthesis (95%) in rat liver by cycloheximide (0.2-0.4 mg/100 g of body weight) the recovery and subsequently prolonged marked stimulation of proteins, lipids and DNA were found. The correlation of nuclear membrane proteins and lipids synthesis was observed in a recovery and stimulation phases. Nuclear DNA synthesis increases after the stimulation biosynthesis of nuclear membrane components (36-40 hours after cycloheximide injection). The changes of a phospholipid composition and structure organisation of nuclear membrane hydrophobic zones (by spin probe) were found in stimulated DNA synthesis (48-60 hours).

Animals↗

[Ecdysterone modulates antitumor activity of cytostatics and biosynthesis of macromolecules in tumor-bearing animals].

The influence of therapeutic and half doses of cisplatin and adriamicin combination with the anabolic drug ecdisteron (20-hydroecdison) on development of subcutaneously and intraperitonially transplanted P388 and L1210 leukemia and metastasizing B16 melanoma was studied. Ecdisteron significantly stimulated the chemotherapeutic effect of low doses of the cytostatics: inhibition of tumor growth, mice survival rate, their lifespan, and the antimetastatic activity index were comparable or better than after therapy with high doses of the antitumor drugs. The influence of high and low doses of cisplatin and its low dose in combination with ecdisteron on the dynamics of protein and DNA biosynthesis in the liver, pancreas, thymus, spleen, and adrenals of tumor-bearing mice were also studied. Although the therapeutic effect of 4 mg/kg cisplatin by activated protein biosynthesis and DNA repair is comparable or better than that of its low dose (2 mg/kg) in combination with ecdisteron, in terms of chemotherapy the combination looks preferable since the therapeutic dose of cisplatin is toxic for the intact tissues.

Adrenal Glands↗

[The inhibitor of free radical processes decrease of protein biosynthesis in gun short wound tissues and weaken development of the general adaptation syndrome].

The dynamics of total protein biosynthesis and procollagen biosynthesis in skeletal muscle of injury tissues with the antioxidant BHT (dibunol) treatment and with common healing were studied. The obtained date indicate that the AO treatment reduce the rate of biosynthesis both the total proteins and procollagen at the 3th day of healing. Dibunol also considerably reduce the protein biosynthesis in adrenals and brake of corticosteroids biogenesis as measured by ESR-signals intensity of reduced adrenodoxine. AO treatment also reduce the protein biosynthesis in thymus, spleen and bone marrow. The lowering of functional activity of endocrine and immune systems indicate that the AO significantly inhibit the systemic reactions of organism induced by acute wound affect. It was suggested that as "primary mediator" of stress-reaction may be considered lipoperoxide radicals and decay products of lipohydroperoide.

Animals↗

[Paramagnetic metal complexes of iron in the regenerative processes of the liver].

ESR study was carried out of the content of oxidized form of cytochrom P-450 at regenerative processes in the liver. It has been shown that after partial hepatectomia and the effect of cycloheximid in the liver of experimental animals regular gradual changes of the content of the paramagnetic form of cytochrom P-450 are observed, an inverse correlation between these changes and protein biosynthesis being noted.

Animals↗