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Biomedical subjects

L A Goncharova

Publications and source records attributed to L A Goncharova.

14 recordsLinked to original sources
PubMed1981

[Diagnosis and treatment of bone tumors complicated by pathological fractures].

The article elucidates certain questions of modern methods of diagnosis and treatment of tumors of long tubular bones complicated by pathological fractures. The methods were used for the treatment of 41 patients. The authors emphasize the importance of such methods as radio- and angiography, punctional and trepanobiopsy, measurement of the intraosseous pressure. The efficiency of the ultrasound resection in association with cryodestruction for the treatment of the diseases mentioned is reported.

Adolescent↗
PubMedDate not supplied

[Selenium correction of male subfertility].

To study the effect of selenium in subfertile men, three groups of men were studied. Group 1--31 subfertile men living in healthy environment, group 2--25 subfertile men exposed for a long time to low doses of gas containing hydrogen sulfide, group 3--control 43 fertile men. Men of groups 1 and 2 received 3 courses of selenium (3.5 microg/kg/day for 30 days). Before the treatment and after each course ejaculate fertility was assessed by spermogram, enzyme activity of alpha-amylase (EC 3.2.1.1) and lactate dehydrogenase (EC 1.1.1.27), concentrations of prostatic acid phosphatase, sperm-specific inhibitor tripsin and prostate-specific antigen. Selenium proved effective, the response being higher in group 2 than in group 1. The causes of this difference are discussed. It is thought possible to use selenium for correction of some subfertility forms in men.

Acid Phosphatase↗
PubMedDate not supplied

[Biosynthesis of proteins and ribonucleic acids in red and white rat skeletal muscles].

Protein biosynthesis is studied in red and white rat shank muscles in vitro. It is found that the incorporation rate of 14C-lysine in red muscle was 2-fold higher than that in white muscle. The difference in the lysine incorporation rate into muscle proteins studied increased with the increase of lysine molar concentration in the incubation medium, which was probably due to a selective protein synthesis activation in the red muscle. A higher level of 14C-lysine incorporation in red muscle proteins was found under similar uptake of the labelled amino acid in both red and white muscles. RNA synthesis rate was the same in both muscles and its inhibition with actinomycin D did not affect the ratio of protein synthesis rates in red and white muscles.

Animals↗
PubMedDate not supplied

[Effect of prolonged weightlessness on protein metabolism in rat red and white skeletal muscles].

With the aid of C14-leucine incorporation into proteins the protein synthesis in the red (m. soleus) and white (m. extensor dig. longus) skeletal muscles of flight and synchronous rats from the Cosmos-605 experiment was investigated. On the 2nd postflight day the total synthesis of proteins (as calculated per whole muscle) in the red muscle of flight rats remained unaltered. Therefore, distinct atrophy of this muscle that was seen only in flight rats can be attributed to increased degradation of proteins. On the 2nd postflight day the white muscle of both flight and synchronous rats showed moderate atrophy, not only increased protein degradation but also inhibited protein synthesis contributes to this.

Actomyosin↗
PubMedDate not supplied

[Metabolic mechanisms of different types of disuse muscular atrophy].

Radiotracer studies in vivo on protein biosynthesis have been made in red (m. soleus) and white (m. extensor digitorum longus) rat shin muscles during their disuse atrophy caused by foot exarticulation. The rate of protein biosynthesis (as calculated per mass unit of total RNA) was increased in the white muscle on the 4th and 14th days, being unaltered on the 7th day after the surgery, but this rate was decreased in the red muscle at all these stages. The data obtained suggest that all these stages. The data obtained suggest that the atrophy, more pronounced in the red muscle than in the white one, can be mainly attributed in the former to decreased protein biosynthesis but in the latter to the increased protein degradation.

Animals↗
PubMedDate not supplied

[Patterns of adaptive mobilization of proteins from skeletal muscles during development of compensatory hypertrophy of internal organs].

These studies were dealing with muscle protein depletion in rats under the heart hypertrophy induced by aorta coarctation or under liver regeneration after partial hepatectomy. The last experimental model was also used in order to establish how far such protein mobilization from muscles is realized during their simultaneous adaptation to local overload or disuse induced by a surgical method. 3 and 7 days after induction of hypertrophy of organs investigated, the quantities of sarcoplasmic, myofibrillar and stroma proteins were measured in last-twitch (m. extensor digitorum longus, m. biceps brachii) and slow-twitch (m. soleus) muscles. The contributions of protein biosynthesis and/or protein degradation change into muscle protein loss were evaluated by specially elaborated radiotracer method. The data obtained demonstrate that the pattern of muscle protein mobilization depends on nature of organ and rate of its hypertrophy. The process occurs differently in muscle of different type and in various muscle structures. It appears to be potentiated in overloaded muscles and to a lesser extent in unused ones. The loss of muscle proteins is certainly associated with inhibition of their biosynthesis. Increased degradation (or release) of preformed (non-labelled) protein molecules may also contribute to this loss whereas degradation of newly-formed (labelled) molecules does not change appreciably, possibly because their distribution in muscle structures is non-uniform.

Animals↗
PubMedDate not supplied

[Effect of long-term space flight on protein biosynthesis in different rat tissues and organs].

Protein synthesis in the heart, lungs, liver, pancreas, thymus, kidneys, skeletal muscles and testes of the 22-day Cosmos-605 flight and synchronous rats was studied with the aif of 14C-amino acid incorporation. On the 2nd postflight day both flight and synchronous rats showed an increased synthesis of heart sarcoplasmatic proteins. On the 26th postflight day the rate of incorporation was normal. On the 2nd and 26th days the synthesis of myofibrillar proteins in the m. quadriceps femoris was inhibited in flight animals postflight day the rate of incorporation was normal. On the 2nd and 26th days the syn-only. On the 2nd and 26th days the liver of the flight and synchronous rats showed qualitatively similar changes in protein metabolism of subcellular structures. No changes in the protein synthesis of other organs tested were detected.

Animals↗