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T S Chirikova

Publications and source records attributed to T S Chirikova.

10 recordsLinked to original sources
PubMed1999

Tissue distribution of rat macroglobulins in tumour-bearing rats.

Rat macroglobulins were determined in blood sera and extracts of tissues of intact rats and rats with Walker carcinoma by rocket immunoelectrophoresis. The serum levels of alpha1-macroglobulin (alpha1MG) alpha2-macroglobulin (alpha2MG) and pregnancy-associated alpha1-glycoprotein (alpha1PAG) were 1.86 +/- 0.07 mg/ml, 0.12 +/- 0. 02 mg/ml and 18.32 +/- 4.07 AU/ml respectively in control rats. Maximum concentrations of alpha1MG were found in heart, lung and spleen and lesser quantities were in liver and thymus, while alpha2MG and alpha1PAG were not found at all in tissue extracts from control rats. Serum alpha2MG and alpha1PAG concentrations increased more than 30-fold in tumour-bearing rats compared to control animals, while alpha1MG serum concentration was little changed. Increases in all three macroglobulins occurred in the tissues of tumour-bearing rats, particularly alpha1PAG. The tissue concentrations of alpha1MG and alpha2MG were similar and the tissue distribution was also similar with highest concentrations in heart and lung. Considerable quantities of the proteins were found in the tumour and part of peritoneum which made contact with the tumour. Changes in the protein concentrations in serum and tissue extracts of tumour-bearing rats suggest that all members of rat macroglobulin family are disturbed during the development of the Walker carcinoma, though only alpha2MG and alpha1PAG were substantially elevated.

Animals↗
PubMed1994

Changes in tissue distribution of rat alpha 1-macroglobulin and pregnancy-associated alpha 1-glycoprotein after inflammatory injury.

Antiserum against rat alpha 1-macroglobulin (alpha 1MG) was produced in rabbits. Antiserum against rat pregnancy-associated alpha 1-glycoprotein (PAG) was obtained by immunization with a partly purified PAG preparation and absorption of the serum with male rat serum. Acute inflammation was produced in non-pregnant female rats by a single intramuscular injection of turpentine. The concentrations of both macroglobulins in the serum and in tissue extracts were measured by rocket immunoelectrophoresis at various times up to 7 days after injury. Inflammation produced in the rats resulted in moderately elevated serum levels of these proteins soon after injury. At first, alpha 1MG levels in a number of tissues (heart, lung, kidney, spleen, pancreas, uterus and ovary) were depressed markedly; they then stabilized. The elevated serum concentrations of alpha 1MG remained unchanged during inflammation. The store of PAG in the tissues was rapidly depleted and its serum level decreased to a normal value 7 days after injury. Our findings indicate that alpha 1MG plays a more important role in maintenance of the proteinase inhibitory potential in the rat than does PAG.

Acute-Phase Reaction↗
PubMedDate not supplied

[Influence of the inflammatory reaction on the distribution of alpha1-macroglobulin and pregnancy-associated alpha1-glycoprotein in the rat].

The authors studied the distribution of proteinase inhibitors in inflammation induced by intramuscular turpentine injection. It was found that it reduces the concentration of the studied proteins in the tissues, which is attended by an increase of their plasma levels. The store of pregnancy-associated alpha 1-glycoprotein in the tissues is rapidly depleted, while the concentration of alpha 1-microglobulin reduces to a relatively stable level. The role of the both proteins in the inflammatory process is discussed.

Animals↗
PubMedDate not supplied

[The evolutionary problems of the family of human and animal macroglobulins].

Studies have been made on physicochemical and immunochemical properties of macroglobulins, as well as of associated with pregnancy glycoproteins, from human subjects, mammals, birds, fishes and invertebrates. It was shown that these proteins exhibit similar composition, structure and capacity to bind proteinases inhibiting the latter. Using immunochemical methods, reactions of antigenic identity of these proteins were investigated. A hypothesis of evolutionary formation of macroglobulin family is discussed.

Animals↗
PubMedDate not supplied

[Human alpha 2-macroglobulin and its analogs in animals].

Biochemical and immunochemical properties of human alpha 2-macroglobulin and its analogues from cattle, horse, rabbit, guinea pig, rat, mouse, hen and perch have been investigated. It was found that all analogues have the identical molecular mass and structure, being different in their isoelectric point and carbohydrate composition. It was shown that some antigenic properties of macroglobulins remained constant during evolution, whereas other ones were strictly differentiated at the level of families and species. These data allow to classify macroglobulins as proteins which appeared in vertebrates at early stages of evolution revealing only relatively slight changes during the latter.

Animals↗
PubMedDate not supplied

[Changes in the alpha-macroglobulins during evolution].

It has been demonstrated that antigenic properties of alpha-macroglobulins from 6 species of vertebrate and invertebrate animals are rather similar. All proteins consist of identical subunits which are associated by covalent and noncovalent bonds. All of them are presented by glycoproteins and exhibit the capacity to bind proteinases, as well as the capacity to inhibit the latter with respect to protein and low-molecular synthetic substrates.

Animals↗
PubMedDate not supplied

[Comparative characteristics of the vitreous body proteins in vertebrates].

Using disc-electrophoresis in polyacrylamide gel and immunochemical methods, studies have been made on proteins from the vitreous body of mammals (albino mouse, rat, guinea pig, pig, dog, cat), birds (hen), amphibians (the frog Rana ridibunda) and fish (the perch Perca fluviatilis). It was found that vitreous body proteins in man and animals include both the specific proteins and those of the blood serum. During evolution, specific antigens of the vitreous body attained strict species specificity, although some of them preserved the initial properties.

Animals↗
PubMedDate not supplied

[A comparative study of pregnancy-associated protein A and its analogs in animals].

Glycoproteins similar in composition, structure, and functions were isolated from the blood serum of pregnant women, cows, dogs, and rats. They consist of four identical subunits, which form dimers due to covalent bonds, while dimers form tetramers due to hydrogen bonds. All these proteins are non-specific inhibitors of proteases and bind these enzymes in the same way as alpha-macroglobulins do, by capture in a "trap". Furthermore, they are capable of binding and transporting various cytokines. The results obtained indicate that these proteins belong to the family of macroglobulins.

Affinity Labels↗
PubMedDate not supplied

[A comparative study of the physicochemical and antigenic properties of human and animal albumins].

Studies have been made on physico-chemical and antigenic properties of albumins from man, mammals, birds, insects, amphibians, worms, fishes and crustaceans. It was found that all the animals contain structurally identical proteins with similar physico-chemical properties. At the same time, the level of antigenic identity of the proteins decreases in the following order: type, genus, family, species.

Amphibians↗