[Frequencies of Y chromosome binary haplogroups in Belarussians].

The compositions and frequencies of Y-chromosome haplogroups identified by genotyping 23 biallelic loci of its nonrecombining region (YAP, 92R7, DYF155S2, 12f2, Tat, M9, M17, M25, M89, M124, M130, M170, M172, M174, M173, M178, M201, M207, M242, M269, P21, P25, and P37) have been determined in a sample of 68 Belarussians. Eleven haplogroups have been found in the Belarussian gene pool (E, F*, G, I, I1b, J2, N3a*, Q*, R1*, R1a1, and R1b3). Haplogroup R1a1 is the most frequent; it includes 46% of all Y chromosomes in this sample. The frequencies of haplogroups I1b and I are 17.6 and 7.3%, respectively. Haplogroup N3a* is the next in frequency. The frequencies of haplogroups E, J2, and R1b3 are 4.4% each; that of R1* is 3%; and those of F*, G, and Q* are 1.5% each.

[Distribution of the HIV-1 resistance-conferring alleles (CCR5delta32, CCR2-64I, and SDF1 3'A) in Russian, Ukrainian, and Belarusian populations]. / Raspredelenie VICH-protektivnykh allelei (CCR5delta32, CCR2-64I i SDF1-3'A) v vyborkakh russkikh, ukrintsev i belorusov.

The frequencies of three alleles, CCR5delta32, CCR2-64I, and SDF1 3'A, known to decrease the risk of AIDS onset and the rate of the disease progression in HIV-infected individuals were determined in three native population samples from Russia, Ukraine, and Belarus. The frequencies of the alleles were 0.15, 0.12, 0.21; 0.12, 0.07, 0.20; and 0.12, 0.08, 0.26 for Russians, Ukrainians, and Belarussians, respectively. The proportion of the individuals without any of three protective alleles among Russians, Ukrainians, and Belarussians constituted 49, 65, and 61%, respectively. The genotype frequencies for the three loci studied were in Hardy-Weinberg equilibrium. Based on the three-locus genotype frequencies, the hazard ratios (relative hazards, RH) of AIDS onset in HIV-infected individuals in each sample were calculated as ranging from 0.79 to 0.88. In the samples of Eastern Slavs analyzed the estimated frequencies of the AIDS-protective alleles tested, as well as the frequencies of the corresponding genotypes and the relative hazards of AIDS onset were within the range of these parameters for the other European populations. The data on the allele frequencies and the relative hazard values in Russians, Ukrainians and Belarussians can be used as the predictors of AIDS onset and progression rate in HIV-1-infected individuals from the populations studied.

[The "major" proteins of the human myocardium in ontogeny]. / Izuchenie "mazhornykh" belkov miokarda cheloveka v ontogeneze.

Two-dimensional electrophoresis according to O'Farrell was used for studying changes in the content of major proteins of human myocardium at various stages of pre- and postnatal development. On the basis of the protein pattern specific of certain stages of myocardium differentiation the degree of development of the human cardiac muscle can be determined. The most pronounced changes in myocardium protein spectra are characteristic of the first half of pregnancy.

[The topographic characteristics and changes in the ontogeny of light-chain myosin in the human myocardium]. / Izuchenie topograficheskikh osobennostei i izmenenii v ontogeneze legkikh tsepei miozina v miokarde cheloveka.

Pattern of myosin light chain in human atrium and ventricles was studied using two-dimensional electrophoresis. Minor fraction was found in ventricles and atria of adult man that coincided in molecular weight, isoelectric point and staining specificity with fetal myosin light chain. The 23 kDa and 24 kDa fractions of auricles were not detected in ventricles.

[The structure of chordin: characteristics of protein and carbohydrate components and their role in antigenicity]. / Struktura khordina: kharakteristika belkovogo i uglevodnogo komponentov i ikh rol' v antigennosti.

Using immobilized monoclonal antibodies, a tissue-specific antigen, chordin, was isolated from cell extracts of giant sturgeon (beluga) notochord. The antigen was further purified by gel filtration through SP-Sephadex (pH 2.1) and gel chromatography on TSK Toyopearl HW-60. Purified chordin preparations contained 40% of protein and 60% of carbohydrates. The predominant polar amino acids were threonine, serine, glycine, asparagine and glutamine (or aspartic and glutamic amino acids). The carbohydrate moiety comprised mannose, fucose, galactose, galactosamine and glucosamine. Treatment of chordin with three enroglycosidases specifically hydrolyzing the carbohydrate chains of proteoglycans did not affect the antigenic properties of chordin or its behaviour on gel filtration. These findings and the fact that 75% of galactosamine was converted to galactosaminite after treatment with alkaline NaBH4 permitted to relate chordin to glycoproteins carrying O-glycosidic carbohydrate-peptide bonds between the N-acetyl-galactosamine and beta-hydroxyamino acid residues. Besides, chordin seems to contain a N-glycosylamide carbohydrate-peptide bond as can be judged from glucosaminite formation after treatment of the antigen with alkaline LiHB4. The changes in the antigenic properties of chordin after its treatment with neuraminidase, pronase, sodium periodate, alkali, alkaline NaBH4 or LiBH4 suggest that the polypeptide moiety of the chordin molecule and, perhaps, the N-acetylgalactosamine within the composition of the carbohydrate-peptide bond are involved in the construction of its most immunogenic determinants (P-determinants).

The absence of type II collagen and changes in proteoglycan structure of hyaline cartilage in a case of Langer-Saldino achondrogenesis.

Structural analysis of hyaline cartilage extracellular matrix components from the ribs and knee joint of a stillborn female with type II achondrogenesis was carried out. The absence of type II collagen, a decrease in the amount of proteoglycans (PG), and structural changes in PG, namely, increased electrophoretic mobility of PG, lower relative content of chondroitin 4-sulfate (Ch4-S), lower molecular weight and decreased total chondroitin sulfate (ChS) sulfation, were detected. Increased amounts of type I and type III collagens, atypical for hyaline cartilage, were revealed. Among the link proteins (LPs), a large protein with a mol. wt. of 48 kDa was predominant. Molecular and cellular mechanisms of the pathogenesis of achondrogenesis ("chondrogenesis imperfecta") are discussed. The data obtained suggest that the primary defect in type II achondrogenesis involves ChS or type II collagen synthesis.

[Molecular heterogeneity of proteoglycan aggregates of human hyalin cartilage in normal conditions and in systemic bone dysplasia]. / Molekuliarnaia geterogennost' komponentov proteoglikanovykh agregatov gialinovogo khriashcha cheloveka v norme i pri sistemnykh kostnykh displaziiakh.

Components of proteoglycan aggregates of human hyalin cartilage were studied under conditions of normal state and in some forms of osteochondrodysplasia. Extraction of uronic acids and protein from the tissue, amount of fractions and electrophoretic mobility of proteoglycan monomers, rations protein/glycosaminoglycans, keratan sulfate/chondroitin sulfate, a level and type of sulfatation as well as molecular mass of chondroitin sulfate, amino acid composition of rod protein, heterogeneity of binding proteins (concerning their isoelectric points and molecular masses) and immunoreactivity of protein moiety in proteoglycan aggregates were studied in rib cartilage, knee joint and ala ossis ilii. Structural parameters of proteoglycan aggregates proved to be dissimilar and depended on cartilage localization and age of the donors. Impairments in the rate of chondroitin sulfate sulfatation were detected in achondrogenesis of the II type and in diastrophic dysplasia; an extraction ability and amount of proteoglycan fractions, relative content of glycosaminoglycans and binding proteins were altered in some other forms of osteochondrodysplasias. Numerous biochemical markers of extracellular matrix deterioration were detected, which are typical for various morphofunctional alterations in hyalin cartilage--hyperproliferative reactions, tissue prematuration, persistence of the embryonal type of metabolism.

[Changes in the protein spectrum of human kidney anlagen]. / Izmenenie belkovogo spektra zachatkov pochki u cheloveka.

Extracts of metanephros were studied using two-dimensional electrophoresis in human embryos at the age of 7 to 21 week of intrauterine development. Electrophoregrams show 160 to 190 protein fractions. Fractions have been identified which corresponded to actin, albumin, alpha-chain of tropomyosin, light chains of myosin. The tropomyosin zone fractions were subject to greatest changes during development. Other zones of the embryonic kidney electrophoretogram displayed, predominantly, quantitative changes of polypeptides.

[Human heart muscle proteins: two-dimensional electrophoretic analysis in embryos]. / Belki serdechnoi myshtsy cheloveka: dvukhmernyi élektroforeticheskianaliz u émbrionov.

Human myocardium proteins synthesized in the course of heart muscle development have been analyzed by two-dimensional electrophoresis. The quantitative change was found in representation of the main retractable proteins in the course of the heart muscle formation (the light myosin chains, tropomyosin, etc.). Four polymorphous variants of myocardium proteins were found, one of which is, possibly connected with the defect in heart development.

Campomelic syndrome: concepts of the bowing and shortening in the lower limbs.

A comprehensive study (bone roentgenography, arteriography, gross dissection, microscopy of the long bones, and biochemical study of proteoglycan-aggregates in the hyaline cartilage) of the lower limbs in a full-term stillborn with the campomelic syndrome was performed. Hyaline cartilage immaturity of the long bones, dysplasia of growth plates, focal shaft dysplasia, and a defective length of the posterior femur and crus muscles were revealed. The genesis of the bowing and shortening of the long bones in the lower limbs is discussed.

[Interaction of glycosaminoglycans with positively charged fluorochromes]. / Vzaimodeistvie glikozaminoglikanov s polozhitel'no zariazhennymi fliuorokrasiteliami.

Interaction of glycosaminoglycans (GAG) with cationic fluorochromes, which are used for binding with DNA, was studied in biological material (urine, extract from hyalin cartilage) obtained from patients with hereditary mucopolysaccharidoses and from healthy persons. Among the four fluorochromes studied in the reactions with standard GAG's, DAPI proved to be the most suitable fluorochrome. Quantitative fluorimetric technique enabled to estimate the GAG concentration and to evaluate the individual content of heparan-SO4 and keratan-SO4 in biological sources. Interaction of DAPI with GAG was electrostatic and depended on stereometry of DAPI-binding sites on the GAG molecule.

[Collagen proteins of human hyaline cartilage in normal states and in various bone dysplasias]. / Izuchenie kollagenovykh belkov gialinovogo khriashcha cheloveka v norme i pri nekotorykh formakh sistemnykh kostnykh displazii.

Using SDS electrophoresis and subsequent densitometry, isolated collagen proteins of infantile rib and knee joint hyaline cartilage were characterized. Both the normal samples and hyaline cartilages of children with osteochondrodysplasias were shown to contain collagens type I and II as well as collagen proteins with Mr 160 (A), 150 (B), 140 (C), 120 (D), 110 (E) and 39 kD (F), whose content in normal samples varied, depending on the donor age. An analysis of normal and pathological samples revealed the following biochemical markers of intensive chondrocyte proliferation: an increased content of collagen proteins A--F and a decreased number of intramolecular cross-links of collagen type II. Conversely, the increased number of intramolecular cross-links in collagen type II and the elevation of the relative content of collagen type I in lethal forms of osteochondrodysplasias and funnel chest may testify to chondrocyte dedifferentiation. It was assumed that collagen proteins D and E correspond to proteins 1 alpha and 2 alpha, whereas proteins A, B, C and F are the products of hydrolysis by pepsin type M of collagen detected previously only in animal cartilages. Mapping of collagen type II CNBr-peptides and electron microscopic analysis of its SLS-form were carried out. The experimental results are suggestive of the involvement of collagen proteins in the pathogenesis of human osteochondridysplasias as well as of the pronounced biochemical heterogeneity of the disease.

[Heterogeneity of binding proteins of proteoglycan aggregates from human hyaline cartilage under normal conditions and in systemic bone dysplasias]. / Geterogennost' sviazyvaiushchikh belkov proteoglikanovykh agregatov gialinovogo khriashcha cheloveka v norme i pri sistemnykh kostnykh displaziiakh.

Using SDS electrophoresis and subsequent densitometry, the link proteins (LP) of proteoglycan aggregates of the knee joint hyaline cartilage, rib and/or the iliac crest cartilage were investigated. Both the control and experimental samples (n = 9 and n = 16, respectively) contained three LP with Mr 48.0 (LP-1), 44.0 (LP-2) and 41.5 KD (LP-3); however, their ratio varied within very broad limits. Low molecular weight forms of LP were also observed in the infundibulum-like deformation of the thorax. The considerable decrease of LP-3 and the elevated content of LP-2 were observed in lethal osteochondrodysplasias, which probably reflects the genetically determined disorder of limb morphogenesis, eventually resulting in the maintenance of embryonic ratio of LP. Almost all the preparations contained a protein with Mr 52 KD that was previously unknown for the LP system. The content of this protein was the highest in the exostose cartilage and in newborns. Possible mechanisms of LP heterogeneity and the significance of this parameter for the regulation of chondrogenesis and realization of certain physical properties of cartilages from different parts of the skeleton are discussed.

[Components of proteoglycan aggregates in human hyaline cartilage]. / Izuchenie komponentov proteoglikanovykh agregatov gialinovogo khriashcha cheloveka.

The components of proteoglycan aggregates--proteoglycan subunits and link proteins from articular cartilage extracts of newborns--were isolated and purified. The content of extracted uronic acids and protein per 1 g of wet weight was 4.77 +/- 0.52 and 3.19 +/- 0.14 mg, respectively. The components of proteoglycan aggregates were isolated and purified by caesium chloride density gradient ultracentrifugation under association and dissociation conditions, as well as by gel filtration on Sephacryl S-200. The uronic acids/protein ratio for proteoglycan subunits was equal to 59.13 +/- 10.19, their relative electrophoretic mobility was 0.54 +/- 0.01 (the mobility of the chondroitin sulfate was taken for unity). The IR spectra of proteoglycan subunits were characterized. Three link proteins with Mr 48 000, 44 000 and 41 500 were isolated from proteoglycan aggregates and characterized. The protein with Mr 48 000 was predominant.