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Biomedical subjects

S Braga

Publications and source records attributed to S Braga.

44 records · Page 3Linked to original sources
PubMed1985

[Genetic heterogeneity and pathology of congenital nephrotic syndrome and its significance in prenatal diagnosis].

Familial occurrence of congenital nephrotic syndrome (CN) has been most extensively studied in Finland where it is known to be inherited as an autosomal recessive disease. In this Finnish type of congenital nephrotic syndrome (CNF) prenatal diagnosis by alphafetoprotein (AFP) determination in the amniotic fluid has been reported to be conclusive. Within the last six years we observed 10 cases of CN occurring in 5 families. In all patients renal histology has been studied. Although each family presented a different type of CN, the appearance within the same sibship was always identical.

Adult↗
PubMed1982

Clinical and cytogenetic spectrum of duplication 3p.

An eight months old child with duplication 3p (p21 leads to 3pter) [karyotype: 46,XX,-6,+t(3;6)(6pter leads to 6q27::3p21 leads to 3pter)] resulting from a maternal balanced translocation (3;6) is described. The major clinical findings include congenital heart defects (several ventricular septal defects, atrial septal defect, patent ductus arteriosus, and double outlet right ventricle), and multiple dysmorphic features, such as brachycephaly, frontal bossing, square shaped face, hypertelorism, epicanthus, short prominent philtrum, and short neck. The motor development is retarded. The size of the duplicated segment of 3p is compared to 12 cases reported in the literature. Although the size of the duplicated segment differs in most of the patients, all show a similar pattern of developmental defects. It appears that the region 3p25 leads to 3pter is responsible for the phenotype of duplication 3p syndrome.

Chromosome Aberrations↗
PubMed1981

Congenital osteogenesis imperfecta in three sibs.

Three sibs of a Turkish family were affected with lethal congenital osteogenesis imperfecta (OI). The disease was characterized by extremely fragile bones and crumpled femora, but in contrast to reported cases of OI type II, relatively normal ribs with only few fractures. The children affected died shortly after birth. Although their parents both came from the same small village in Turkey, consanguinity could not be demonstrated. Our observations support that this disorder is inherited in an autosomal recessive mode. We consider the possibility that these patients represent either a new subgroup of OI type II (milder, although still lethal) or of type III (more severe).

Female↗
PubMed1981

Muscle ribosome detachment factor. Does it have a role in the pathogenesis of Duchenne muscular dystrophy?

A protein that detaches ribosomes from rough microsomal membranes ("detachment factor") (DF) was isolated from the cytosol fraction of rat and human muscle. The procedure of isolation included differential centrifugation, precipitation with ammonium sulfate and column chromatography with Sephadex G-100. The protein which is not completely homogenous, has a molecular weight of 50,000-60,000 daltons, is heat labile and has an optimum pH at 7.4-7.6. The DF activity of the protein is inhibited by soybean trypsin inhibitor (73%), pepstatin (67%), and leupeptin (42%), although no proteolysis could be measured. The DF activity was tested on muscle samples (rough microsomal membranes) obtained from Duchenne muscular dystrophy (DMD) patients (7 cases) and normal controls (16 cases). The yield of membrane bound ribosomes (MBR) obtained from muscle samples of DMD patients by extraction with DF is 5-fold higher than from muscle samples of normal controls. The difference in MBR yield is not related to the type of DF. Similar values for MBR were obtained with rat and human (normal and dystrophic) DF. Ribosomal protein synthesis (RPS) with ribosomes extracted by DF showed values similar to the RPS of detergent extracted ribosomes. Our findings suggest the observed increase in membrane bound ribosomes in DMD probably results from increased levels of mRNAs coding for membrane and secretory proteins such as collagen.

Amino Acids↗