This paper offers a quantitative evaluation of the scientific information produced in Brazil on several endemic diseases: Chagas' disease, schistosomiasis, leishmaniasis, leprosy, malaria and filariasis. The source of data was the Index Medicus Latino Americano (IMLA), and the published scientific information was analyzed in general and specifically, by type of disease and year of publication. The indexed production of articles on the material of the Latin American countries as a whole increased from 3,506 articles in 1978 to 5,528 in 1982 (for an increase of 52.7%), whereas that of Brazil alone rose from 1,781 to 2,531 (an increase of 42.1%) during the same period. The output of articles on endemic diseases totaled 703 papers (6.3% of the total indexed production). Of this total, 441 (62.7%) was on applied research and 262 (37.3%) were on basic research, and these proportions held relatively constant. Chagas' disease and schistosomiasis accounted for 75.2% of that total over the period considered. The production of papers on the diseases of interest grew 79.2%, at the same rate as that of all biomedical information published in Brazil over the period. An equilibrium was reached between the numbers of basic and applied papers. The analysis also identified the core of Brazilian periodicals that most frequently publish information on those endemics. It was also found that a large proportion of articles by Brazilian authors are published in journals of international circulation, and the foreign journals that publish papers by researchers in Brazil were identified.

Brazil↗

PubMed1985

Binding and degradation of proteoglycans by cultured arterial smooth muscle cells. II. Binding sites of proteoglycans on the cell surface.

Exogenous proteoglycans stained for electron microscopy with colloidal gold and/or cuprolinic blue bind to the surface of cultured arterial smooth muscle cells at two different sites. (I) About 20% of the proteoglycans adsorbed to the cells from the culture medium interact as monomeric and multimeric proteoglycans with smooth or coated membrane areas. (II) The bulk of exogenous proteoglycans exhibits high affinity binding to cell membrane-associated 10 nm fibrils containing or being closely associated with fibronectin and to collagen. It is suggested that the self association of proteoglycans and their binding to the cell membrane and to cell surface-associated fibronectin and collagen are important for maintaining an appropriate micro-environment for the cultured cells.

Arteries↗

PubMed1985

[Perforation by a foreign body in esophagus duplication in an infant].

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Esophageal Perforation↗

PubMed1984

DNA sequence comparison of the regulatory signals at the 5' end of the mouse and chick alpha 2 type I collagen genes.

We have isolated a DNA segment that contains the presumptive transcriptional and translational control signals located at the 5' end of the mouse alpha 2(I) collagen gene. The DNA sequence of the first exon of this gene and of 400 base pairs preceding the start of transcription was compared with an analogous sequence in the chick alpha 2(I) collagen gene. The most striking similarity is a block of 68 nucleotides surrounding the translation initiation site which is perfectly conserved except for four contiguous nucleotides in the middle of the conserved sequence. These four nonconserved bases lie between the arms of a perfect inverted repeat with nine nucleotides in each arm. The very high degree of sequence conservation of this segment suggests that both the inverted repeat and the rest of the perfectly conserved sequence have a regulatory role, possibly in translation. The segment preceding the transcription start shows blocks of similarities interspersed with dissimilar sequences. The conserved sequences include the TATA box, CAT box, a G/C rich sequence around -110, a segment that contains almost exclusively pyrimidines on one strand and is sensitive to endonuclease S1 in both promoters, and several other segments that extend to 350 base pairs preceding the start of transcription. Although the distances between these regions of similarity and the TATA box are not the same in the two promoters, we believe the conserved sequences play a role in the transcriptional activation of this gene.

Amino Acid Sequence↗

PubMed1984

Influence of muzolimine on arterial wall elastin.

Muzolimine, 3-amino-1-(3,4-dichloro-alpha-methylbenzyl)-2- pyrazolin -5-one, an antihypertensive and diuretic drug, accumulates in the arterial tissue of rats and dogs after oral administration. Two weeks after the administration of 3 mg [14C]muzolimine, the aorta of rats contained 60-300 times more 14C-radioactivity/weight unit than the skin or tail tendon. The 14C-radioactivity was exclusively bound to the isolated aortic elastin and corresponded to 0.04% of the applied muzolimine dose. Up to ca 250 ng bound muzolimine/mg elastin was found in the aorta of dogs treated with non-labelled muzolimine for 52 weeks. The elastin-bound [14C]muzolimine was not extractable by organic solvents or by weak acids or bases but was released in a soluble form by pancreatic elastase and extracted from the elastase digest by dichloromethane. In the dichloromethane extract muzolimine was detected by HPLC and HPTLC, and was identified by mass spectrometry. Muzolimine pretreatment of rats for 2 months did not influence the elastin content of arterial tissue or [3H]glycine incorporation into aortic elastin under organ culture conditions, but after labelling the elastin with [4,5-3H]lysine, the [3H]desmosine and [3H]-isodesmosine isolated from the elastin of muzolimine-pretreated rats and incorporated under organ culture conditions was lower than that of control animals. In addition, aortic elastin of rats pretreated for 2 months with 800 ppm muzolimine in the diet was more resistant to elastase degradation. This effect might give some implications for muzolimine in the therapy of cardiovascular disorders with impaired arterial elastin metabolism.

Animals↗

PubMed1984

A sequence conserved in both the chicken and mouse alpha 2(I) collagen promoter contains sites sensitive to S1 nuclease.

We have examined the S1 nuclease sensitivity in the promoter of both the chicken and mouse alpha 2(I) collagen genes. When these DNAs are introduced into supercoiled plasmids and digested with S1 nuclease, a discrete region containing one or more cleavages is found in each promoter. These S1 cleavage sites were mapped by the distance of the S1 site from known restriction enzyme cleavage sites. In the chicken gene, the S1-sensitive segment is located 180 to 200 base pairs preceding the start site of transcription, whereas in the mouse promoter it is between -145 to -165 base pairs. This site in the chicken promoter maps to the segment that has previously been shown to be S1 and DNase I hypersensitive in chromatin. Although these S1 sites are found at different distances from the start site of transcription in the two promoters, the sequences at these sites are strongly conserved between the two species. Each sequence consists of an identical tandem repeat containing a short palindrome within each repeat. Since the DNA sequence does not exhibit the features that would favor either a left-handed Z-DNA configuration or a cruciform structure, an alternative model is discussed that could account for the S1 sensitivity of these sequences. The conservation of these sequences and their S1 sensitivity suggests they play a role in the activation or regulation of the alpha 2(I) collagen gene promoters.

Animals↗

PubMed1984

[Formation of secretory immunoglobin by the hepatic clearance mechanism].

In patients suffering predominantly from several types of dermatosis as well as from cholecystitis and cholelithiasis relationships to the formation of secretory immunoglobulin by the hepatic clearance mechanism have been investigated. In the duodenal content and in operatively yielded gall-bladder bile, immunoglobulins, complement C3, and albumin were detected. The amount of immunoglobulins and of albumin in the duodenal content was substantially increased if infectious germs could be detected in the stomach content.

Bile↗

PubMed1984

Differentiation of a human monocyte-like cell line by (2'-5') oligoisoadenylate.

Treatment of a human monocyte-like cell line (U-937) by (2'-5')ApApA, the 5' dephosphorylated product of (2'-5')oligo-isoadenylate [oligo(A)] synthetase, an interferon-induced enzyme, was able to induce differentiation, mimicking the effect of interferon treatment. Treatment of U-937 cells with (2'-5')ApApA resulted in morphologic changes, new (monocyte-associated) membrane antigen expression, and acquisition of the capacity to mediate antibody-dependent cellular cytotoxicity (ADCC). (2'-5')ApA and (3'-5')ApApA were without effect. A myeloid cell line (HL-60) which differentiates in response to other agents, but not to alpha-interferon, was not able to differentiate in response to (2'-5')ApApA, despite the ability of interferon to induce (2'-5')oligo (A) synthetase.

Antibody-Dependent Cell Cytotoxicity↗

PubMed1984

Effects of As-deficiency on skeletal muscle, myocardium and liver. A histochemical and ultrastructural study.

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Animals↗

PubMed1984

Formation of Elemental Sulfur by Chlorella fusca during Growth on l-Cysteine Ethylester.

During growth on l-cysteine ethylester, Chlorella fusca (211-8b) accumulated a substance which contained bound sulfide, which could be liberated by reduction with dithioerythritol (DTE) as inorganic sulfide. This substance was extracted with hot methanol and purified by thin layer chromatography. This substance liberated free sulfide when incubated with mono- and dithiols, and thiocyanate was formed after heating with KCN. The isolated substance cochromatographed with authentic sulfur flower using different solvent systems for thin layer chromatography, high pressure liquid chromatography, and the identical spectrum with a relative lambda(max) at 263 nm was found. The chemical structure was confirmed by mass spectrometry showing a molecular weight of 256 m/e for the S(8) configuration. No labeled elemental sulfur was detected when the cells were grown on [(35)S]sulfate and l-cysteine ethylester indicating the origin of elemental sulfur from l-cysteine ethylester. C. fusca seems to have enzymes for the metabolism of elemental sulfur, since it disappeared after prolonged growth into the stationary phase. Cysteine was formed from O-acetyl-l-serine and elemental sulfur in the presence of thiol groups and purified cysteine synthase from spinach or Chlorella.

Journal Article↗

PubMed1984

Event-related potential studies of cerebral specialization during reading. A comparison of normally hearing and congenitally deaf adults.

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Adult↗

PubMed1984

Characterization of proteoglycans synthesized by cultured arterial smooth muscle cells of the rat.

Arterial smooth muscle cells cultured from rat aorta were labelled with sodium [35S]-sulfate in combination with either [3H]glucosamine or [3H]mannose. The newly synthesized hyaluronate and sulfated proteoglycans obtained from the growth medium (M-PG) and extracted from the cell layer (C-PG) with 4M guanidinium chloride in the presence of proteinase inhibitors were purified by sequential fractionation on Sepharose 4B CL, equilibrium density gradient centrifugation and ion exchange chromatography under dissociative conditions. Gel filtration of M-PG resulted in the separation of free hyaluronate and two size classes of [35S]-proteoglycan populations eluted at Kav 0.15 (fraction M-A) and 0.48 (fraction M-B). On further fractionation M-A dissociated into hyaluronate (Mr 1.6 X 10(6)) and a proteoglycan monomer (M-PG A, Mr 180 000), which contained chondroitin 4-sulfate (Mr 21 000) as the main glycosaminoglycan moiety. The proteoglycan isolated from M-B (M-PG B) was identified as a proteoglycan monomer (Mr 200 000) containing mainly chondroitin sulfate/dermatan sulfate hybrid side chains (Mr 34 000). [3H]Mannose labelling and binding to ConA Sepharose of both M-PG A and B indicated the presence of oligosaccharides of the glycoprotein type. An analogous fractionation of proteoglycans associated with the cell layer yielded two hyaluronate-proteoglycan complexes (C- PreA and C-A). The proteoglycan monomers of these complexes (C-PG PreA and C-PG A) had Mr values of 420 000 and 130 000. A non-complexed proteoglycan monomer C-PG B (Mr 90 000) was also found. All cell layer bound proteoglycans had glycosaminoglycan side chains with Mr approximately 36 000 but the predominant glycosaminoglycan component was either heparan sulfate, chondroitin sulfate or dermatan sulfate. All cell layer bound proteoglycans contained [3H]mannose radioactivity, about 15% of which was bound to ConA Sepharose.

Animals↗

PubMed1984

Processing and transport of lysosomal enzymes in human monocyte line U937.

Precursors of cathepsin D and beta-hexosaminidase synthesized in the U937 monocyte line are processed to mature forms with similar kinetics as in fibroblasts. In U937 cells the processing of the precursor of the beta-chain of beta-hexosaminidase, however, results in a larger fragment that resembles a processing intermediate in fibroblasts. This difference is explained by differences in the equipment of the cells with proteinases, since cross-feeding of the precursors to the cells results in a processing characteristic for the recipient cell type. In sucrose gradients the precursors are found partly in a low- and partly in a high-density region. Mature polypeptides and activity of lysosomal enzymes fractionate mainly in the higher density region. In U937 cells the transport and maturation of endogenous lysosomal enzymes are less sensitive to bases (NH4Cl, chloroquine, tilorone) and to antibody against the mannose 6-phosphate specific receptors than in fibroblasts. A small portion of enzymes released from U937 cells contains the markers recognized by the mannose-6-phosphate specific receptors. U937 cells express these receptors and utilize them for transport of endogenous and exogenous lysosomal enzymes. It appears, however, that a fraction of lysosomal enzymes is transported in U937 cells independent of the mannose-6-phosphate-specific receptors.

Biological Transport↗

PubMed1984

[Hemodynamics and changes in compliance of the extra-thoracic capacity system following administration of prostacyclin (PGI2)].

Hemodynamic effects of prostacyclin (PGI2) given as an intravenous infusion at a rate of 8 ng/kg/min were assessed in 50 patients with coronary artery disease at the time of aortocoronary bypass surgery. 1. During steady-state neuroleptic anesthesia, after sternotomy and pericardiotomy, before cannulation of the aorta and vena cava PGI2 led to the following changes: decreases in mean arterial pressure (-24%), total peripheral resistance (-46%), left ventricular pressure (-12%) and left ventricular end-diastolic pressure (-48%), increases in heart rate (+9%), cardiac output (+41%), stroke volume (+30%) and dp/dtmax (+26%) as well as nonsignificant decreases in right ventricular filling pressure (-13%) and mean pulmonary arterial pressure (-9%) together with an unaltered rate-pressure product. 2. In a randomized double-blind study PGI2 was infused throughout the period from two minutes prior to, until termination of extracorporeal circulation. The effects on compliance of the extrathoracic venous system were analyzed on the basis of changes in venous pressure and oxygenator volume. As compared with controls, patients receiving PGI2 were found to have a significant increase in compliance (.157 ml/mm Hg X kg). Thus, in this setting, PGI2 can affect marked vasodilatation with reductions in peripheral resistance and mean arterial pressure together with increases in cardiac output and heart rate.

Clinical Trials as Topic↗