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V Goyal

Publications and source records attributed to V Goyal.

At least 37 records · Page 2Linked to original sources
PubMed1997

New technique using temporary balloon occlusion for transcatheter closure of patent ductus arteriosus with Gianturco coils.

We describe our early experience with a new technique involving temporary balloon occlusion for transcatheter closure of patent ductus arteriosus (PDA) using single or multiple Gianturco coils. Coil occlusion was attempted in 21 patients of median age 3 (range 1-11) years, and angiographic PDA diameter 3.0 mm +/- 0.87 mm. The inflated balloon of a pulmonary wedge pressure catheter over a transductal wire was used to mechanically hold the first extruded loop of the coil at the pulmonary end of the duct. If a residual shunt persisted after the delivery of the first coil, additional coils were delivered with or without the balloon support. One to nine coils (median 2) of different sizes varying between 3-12 mm diameter and 4-15 cm length were used. Immediate angiographic occlusion rate was 47.6%. However color Doppler (CD) at 24 hours and at 6 weeks revealed complete closure in 66.6% and 80.9%, respectively. Blood transfusion was required in 2 (9.5%) patients. Three out of 56 coils (5.4%) embolized during deployment. The use of balloon occlusion is effective and safe in the treatment of ducti up to 4.7 mm. Residual shunts lend to occlude with time.

Aortography↗
PubMed1995

The hypoglycemic effect of chloroquine.

Ten persons were studied to observe the effect of intravenous administration of chloroquine on serum glucose level. Ten healthy individuals were given 800 mg of chloroquine in three hours infusion. There was a significant (p = 0.001) fall of 25.86 per cent of initial blood glucose level in test group, while it was only 10.47 per cent in control group. Therefore, it is emphasized that seriously III patients and those who are prore to hypoglycemia should be carefully monitored when giving IV chlorquine.

Adult↗
PubMed1994

Transient myocardial dysfunction in a patient with subarachnoid haemorrhage.

We report a patient of subarachnoid haemorrhage who presented with severe left ventricular dysfunction and marked electrocardiographic changes indistinguishable from acute myocardial infarction. Coronary arteriography showed normal anatomy and the ventricular regional wall motion abnormalities recovered spontaneously after 3 weeks. The implications of this association are discussed.

Coronary Angiography↗
PubMed1993

Ultrastructure of human dermal mast cells in 29 different lysosomal storage diseases.

The effect of lysosomal storage diseases on the ultrastructure of human mast cells has not previously been reported. Indeed, there has been little published evidence indicating that mast cells contain typical lysosomes. However, mast cell cytoplasmic granules contain hydrolases similar to those found in lysosomes, but which differ from lysosomal hydrolases in exhibiting optimal activity at higher pH. We therefore examined by transmission electron microscopy the dermal mast cells in 58 biopsies of patients exhibiting 1 of 29 different lysosomal storage diseases. We found mast cells containing abnormal lysosomes in 16 of these disorders. In 6 of these 16 diseases, the mast cells' cytoplasmic granules appeared normal. These observations indicate that human mast cells can contain lysosomes, and provide evidence that the enzymes affected by lysosomal storage diseases are active in mast cells.

Biopsy↗
PubMed1992

Storage of glycoprotein in NCTR-Balb/C mouse. Lectin histochemistry, and biochemical studies.

A strain of Balb/C mice carrying a lysosomal storage disorder exhibits metabolic and phenotypic abnormalities similar to patients with sphingomyelin-cholesterol lipidoses type II (i.e., Niemann-Pick C and D). Their foamy cells, which belong to the reticuloendothelial system, stained intensely by periodate-Schiff (PAS) reagent and were resistant to predigestion with diastase. To identify the chemical nature of the PAS-positive storage material, we applied lectin histochemistry and biochemical methods. Paraffin embedded sections, and delipidated frozen tissue sections, were treated with biotinylated lectins and localized with avidin-biotin-peroxidase complex. Araldite-embedded semithin sections were incubated with biotinylated lectins followed by avidin-gold and were enhanced with silver. By both histochemical methods the affected foamy cells stained positively as follows: Concanavalia ensiformis agglutinin, Datura stramonium agglutinin, Griffonia simplicifolia-I, Lens culinaris agglutinin, peanut agglutinin, Ricinus communis agglutinin-I, wheat germ agglutinin (WGA), and succinylated-WGA. Biochemical analysis of liver extracts complemented the histochemical data and demonstrated accumulation of glycoproteins containing polylactosaminoglycans in affected mice. Our findings indicate that the storage material in NCTR-Balb/C mice is heterogeneous. The lipids that are extracted by organic solvents during the histologic preparations mask the occurrence of polylactosaminoglycan containing glycoproteins in native frozen sections.

Animals↗
PubMed1990

Increased blood loss with in situ bypass.

This study uses perioperative hematocrit determinations to quantitatively evaluate blood loss in patients undergoing either in situ (n = 37) or reverse vein technique (n = 44) for femorodistal popliteal or proximal tibial/peroneal reconstruction. The median drop in hematocrit was significantly greater on the fourth postoperative day in the in situ group as compared with the reverse vein group. The median drop in hematocrit was 8.8 +/- 4.2 per cent in the in situ group as compared with 4.8 +/- 4.1 per cent in the reverse vein group (P less than 0.0005). Blood transfusions were required in 11 of 37 patients (30%) in the in situ group as compared with five of 44 patients (11%) in the reverse vein group (P less than 0.05). Despite limitations of a retrospective study, our data indicate that there is greater blood loss with in situ technique as compared with reverse vein technique for femoropopliteal and crural reconstruction.

Aged↗
PubMed1990

Glycoprotein storage in Gaucher disease: lectin histochemistry and biochemical studies.

Lectin histochemical studies were performed on formalin-fixed, frozen, and paraffin-embedded tissue sections from 19 patients with glucosylceramide lipidosis (i.e., Gaucher disease). Eleven different lectins were used to identify the specific carbohydrate residues in the undegraded stored compounds in the cytoplasm of Gaucher cells. In all cases studied, Gaucher cells stained with Concanavalia ensiformis agglutinin, Datura stramonium agglutinin, Lens culinaris, Ricinus communis agglutinin-I, and wheat germ agglutinin. These results demonstrated common carbohydrate residues in the undegraded material stored within Gaucher cells and indicated the presence of fucosylated N-linked complex oligosaccharides, and glycans containing N-acetyllactosamine repeating sequences, as well as nonreducing terminal beta-galactosyl and sialyl residues. In order to confirm these findings using biochemical methods, livers and spleens from Gaucher patients and controls, and from a patient with Niemann-Pick disease type C (included for comparison) were digested with Pronase and the resulting glycopeptides separated by gel filtration into fractions with high and low molecular weight. In the high-molecular-weight fractions from livers of Gaucher patients, the levels of sugars corresponding to N-linked glycans, as measured by gas-liquid chromatography, were elevated over those in controls. In the high-molecular-weight fractions from spleens, the levels of the same sugars were elevated in both Gaucher and Niemann-Pick type C patients. Digestion of the glycopeptides with endo-beta-galactosidase, which specifically cleaves polylactosaminoglycans, showed the presence of material containing N-acetyllactosamine repeating units in Gaucher liver glycopeptide fractions, but not in control and Niemann-Pick type C derived glycopeptide fractions. Our histochemical and biochemical studies demonstrated that in addition to glucosylceramide, affected tissues of patients with Gaucher disease accumulate glycoproteins. This accumulation could not have been predicted on the basis of the primary enzymatic defect.

Carbohydrates↗
PubMed1989

Glycoconjugates of the intestinal epithelium of the domestic fowl (Gallus domesticus): a lectin histochemistry study.

A lectin histochemical study was performed on formalin-fixed paraffin-embedded tissues of duodenum, jejunum, ileum, caecum and colon from six fasted and six non-fasted 8-week-old chickens (Gallus domesticus). The purpose of this study was to identify in situ the pattern of carbohydrate residues present on the luminal surface of the intestinal epithelium. Ten biotinylated lectins with different sugar specificities were used as probes, and avidin-biotin-peroxidase complex (ABC) was used as a 'visualant'. The most significant finding was the binding pattern of Lens culinaris agglutinin to various segments of the intestines. The luminal surface of the small intestinal epithelium did not stain with this lectin. In the colon the luminal surface was lightly stained, while the caecal luminal surface was intensely stained. Throughout the intestine the luminal surface stained with Canavalia ensiformis agglutinin, Ricinus communis agglutinin-I and wheatgerm agglutinin, but it did not stain with Dolichos biflorus agglutinin. These findings indicated that, throughout the intestine, the luminal surface contains glycoconjugates with either N- or O-linked glycoprotein, or both, with terminal non-reducing beta-galactosyl and sialyl residues. Furthermore, the caecal surface is rich in N-linked glycoproteins with an alpha-(1----6)-linked fucosyl residue near the glycosidic linkage. The potential significance of these observations and the role of glycoconjugates in host-parasite interaction (i.e. Eimeria sp. versus Gallus domesticus) are discussed.

Animals↗
PubMed1989

Morphology of leukocytes from cats affected with alpha-mannosidosis and mucopolysaccharidosis VI (MPS VI).

The morphology and ultrastructure of circulating white blood cells from six Persian and from five Russian Blue/Siamese cats deficient in lysosomal activity of alpha-mannosidase and arylsulfatase B, respectively, were studied and compared to cells from corresponding normal and carrier cats. In cats with mannosidosis, light microscopic examination revealed vacuoles in lymphocytes and monocytes, whereas electron microscopic studies demonstrated additional vacuoles in neutrophils, eosinophils, and basophils. In cats with mucopolysaccharidosis VI (MPS VI), vacuoles containing metachromatic granules were observed in lymphocytes, neutrophils, eosinophils, and monocytes. Ultrastructural studies of these cells identified the accumulation of fibrillar material, which often was associated with lamellated membrane structures.

Animals↗
PubMed1988

Lectin histochemistry of gangliosidosis. I. Neural tissue in four mammalian species.

Lectin histochemical studies were performed on paraffin-embedded brain, spinal cord and eye sections of 16 animals from four different species affected with GM1- and GM2-gangliosidosis to identify specific carbohydrate residues in the perikaryon of neurons. We examined tissues from cats, cattle and dogs with GM1-gangliosidosis and from cats, dogs, and swine with GM2-gangliosidosis and compared them to corresponding normal animals. In all but two cases, the neurons stained intensely with Concanavalia ensiformis agglutinin (Con A); in 12 cases they stained with Dolichos biflorus agglutinin; in 10 cases with Ulex europaeus agglutinin-I; in 9 cases with Griffonia simplicifolia-I; and 8 with soybean agglutinin. Neurons from control tissues stained weakly with Con A, but not with any of the other lectins used. Similar staining patterns of neurons were noted in animals affected with the same disorder originating from the same mutant line. These findings highlight the fact that in gangliosidosis, the lectin staining patterns of neurons may be influenced by the deficiency in enzyme activity and by additional unknown but inherited factors.

Animals↗
PubMed1987

Lectin histochemistry of mammalian endothelium.

Lectin-histochemical studies were performed on formalin-fixed, paraffin-embedded tissues from ten mammalian species to demonstrate the pattern of carbohydrate residues in vascular endothelium. Ten different biotinylated lectins were used as probes and avidin-biotin-peroxidase complex (ABC) was used as visualant. Ricinus communis agglutinin-I (RCA-I) and wheat germ agglutinin (WGA) stained vascular endothelium in all species. Peanut agglutinin (PNA) stained vascular endothelium in all species only after preincubation with neuraminidase. Bandeirea simplicifolia agglutinin-I (BS-I) stained vascular endothelium in all species but human, while Ulex europeus agglutinin-I (UEA-I) stained only human endothelium. Individual differences in staining of human vascular endothelium were noted with BS-I and succinylated-WGA (SWGA). Similarly, individual differences in staining of animal vascular endothelium were noted with soybean agglutinin (SBA) after preincubation with neuraminidase. Finally, Concanavalia ensiformis agglutinin (Con A), Dolichos biflorus agglutinin (DBA) and Lens culinaris agglutinin (LCA) did not stain vascular endothelium in any of the species studied.

Animals↗
PubMed1987

The use of avidin-gold complex for light microscopic localization of lectin receptors.

In the present study, we have investigated the use of avidin-gold complex (AG) as a possible cytochemical marker for visualizing and identifying lectin receptors in deparaffinized tissue sections. Monodispersed gold sols of 15 nm average diameter were prepared by sodium citrate reduction. The AG complex was prepared with highly purified egg-white avidin (avidin-D). Deparaffinized sections of cat duodenum were labeled with five different biotinylated lectins, then were washed and stained for 1-2 h with AG. Intensification of the gold staining was achieved by a modification of the silver-enhancement method. For each lectin, the labeling properties of the avidin-gold-silver (AGS) were compared with those of the avidin-biotin-peroxidase (ABC) and the lectin-gold (LG) methods. We found the lectin binding pattern demonstrated by the AG method to be similar to that of the ABC. The AG localization of the carbohydrate residues is more precise, compared to the peroxidase reaction due to lack of diffusion of the gold marker. Labeling with AGS resulted in improved staining over the AG method, similar to the staining intensity of the ABC. In addition, the two-step AG method provided more intense staining than the direct one-step procedure of the lectin-gold labeling. In conclusion, the use of the AGS method for histochemical visualization of lectin receptors requires a simple two-step procedure which allows highly accurate localization of tissue glycoconjugates. It entails using only a single gold-ligand complex applicable to any biotinylated lectin regardless of its biochemical nature.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1986

Histochemical similarities between human and animal globoid cells in Krabbe's disease: a lectin study.

Lectin-histochemical studies were performed on paraffin-embedded brain tissue sections to identify the specific sugar residues of undegraded "stored" substances in the cytoplasm of globoid cells from patients with globoid cell leukodystrophy. We studied brain tissues from six human patients with galactosylceramide lipidosis (i.e., Krabbe's disease) and compared them to brain tissues from animals with a similar enzyme deficiency including seven Twitcher mice, three dogs and two cats. The globoid cells in all 18 cases studied stained with succinylated-wheat germ agglutinin (S-WGA), but did not stain with Dilichos biflorus agglutinin, soybean agglutinin or Ulex europaeus agglutinin-I. Bandeirea simplicifolia agglutinin-I stained the globoid cells in Twitcher mice, dogs and cats but not those in humans. Concanavalia ensiformis agglutinin, wheat germ agglutinin and Ricinus communis agglutinin-I all stained each of the globoid cells in the mouse, dog and cat tissues, but only in some of the human cases. Peanut agglutinin, however, variably stained globoid cells in the mouse and dog cases but not at all in the human and cat cases. These results demonstrate a common terminal carbohydrate residue N-acetyl glucosamine, which binds S-WGA in the undegraded material stored within the globoid cells in galactoceramide lipidosis. These cells also contained various other stored molecules with sugar residues whose nature is determined by species or individually.

Animals↗
PubMed1986

Lectin histochemistry of glycolipid storage diseases on frozen and paraffin-embedded tissue sections.

Lectin histochemical studies were performed on frozen and paraffin-embedded brain tissue sections from six cases of galactosylceramide lipidosis (i.e., globoid cell leukodystrophy, or Krabbe's disease) in Twitcher mice and one case of canine infantile GM1-gangliosidosis. The globoid cells in Krabbe's disease stained with Ricinus communis agglutinin-I (RCA-I), peanut agglutinin (PNA), and Bandeirea simplicifolia agglutinin-I (BS-I) in frozen sections. However, paraffin sections and frozen sections pretreated with chloroform-methanol or xylene, from the same animals, stained with Concanavlia ensiformis agglutinin (ConA), wheat germ agglutinin (WGA), and succinylated-WGA (S-WGA), in addition to staining with RCA-I, PNA, and BS-I. The affected neurons of canine infantile GM1-gangliosidosis stained only with RCA-I in frozen sections. In paraffin sections, however, these cells were negative with RCA-I but positive with BS-I, ConA, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA) and Ulex europaeus agglutinin (UEA-I) in paraffin sections. These results indicate that in paraffin processing of glycolipid storage disease tissue, some lectin receptors are lost and others are unmasked. The retained receptors can be stained with specific lectins and could serve as markers to characterize and differentiate among the various glycolipid storage diseases.

Animals↗