Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

PAS genes are required for peroxisome biogenesis in the yeast S. cerevisiae. Here we describe the cloning, sequencing, and characterization of the PAS1 gene. Its gene product, Pas1p, has been identified as a rather hydrophilic 117 kd polypeptide. The predicted Pas1p sequence contains two putative ATP-binding sites and reveals a structural relationship to three other groups of proteins associated with different biological processes such as vesicle-mediated protein transport (NSF and Sec18p), control of cell cycle (Cdc48p, VCP, and p97-ATPase), and modulation of gene expression of the human immunodeficiency virus (TBP-1). The proteins share a highly conserved domain of about 185 amino acids including a consensus sequence for ATP binding. We suggest that these proteins are members of a novel family of putative ATPases and may be descendants of one common ancestor.
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PMID:PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases. 182 27

Serial transverse sections of m. vastus lateralis biopsies from six healthy men were reacted: (1) for myofibrillar adenosine triphosphatase (mATPase) to identify fibre types; or, (2) with alpha-amylase, periodic acid-Schiff (alpha PAS) to visualize capillaries. Sections were also processed with a new histochemical method for identification of fibre types and capillaries on the same skeletal muscle slice (mATPase/alpha PAS). Fibre type composition using either method was 41% type I, 37% type IIA and 22% type IIB. Types I, IIA and IIB least diameter areas (mean +/- SE, micron2) were similar in sections processed for mATPase/alpha PAS or mATPase (3976 +/- 338, 5187 +/- 373 and 4389 +/- 514 vs. 4092 +/- 345, 5100 +/- 360 and 4289 +/- 474, respectively). The number of capillaries per mm2 and per fibre did not differ in sections processed using the alpha PAS (315 +/- 29 and 1.48 +/- 0.12) or mATPase/alpha PAS (317 +/- 25 and 1.43 +/- 0.10) method. The number of capillaries was greater (P less than 0.05) around types I or IIA than type IIB fibres whether a section was processed for mATPase/alpha PAS (4.5 +/- 0.2 or 4.6 +/- 0.2 vs. 3.4 +/- 0.3) or when fibre profiles of serial sections reacted for mATPase or alpha PAS were 'matched' (4.5 +/- 0.2 or 4.4 +/- 0.2 vs. 3.4 +/- 0.3). The results indicate that histochemical and morphometric measures can be made on the same transverse section using the new method with substantial savings of time, cost and energy.
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PMID:Histochemical demonstration of skeletal muscle fibre types and capillaries on the same transverse section. 182 95

In 21 sudden and unexpected deaths of infants and three young children who died unexpectedly with known pathological conditions the authors examined by histochemical methods the atrioventricular node and bundle of His. The activity of "glycogen dependent" phosphorylase and the PAS reaction was in the majority week or negative. The probable cause of this finding is hypoxia, although other influences cannot be ruled out (inflammation, hypotrophy, autolysis). The activities of other enzymes (oxido-reductases ATPase, acetylcholine sterase, non-specific 1-naphtyl acetate esterase and acid phosphatase) were similar as in the normal conduction system.
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PMID:[Findings in the atrioventricular node and the bundle of His in sudden and unexpected death in childhood. Histochemical study]. 192 9

Enzyme histochemistry was assessed in semi-thin glycolmethacrylate sections after 100 mg/kg 2-bromoethanamine (BEA) hydrobromide had been given ip to male Wistar rats to induce renal papillary necrosis. Changes in the proximal tubular marker enzymes alkaline phosphatase (Alk Phos), gamma-glutamytranspeptidase (GGT) and adenosine triphosphatase (ATPase) were not apparent before 8 hr, but there was a progressive loss up to 144 hr. The proteinaceous PAS-positive casts in the loops of Henle and the collecting ducts stained for Alk Phos and GGT (from 12 hr) and for ATPase (from 18 hr). Acid phosphatase (Acid Phos) staining was increased in the proximal tubule lysosomes from 18 hr. There was a marked increase in Alk Phos in all hyperplastic upper urothelial cells from 8 to 24 hr, and a mosaic of staining remained in the pelvis adjacent to the necrosed papilla at 144 hr. At 12 hr, there was an increase in the staining of the pelvic, ureter and bladder vascular endothelial ATPase, the intensity and area of which increased progressively from 18 hr and almost occluded the capillary lumens in the worst affected areas by 144 hr. These data show several distinct series of pathological changes after the administration of BEA. The subtle degenerative changes in the proximal tubule followed the papillary lesion, but exfoliated brush border and proximal tubular cells were important components of the protein casts in the distal nephron. Similarly, the intense Alk Phos staining in the hyperplastic regions of the upper urothelium and the increased pelvic, ureteric and bladder endothelial ATPase staining suggested they develop as a consequence of the papillary lesion.
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PMID:Enzyme histochemical changes in an acutely induced renal papillary necrosis. 197

We studied the metabolism of the conduction system and the working myocardium in diabetic rat hearts by enzyme histochemistry. The experiment was performed three weeks following the administration of streptozotocin (65 mg/kg) to male Wistar rats. The hearts were quickly excised and tissue was frozen immediately by immersion in isopentane at -30 degrees C and cut into 16 microns thick sections in a cryostat. The PAS positive reaction was increased in the conduction system compared to the working myocardium in control rats. In diabetic rat hearts, these reactions in the working myocardium and the conduction system were strongly increased compared to control hearts. Several enzyme activities, such as phosphofructokinase, pyruvate dehydrogenase, glucose-6-phosphate dehydrogenase, Na-K ATPase, were reduced in both the working myocardium and conduction system of diabetic rat hearts. These results suggest that the changes in metabolic condition also exist in the conduction system of the diabetic rat hearts as well as the working myocardium.
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PMID:Histochemical studies on the conduction system of diabetic rat hearts. 216 29

The Escherichia coli primosome is a mobile multiprotein DNA replication-priming apparatus that assembles at a specific site (termed a primosome assembly site (PAS] on single-stranded DNA-binding protein-coated single-stranded DNA. The PRI A protein (factor Y, protein n') is a PAS sequence-specific (d)ATPase as well as a DNA helicase and is believed to direct the assembly of the primosome at a PAS. In this report, the PRI A DNA helicase reaction is dissected in vitro, by use of a strand displacement assay, into three steps with distinct ATP requirements. First, the PRI A protein gains entry to the DNA via an ATP-independent, PAS sequence-specific binding event. Second, the PRI A protein translocates along the single-stranded DNA in the 3'----5' direction at a maximal rate of 90 nucleotides/s. DNA translocation requires ATP hydrolysis. The ATP concentration required to support half of the maximal translocation rate is 100 microM, which is identical to the Km for ATP of the PRI A protein DNA-dependent ATPase activity. Finally, the PRI A protein unwinds duplex DNA. The ATP concentration required for duplex DNA unwinding depends upon the length of the duplex region to be unwound. Displacement of a 24-nucleotide long oligomer required no more ATP than that required for the translocation of PRI A protein along single-stranded DNA, whereas displacement of a 390-nucleotide long DNA fragment required a 10-fold higher concentration of ATP than that required for oligomer displacement.
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PMID:Differential ATP requirements distinguish the DNA translocation and DNA unwinding activities of the Escherichia coli PRI A protein. 217 Mar 65

This experiment investigated the reinnervation of the canine posterior cricoarytenoid (PCA) muscle with preganglionic neurons of the sympathetic nervous system. Six dogs had their right recurrent laryngeal nerve (RLN) sectioned. Four of these dogs had the sympathetic cervical trunk (SCT) implanted into the right PCA muscle, and the two remaining dogs served as denervated controls. Four months later all dogs underwent videolaryngoscopy, electromyography, and electrical stimulation of the SCT. The PCA muscles were excised, sectioned, and stained for glycogen and ATPase. All four experimental PCA muscles demonstrated electrically evoked abduction and tonic electromyographic activity. In two of the specimens, staining (ATPase and PAS) revealed areas of reinnervation with fiber type grouping and glycogen depletion. These results are consistent with the successful reinnervation of the PCA muscle. Further refinement of this technique could be of benefit to patients with bilateral vocal cord paralysis.
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PMID:Reinnervation of the canine posterior cricoarytenoid muscle with sympathetic preganglionic neurons. 231 Jan 30

A modified ATPase method for the simultaneous demonstration of capillaries and fiber types in skeletal muscle is presented. Muscle biopsies were obtained from mice, hamsters, rats, cats, and dogs, quick frozen, and sectioned at 8 microns in a cryostat. The frozen slides were fixed in a neutral formalin solution at 4 C for 5 min, and then incubated at 37 C for 1 hr in a medium containing ATP, Pb2+, and Ca2+ in a tris-maleate buffer (pH 7.2). Dilute (NH4)2S was used as a developer. To test the reliability of the proposed method, serial sections of each biopsy were stained separately for capillaries (amylase-PAS method) and for fiber types by a standard myosin ATPase (m-ATPase) method. Fiber type percent and capillary parameters were determined for each biopsy. No difference in results was observed for parameters determined using the modified ATPase method compared to the standard capillary and fiber type staining methods. This modified technique is therefore suitable for the simultaneous demonstration of capillaries and fiber types in skeletal muscle.
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PMID:A histochemical method for the simultaneous demonstration of capillaries and fiber type in skeletal muscle. 244 Jan 55

A first Japanese case of an adult polysaccharide storage myopathy (APSM) was reported. A 30-year-old Japanese male was admitted because of weakness of the lower limbs. The onset of the symptoms was at the age of 23. Neurologically he had moderate weakness of proximal limb muscles involving the lower limbs more than the upper and slightly decreased vibratory sense in the feet. His gait was waddling. The following laboratory values were obtained; SGOT 45 I.U., SGPT 83 I.U., CPK 218 I.U., UA 8.3 mg/dl. Ischemic exercise test of the forearm showed a normal rise of venous lactate. EMG revealed a mixture of myopathic and mild neurogenic patterns characterized by motor units of short duration and low amplitude with intermittent high amplitude potentials, fibrillation and fasciculation. There were also prominent myotonic discharges without clinical myotonia. MCV was normal, however sural nerve SCV was slightly slow (lt. 36/m, rt. 38 m/s). Muscle biopsy revealed vacuolar myopathy. Most vacuoles contained basophilic, PAS-positive, diastase-resistant and Lugol's iodine-negative material. With ATPase staining there was type 1 fiber predominance (84%), but the vacuoles were predominantly seen in type 2A fiber. In ultrastructural study, the storage material was located under the sarcolemma and in the areas of the intermyofibrillar network. No delimiting membranes were seen. At higher magnification, these masses were consisted of filaments. Therefore the storage material was considered to be unusual polysaccharide. Glycogen storage disease was suspected, however, biochemical study of the muscle specimen disclosed no enzymatic defect including branching enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Adult polysaccharide storage myopathy]. 269 Nov 65

Since it has been demonstrated that endurance-trained cyclists are able to synthesize glycogen during mild exercise, glycogen synthesis was investigated in non-endurance-trained males and females as well. Seven males and nine females exercised on a cycle ergometer to deplete muscle glycogen. After the exhaustive exercise and taking a muscle biopsy, the males either exercised 2.5 h at 40% of maximal work load (trial A) or rested for 2.5 h (trial B). In both trials the subjects drank a 25% maltodextrin-fructose solution. After 2.5 h of exercise or rest, a second muscle biopsy was taken for determination of glycogen and for histochemistry (ATPase and PAS). In the females glycogen synthesis was only studied during 2.5 h rest, after prior glycogen depletion. In the male subjects, during mild exercise with carbohydrate feeding muscle glycogen did not increase. During rest muscle glycogen increased in the males from 123 +/- 49 mmol/kg DW at exhaustion to 229 +/- 70 mmol/kg DW (P less than 0.001), resulting in a net increase of 42 mmol/kg DW/h. Glycogen synthesis during rest occurred both in type I and type II fibers. In the females, during 2.5 h of rest, muscle glycogen increased from 130 +/- 56 mmol/kg DW at exhaustion to 224 +/- 51 mmol/kg DW, resulting in a net increase of 37 mmol/kg DW/h. The results demonstrate that glycogen synthesis during mild exercise does not occur in non-endurance-trained athletes, whereas in the resting state glycogen synthesis in non-endurance-trained males is not different from endurance-trained cyclists. In addition, glycogen synthesis during rest is similar in males and females.
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PMID:Glycogen synthesis during exercise and rest with carbohydrate feeding in males and females. 274 28


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