Methyl 1-(4-chlorobenzyl)-2-(4-methylpiperazin-1-yl)-1H-benzimidazole-5- carboxylate hemihydrate.
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Anti-Infective Agents↗
Biomedical subjects
S Ozcan
Publications and source records attributed to S Ozcan.
Arterial vascularization of the uropygial glands (Gl. uropygialis) in geese (Anser anser) and ducks (Anas platyrhynches).
In the present study, arterial vascularization of the uropygial glands (Gl. uropygialis) of 10 adult geese (Anser anser) and 10 adult ducks (Anas platyrhynches) were studied. Takilon was injected into the median coccygeal arteries of six specimens from each species, and Latex (a natural rubber with ammonia) into those of four specimens. Takilon-injected specimens were corrosion casted, and arteries nourishing the gland were revealed via dissection. Vascularization of the uropygial glands of both the goose and the duck was observed to be the right (a. gl. uropygii dextra), left (a. gl. uropygi sinistra) and ventral (a. gl. uropygi ventralis) glandular uropygial arteries, arising from the median coccygeal (a. coccygea media) artery. Both the right and left glandular uropygial arteries were observed, divided into four branches as follows; muscular ramus (ramus muscularis), medial ramus (ramus medialis), ventral ramus (ramus ventralis) and lateral ramus (ramus lateralis). Of these, as the lateral, medial and ventral branches feed the gland, the muscular branch provides blood for the lateral coccygeal (m. coccygealis lateralis) and levator coccygeal (m. levator coccygealis) muscles, and the skin. Among the arteries mentioned above, anastomosis between the first and the second branches of the right ventral uropygial arteries in the five geese and five ducks was found.
Animals↗
Chemical peritonitis associated with high dialysate acetaldehyde concentrations.
BACKGROUND: During the standard heat sterilization process of lactate-buffered peritoneal dialysis (PD) solutions, glucose degrades to form compounds called glucose degradation products such as acetaldehyde, formaldehyde, or glyoxal. Despite evidence that these products may be responsible for some in vitro cytotoxic effects induced by commercially available PD fluids, data on their acute or chronic effects on the human peritoneum is scarce. SUBJECTS AND METHODS: This case presentation is based on an observation of 21 aseptic peritonitis cases of unknown aetiology. All cases appeared within one month in a university hospital PD unit that had a peritonitis rate of 1 episode/26 patient months and 55 active patients on CAPD. Acetaldehyde level in the bags was assayed by gas chromatography. RESULTS: Twenty-one patients presented with signs of peritonitis including cloudy dialysate and abdominal tenderness with additional abdominal pain in 11 patients and vomiting in one. In all cases, cultures and Gram stains were negative for micro-organisms. Fever was not observed in any patient. Average dialysate white blood cell count was 1795/mm(3). All patients were free of intraperitoneal medication when symptoms appeared. Patients were using PD solutions from a newly established domestic production plant. Apparently all patients with symptoms of peritonitis used bags with the same lot number and the solution in the bags appeared to be darker in colour than that in bags with other lot numbers. Chemical analysis of the unused PD solution samples revealed acetaldehyde levels of 17-20 p.p. m. in bags containing darker solution, which is very high compared with the usual acetaldehyde level of 6 p.p.m. in heat-sterilized PD solutions. CONCLUSIONS: Based on the above findings, we hypothesize that higher levels of acetaldehyde and possibly other glucose degradation products may have been an aetiological factor in these 21 cases of chemical peritonitis. Our observation suggests that acetaldehyde, in concentrations 3-4 times higher than the usual level in commercially available PD solutions, may induce acute sterile peritonitis in CAPD patients.
Acetaldehyde↗
(Benzoylacetonato)chloro(1,10-phenanthroline)copper(II)
The crystal structure of the title compound, chloro(1, 10-phenanthroline-N,N')(1-phenyl-1,3-butanedionato-O,O')copper(II), [CuCl(C(10)H(9)O(2))(C(12)H(8)N(2))], has been determined. The Cu(II) ion displays a distorted square-pyramidal coordination, being linked to the two O atoms of the benzoylacetonate ligand and the two N atoms of the 1,10-phenanthroline ligand in the basal plane, and the Cl atom in the apical site. TheCu-N, Cu-O and Cu-Cl bond lengths are 2.043 (2)/2.025 (2), 1.914 (2)/1.941 (2) and 2.485 (1) A, respectively.
Journal Article↗
Function and regulation of yeast hexose transporters.
Glucose, the most abundant monosaccharide in nature, is the principal carbon and energy source for nearly all cells. The first, and rate-limiting, step of glucose metabolism is its transport across the plasma membrane. In cells of many organisms glucose ensures its own efficient metabolism by serving as an environmental stimulus that regulates the quantity, types, and activity of glucose transporters, both at the transcriptional and posttranslational levels. This is most apparent in the baker's yeast Saccharomyces cerevisiae, which has 20 genes encoding known or likely glucose transporters, each of which is known or likely to have a different affinity for glucose. The expression and function of most of these HXT genes is regulated by different levels of glucose. This review focuses on the mechanisms S. cerevisiae and a few other fungal species utilize for sensing the level of glucose and transmitting this information to the nucleus to alter HXT gene expression. One mechanism represses transcription of some HXT genes when glucose levels are high and works through the Mig1 transcriptional repressor, whose function is regulated by the Snf1-Snf4 protein kinase and Reg1-Glc7 protein phosphatase. Another pathway induces HXT expression in response to glucose and employs the Rgt1 transcriptional repressor, a ubiquitin ligase protein complex (SCF(Grr1)) that regulates Rgt1 function, and two glucose sensors in the membrane (Snf3 and Rgt2) that bind glucose and generate the intracellular signal to which Rgt1 responds. These two regulatory pathways collaborate with other, less well-understood, pathways to ensure that yeast cells express the glucose transporters best suited for the amount of glucose available.
Gene Expression Regulation, Fungal↗
Glucose sensing and signaling by two glucose receptors in the yeast Saccharomyces cerevisiae.
How eukaryotic cells sense availability of glucose, their preferred carbon and energy source, is an important, unsolved problem. Bakers' yeast (Saccharomyces cerevisiae) uses two glucose transporter homologs, Snf3 and Rgt2, as glucose sensors that generate a signal for induction of expression of genes encoding hexose transporters (HXT genes). We present evidence that these proteins generate an intracellular glucose signal without transporting glucose. The Snf3 and Rgt2 glucose sensors contain unusually long C-terminal tails that are predicted to be in the cytoplasm. These tails appear to be the signaling domains of Snf3 and Rgt2 because they are necessary for glucose signaling by Snf3 and Rgt2, and transplantation of the C-terminal tail of Snf3 onto the Hxt1 and Hxt2 glucose transporters converts them into glucose sensors that can generate a signal for glucose-induced HXT gene expression. These results support the idea that yeast senses glucose using two modified glucose transporters that serve as glucose receptors.
Amino Acid Sequence↗
Nonfreeing of the lower leaf of the rectus sheath at caesarean section: a randomized controlled trial.
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Cesarean Section↗
Effect of cefodizime on peritoneal mononuclear- and polymorphonuclear-cell chemotaxis.
In this study, a third-generation cephalosporin with proposed immunomodulatory properties, cefodizime, was investigated to see if it has any effect on the chemotactic activity of human peritoneal monocyte and polymorphonuclear cell populations ex vivo. Ten continuous ambulatory peritoneal dialysis patients with peritonitis were entered in the study. Monocytes and polymorphonuclear cells were isolated from the patients' peritoneal effluent prior to initiation of any antibiotic therapy. Chemotaxis was measured by the Boyden chamber method before and after 2-hour incubation with cefodizime (200 mg/2L). Following 2-hour incubation with 200 mg/2L cefodizime, monocyte chemotaxis was increased from 36.8 +/- 5.6 microns to 50.2 +/- 6.6 microns (P = 0.0005). A similar increase was observed in polymorphonuclear cells from 42.0 +/- 8.8 microns to 48.7 +/- 10.3 microns (P = 0.02). We conclude that cefodizime acts as a priming agent on peritoneal polymorphonuclear cells, particularly on monocytes, and increases their chemotactic movements.
Adult↗
Expression of the SUC2 gene of Saccharomyces cerevisiae is induced by low levels of glucose.
High levels of glucose repress expression of the SUC2 gene in the yeast Saccharomyces cerevisiae. We have discovered that low levels of glucose are required for maximal transcription of SUC2: SUC2 expression is induced about five- to ten-fold in cells growing on low levels of glucose (0.1%) compared to cells growing on galactose or glycerol. Two pieces of evidence suggest that this low-glucose-induced expression is mediated by a repression mechanism that involves an upstream repression site in the SUC2 promoter (URS(SUC2)). First, deletion of the URS(SUC2) results in expression of the SUC2 gene in the absence of glucose, and second the URS(SUC2) mediates a six-fold repression of a reporter gene when inserted into a heterologous promoter. However, this URS(SUC2) mediated repression occurs on all tested carbon sources, suggesting that this URS element acts in concert with all other promoter elements to respond to low concentrations of glucose. This repression requires the general repressor SSn6p. SNF3, which encodes a glucose transporter that appears to be a sensor of low levels of glucose, is also required for low-glucose-induced expression of SUC2.
DNA-Binding Proteins↗
Two glucose transporters in Saccharomyces cerevisiae are glucose sensors that generate a signal for induction of gene expression.
Glucose is the preferred carbon source for most eukaryotic cells and has profound effects on many cellular functions. How cells sense glucose and transduce a signal into the cell is a fundamental, unanswered question. Here we describe evidence that two unusual glucose transporters in the yeast Saccharomyces cerevisiae serve as glucose sensors that generate an intracellular glucose signal. The Snf3p high-affinity glucose transporter appears to function as a low glucose sensor, since it is required for induction of expression of several hexose transporter (HXT) genes, encoding glucose transporters, by low levels of glucose. We have identified another apparent glucose transporter, Rgt2p, that is strikingly similar to Snf3p and is required for maximal induction of gene expression in response to high levels of glucose. This suggests that Rgt2p is a high glucose-sensing counterpart to Snf3p. We identified a dominant mutation in RGT2 that causes constitutive expression of several HXT genes, even in the absence of the inducer glucose. This same mutation introduced into SNF3 also causes glucose-independent expression of HXT genes. Thus, the Rgt2p and Snf3p glucose transporters appear to act as glucose receptors that generate an intracellular glucose signal, suggesting that glucose signaling in yeast is a receptor-mediated process.
Amino Acid Sequence↗
Two different repressors collaborate to restrict expression of the yeast glucose transporter genes HXT2 and HXT4 to low levels of glucose.
Transcription of the yeast HXT2 and HXT4 genes, which encode glucose transporters, is induced only by low levels of glucose. This low-glucose-induced expression is mediated by two independent repression mechanisms: in the absence of glucose, transcription of both genes is prevented by Rgt1p, a C6 zinc cluster protein; at high levels of glucose, expression of HXT2 and HXT4 is repressed by Mig1p. Only at low glucose concentrations are both repressors inactive, leading to a 10- to 20-fold induction of gene expression. Mig1p and Rgt1p act directly on HXT2 and HXT4 by binding to their promoters. This transcriptional regulation is physiologically very important to the yeast cell because it causes these glucose transporters to be expressed only in low-glucose media, in which they are required for growth.
Base Sequence↗
Rgt1p of Saccharomyces cerevisiae, a key regulator of glucose-induced genes, is both an activator and a repressor of transcription.
The RGT1 gene of Saccharomyces cerevisiae plays a central role in the glucose-induced expression of hexose transporter (HXT) genes. Genetic evidence suggests that it encodes a repressor of the HXT genes whose function is inhibited by glucose. Here, we report the isolation of RGT1 and demonstrate that it encodes a bifunctional transcription factor. Rgt1p displays three different transcriptional modes in response to glucose: (i) in the absence of glucose, it functions as a transcriptional repressor; (ii) high concentrations of glucose cause it to function as a transcriptional activator; and (iii) in cells growing on low levels of glucose, Rgt1p has a neutral role, neither repressing nor activating transcription. Glucose alters Rgt1p function through a pathway that includes two glucose sensors, Snf3p and Rgt2p, and Grr1p. The glucose transporter Snf3p, which appears to be a low-glucose sensor, is required for inhibition of Rgt1p repressor function by low levels of glucose. Rgt2p, a glucose transporter that functions as a high-glucose sensor, is required for conversion of Rgt1p into an activator by high levels of glucose. Grr1p, a component of the glucose signaling pathway, is required both for inactivation of Rgt1p repressor function by low levels of glucose and for conversion of Rgt1p into an activator at high levels of glucose. Thus, signals generated by two different glucose sensors act through Grr1p to determine Rgt1p function.
Bacterial Proteins↗
Three different regulatory mechanisms enable yeast hexose transporter (HXT) genes to be induced by different levels of glucose.
The HXT genes (HXT1 to HXT4) of the yeast Saccharomyces cerevisiae encode hexose transporters. We found that transcription of these genes is induced 10- to 300-fold by glucose. Analysis of glucose induction of HXT gene expression revealed three types of regulation: (i) induction by glucose independent of sugar concentration (HXT3); (ii) induction by low levels of glucose and repression at high glucose concentrations (HXT2 and HXT4); and (iii) induction only at high glucose concentrations (HXT1). The lack of expression of all four HXT genes in the absence of glucose is due to a repression mechanism that requires Rgt1p and Ssn6p. GRR1 seems to encode a positive regulator of HXT expression, since grr1 mutants are defective in glucose induction of all four HXT genes. Mutations in RGT1 suppress the defect in HXT expression caused by grr1 mutations, leading us to propose that glucose induces HXT expression by activating Grr1p, which inhibits the function of the Rgt1p repressor. HXT1 expression is also induced by high glucose levels through another regulatory mechanism: rgt1 mutants still require high levels of glucose for maximal induction of HXT1 expression. The lack of induction of HXT2 and HXT4 expression on high levels of glucose is due to glucose repression: these genes become induced at high glucose concentrations in glucose repression mutants (hxk2, reg1, ssn6, tup1, or mig1). Components of the glucose repression pathway (Hxk2p and Reg1p) are also required for generation of the high-level glucose induction signal for expression of the HXT1 gene. Thus, the glucose repression and glucose induction mechanisms share some of the same components and may share the same primary signal generated from glucose.
Gene Expression↗
Glucose uptake and metabolism in grr1/cat80 mutants of Saccharomyces cerevisiae.
Glucose repression in the yeast Saccharomyces cerevisiae designates a global regulatory system controlling the expression of various sets of genes required for the utilization of alternate carbon sources. In a screen, designed for the selection of mutants with reduced glycolytic flux we obtained isolates which were shown by complementation of the cloned wild-type gene to be allelic to the glucose repression mutants grr1/cat80/cot2 previously described. We demonstrate that the grr1 lesion lead to a concentration-dependent decrease in glycolytic flux on glucose. It is very likely that this is caused by a significant decrease in the expression of various genes encoding hexose transporters (HXT1,3) leading to a reduced glucose-uptake rate. In contrast, expression of the maltose permease gene (MAL11) and maltose utilization is normal. There is indirect evidence that grr1 affects the uptake of amino acids, and others have shown that the sugar-induced transport of divalent cations is impaired. These effects are not glucose-specific. We suggest that Grr1, a putative cytoplasmic protein, has a central function in the sensing of nutritional conditions for a variety of unrelated substances, and that relief from glucose repression may be a corollary of this defect in sensing.
Biological Transport↗
A wound-induced promoter driving npt-II expression limited to dedifferentiated cells at wound sites is sufficient to allow selection of transgenic shoots.
There is much data to indicate that only a small number of cells in plant explants are competent for stable transformation by Agrobacterium. Circumstantial evidence suggests that certain cells reentering cell division at wound sites are competent for transformation by Agrobacterium. We have discovered a member of the intracellular PR gene family from asparagus (AoPR1) which is strongly expressed upon wounding and during the reactivation of the cell cycle in cultured asparagus cells, but which shows very little expression in intact plant tissues. The promoter from the AoPR1 gene was fused to an intron-containing GUS reporter gene and shown to be more strongly expressed than the commonly used CaMV 35S constitutive promoter in target cells for plant transformation. A transcriptional fusion of the AoPR1 promoter with an NPT-II gene was found to be a very efficient marker for the selection of transgenic tobacco callus. Expression of the AoPR1-NPT-II gene allowed efficient shoot formation on transgenic callus and efficient adventitious root formation on transgenic shoots. These latter observations provided firm evidence that transformation selection marker gene expression is most crucial at the early stages of the transformation process, during the establishment of transformed micro-calli.
Agrobacterium tumefaciens↗
Glucose uptake and catabolite repression in dominant HTR1 mutants of Saccharomyces cerevisiae.
Growth and carbon metabolism in triosephosphate isomerase (delta tpi1) mutants of Saccharomyces cerevisiae are severely inhibited by glucose. By using this feature, we selected for secondary site revertants on glucose. We defined five complementation groups, some of which have previously been identified as glucose repression mutants. The predominant mutant type, HTR1 (hexose transport regulation), is dominant and causes various glucose-specific metabolic and regulatory defects in TPI1 wild-type cells. HTR1 mutants are deficient in high-affinity glucose uptake and have reduced low-affinity transport. Transcription of various known glucose transporter genes (HXT1, HXT3, and HXT4) was defective in HTR1 mutants, leading us to suggest that HTR mutations affect a negative factor of HXT gene expression. By contrast, transcript levels for SNF3, which encodes a component of high-affinity glucose uptake, were unaffected. We presume that HTR1 mutations affect a negative factor of HXT gene expression. Multicopy expression of HXT genes or parts of their regulatory sequences suppresses the metabolic defects of HTR1 mutants but not their derepressed phenotype at high glucose concentrations. This suggests that the glucose repression defect is not a direct result of the metabolically relevant defect in glucose transport. Alternatively, some unidentified regulatory components of the glucose transport system may be involved in the generation or transmission of signals for glucose repression.
Blotting, Northern↗
[Observations on the isolation of polio in 2 cases].
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Enterovirus↗
Shaping the health future in Turkey: a new role for human resource planning.
The expanding health needs and expectations of a growing and changing population in Turkey are placing new pressures on a health system that is increasingly financially constrained. These pressures are bringing into sharp focus the need to take radical approaches to the organization, planning and management of the health sector; and, in particular, in the planning and management of health human resources. Issues of effectiveness, efficiency and value for money are increasingly becoming the central issues for the 1990s and beyond. The article examines the development of the Turkish health system. Within a framework of health care reform proposals emerging from a major development project in the Ministry of Health itself, the text explores current initiatives and future needs in developing human resource planning if the health care reforms are to be successful in meeting the health needs of the population.
Developing Countries↗