scholarly journals Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins

1993 ◽  
Vol 289 (3) ◽  
pp. 735-741 ◽  
Author(s):  
Z Y Zhang-Keck ◽  
A L Burns ◽  
H B Pollard
Keyword(s):  
Amino Acid ◽  
Blot Analysis ◽  
Mouse Liver ◽  
Point Mutations ◽  
Coding Region ◽  
Alpha Helices ◽  
Coding Regions ◽  
Terminal Domain ◽  
Group I ◽  
Group Ii

Two sets of cDNAs encoding mouse synexin were isolated from a liver cDNA library and sequenced. The coding regions of synexin clones show 99% identity. By contrast, the two mouse synexin cDNAs differ in a number of ways in both 5′ and 3′ non-coding regions. The two sets of cDNA encode a polypeptide of 463 amino acid residues which has a deduced molecular mass of 50 kDa. The amino acid sequence of mouse synexin shows a high degree of similarity to both the unique N-terminal domain and the highly conserved C-terminal domain of previously cloned human synexin. Northern-blot analysis using mouse liver polyadenylated RNA revealed two transcripts of 1.8 kb and 2.6 kb, corresponding to group I and group II respectively. Further hybridization analysis using specific sequences from each set of clones showed that the two sizes of mRNAs differ in the length of the 3′ non-coding region which corresponded to the cDNAs. Both mouse liver synexin and recombinant mouse synexin expressed in Escherichia coli reacted after Western-blot analysis with a goat antibody against bovine synexin. Only in the larger group-II cDNAs do we find point mutations leading to amino acid replacements of Ser to Ala at residue 145 in the unique N-terminal domain, and of Ala to Gly at residue 304 in the transition zone between repeats II and III. We conclude from a comparison of mouse, human and Dictyostelium synexins that changes occur predominantly in the hydrophobic N-terminal domain, or, in the C-terminal region at the ends of some predicted alpha-helices, on the hydrophobic face of the amphipathic C-helices, and within a lengthy non-helical domain connecting major repeats II and III.

Effect of amino acid infusion on renal hemodynamics in humans: a dose-response study

1994 ◽  
Vol 267 (5) ◽  
pp. F703-F708 ◽  
Author(s):  
M. Giordano ◽  
P. Castellino ◽  
E. L. McConnell ◽  
R. A. DeFronzo
Keyword(s):  
Amino Acid ◽  
Dose Response ◽  
Renal Hemodynamics ◽  
Group Iv ◽  
Group V ◽  
Group Iii ◽  
Amino Acid Infusion ◽  
Group I ◽  
Basal Plasma ◽  
Group Ii

We evaluated the dose-response relationship between the plasma amino acid (AA) concentration and renal hemodynamics in eight normal subjects. After an overnight fast, a balanced 10% AA solution was infused for 180 min at five separate infusion rates: 0.5 (group I), 1.0 (group II), 2.0 (group III), 4.0 (group IV), and 6.0 (group V) ml.kg-1.min-1 on separate days. Basal plasma AA concentration was 1.87 +/- 0.1 mmol/l and increased to 2.26 +/- 0.1 (group I), 2.66 +/- 0.2 (group II), 3.79 +/- 0.5 (group III), 5.81 +/- 0.4 (group IV), and 7.41 +/- 0.4 mmol/l (group V). Basal glomerular filtration rate (GFR) and renal plasma flow (RPF) averaged 95 +/- 4 and 476 +/- 29 ml.1.73 m-2.min-1, respectively, and rose to 98 +/- 5 and 506 +/- 40 (group I) [P = not significant (NS)], 102 +/- 3 and 533 +/- 30 (group II) (P < 0.05 vs. basal), 110 +/- 4 and 567 +/- 29 (group III), 115 +/- 7 and 610 +/- 55 (group IV), and 117 +/- 7 and 614 +/- 66 ml.1.73 m-2.min-1 (group V) (P = NS vs. group IV). Basal plasma glucagon concentration averaged 68 +/- 10 pg/ml and increased to 74 +/- 10 (group I), 83 +/- 11 (group II) (P < 0.05 vs. basal), 100 +/- 14 (group III), 121 +/- 14 (group IV), and 229 +/- 35 pg/ml (group V) (P < 0.01 vs. basal). Increases in plasma growth hormone (GH) and insulin levels were observed only during groups IV and V.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Pathomechanism of Insulin Resistance in Men with Central Obesity: Correlation of GGT, GPx, hs-CRP and Plasma Total Cysteine

2013 ◽  
Vol 5 (2) ◽  
pp. 101 ◽  
Author(s):  
Ritawaty Ritawaty ◽  
Indriyanti Rafi Sukmawati ◽  
Ilhamjaya Patellongi ◽  
Ferry Sandra
Keyword(s):  
Oxidative Stress ◽  
Insulin Resistance ◽  
Amino Acid ◽  
Fatty Liver ◽  
Central Obesity ◽  
Group Iv ◽  
Group Iii ◽  
Group I ◽  
Group Ii ◽  
Hs Crp

BACKGROUND: Gamma glutamyltransferase (GGT) was reported recently to be associated with inflammation, oxidative stress and increased amino acid. However, role of GGT in insulin resistance pathomechanism is not exactly known. Therefore correlation of GGT with inflammation, oxidative stress and elevated amino acid, in men with central obesity need to be confirmed.METHODS: A cross-sectional study was designed. Men with central obesity were recruited and selected. Anthropometric parameters, creatinine, hs-CRP, fasting glucose, fasting insulin, glutathione peroxidase (GPx) activity, GGT, plasma total cysteine (tCys) and fatty liver were measured. Subjects were then divided in 4 groups based on waist circumference (WC) and fatty liver: Group I: WC ≤100 cm, without fatty liver; Group II: WC ≤100 cm, with fatty liver; Group III: WC >100 cm, without fatty liver; Group IV: WC >100 cm, with fatty liver. All biochemical characteristics in each group were then statistically analyzed.RESULTS: Seventy-two men with central obesity were selected. Numbers of subjects in each group were: Group I: n=33; Group II: n=5; Group III: n=17; Group IV: n=17. We found significant difference of HOMA-IR between Group I and IV, significant correlation between GGT and HOMAIR, and significant negative correlation between tCys with HOMA-IR in Group IV.CONCLUSION: GGT was significantly correlated with HOMA-IR in men with WC >100 cm and fatty liver. Further investigation with more subjects is necessary to determine clear GGT cut-off to distinguish subjects with fatty liver and insulin resistance.KEYWORDS: GGT, hs-CRP, GPx, tCys, HOMA-IR, insulin resistance

scholarly journals The Effect of Parenteral Infusion of Amino Acids in Burn Patient

2013 ◽  
Vol 24 (1) ◽  
pp. 12-15
Author(s):  
Kamrun Nahar ◽  
Zeba-un Naher ◽  
Matira Khanam ◽  
Shaheen Akhter ◽  
Tahmina Bashar ◽  
...  
Keyword(s):  
Amino Acid ◽  
Serum Albumin ◽  
Total Protein ◽  
Burn Injury ◽  
Burn Patients ◽  
Serum Total Protein ◽  
Female Ratio ◽  
Group I ◽  
The Mean ◽  
Group Ii

Adequate nutritional support may prevent weight loss  following severe burn injury. However, persistently low  levels of serum albumin, transferring and serum total  protein in burn patients have suggested that a protein  deficiency may continue to exist which is out of proportion  to energy requirements.  This interventional study cross sectional study was done in  the Department of Biochemistry, Bangabandhu Sheikh  Mujib Medical University (BSMMU), Dhaka, Bangladesh  during January 2008 to December 2008. A total of 40 acute  burn injury (within 24 hours of burn) patients of 20-45  years age with 15%-30% burn were selected for this study  as case. The study subjects were divided into two groups:  Group I represent superficial burn & Group II represents  deep burn.  The mean age of 28.35±6.81 years and 30.85±7.32 years in  group I and group II respectively. The number of male in  Group-I was 08 and Group-II was 08 and male female ratio  was 2:3. The mean serum total protein before infusion of  amino acid in Group-I was 55.31±3.58 g/L and in Group-II  was 52.01±2.26 g/L (p<0.001). The mean serum total  protein after infusion of amino acid in Group-I was  68.02±2.04 g/L and in Group-II was 61.86±2.49g/L  (p<0.001). The mean serum albumin before infusion of  amino acid in Group-I was 27.6±2.88 g/L and in Group-II  was 25.57±1.89 g/L (p<0.001). The mean serum albumin  after infusion of amino acid in Group-I was 22.29±3.50 g/L  and in Group-II was 19.83±2.86 g/L (p<0.001). In group-I,  serum total protein was increased by 22.98% after infusion  and in group-II, that was increased by 18.94% (p<0.01).  In group-I, serum albumin was decreased by 19.24% after  infusion and in group-II, that was decreased by 22.45%  (p<0.05). Serum total protein significantly increased after  infusion of amino acid but serum albumin significantly  decreased after infusion of amino acid. DOI: http://dx.doi.org/10.3329/medtoday.v24i1.14107 Medicine TODAY Vol.24(1) 2012 pp.12-15

Molecular characterization of the Na-K-Cl cotransporter of bovine aortic endothelial cells

1997 ◽  
Vol 273 (1) ◽  
pp. C188-C197 ◽  
Author(s):  
T. R. Yerby ◽  
C. R. Vibat ◽  
D. Sun ◽  
J. A. Payne ◽  
M. E. O'Donnell
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Amino Acid ◽  
Blot Analysis ◽  
Cdna Probe ◽  
Bovine Aortic Endothelial Cell ◽  
Coding Region ◽  
Cerebral Microvessels ◽  
Aortic Endothelial Cells ◽  
Aortic Endothelial

The Na-K-Cl cotransporter is an important regulator of endothelial cell volume and may also contribute to flux of Na and Cl across the endothelium of the blood-brain barrier. To date, two Na-K-Cl cotransport isoforms have been identified, the cotransporter in secretory epithelia, NKCC1, and that in absorptive renal epithelia, NKCC2. Our previous studies showed that a monoclonal antibody to the cotransporter of human colonic T84 epithelial cells, an NKCC1 isoform, recognizes a 170-kDa glycoprotein from endothelial cells. The molecular identity of the Na-K-Cl cotransporter present in endothelial cells, however, has been unknown. In addition, although evidence has been provided that phosphorylation of the endothelial cotransporter plays a role in regulating its activity, little is known about potential sites for protein kinase interaction with the cotransporter. The present study was conducted to determine the molecular structure of the endothelial Na-K-Cl cotransporter. Using a 1.0-kilobase (kb) cDNA fragment from a conserved region of the T84 cell cotransporter, we screened a bovine aortic endothelial cell cDNA library and subsequently identified and sequenced two overlapping clones that together spanned the entire coding region. The endothelial cotransporter is a 1,201-amino acid protein with 12 putative transmembrane segments and large amino and carboxy termini, each containing several consensus sites for phosphorylation by protein kinases. Comparison of the endothelial cotransporter amino acid sequence with known NKCC1 and NKCC2 sequences revealed a 96% identity with NKCC1. Northern blot analysis using a cDNA probe from the endothelial cotransporter revealed high expression of approximately 7.5-kb transcripts in a number of bovine tissues. Finally, a prominent expression of Na-K-Cl cotransporter was found by Western blot analysis in both cultured and freshly isolated endothelial cells of bovine aorta and cerebral microvessels.

Plasma glucose and insulin responses in growing rats fed a total parenteral nutrition diet either intravenously or intragastrically

1984 ◽  
Vol 62 (7) ◽  
pp. 775-780 ◽  
Author(s):  
Norman S. Track ◽  
Ernest Cutz ◽  
Barbara H. Witt
Keyword(s):  
Amino Acid ◽  
Parenteral Nutrition ◽  
Total Parenteral Nutrition ◽  
Plasma Glucose ◽  
Plasma Insulin ◽  
Glucose Levels ◽  
Group I ◽  
Plasma Insulin Levels ◽  
Group Ii ◽  
Insulin Responses

The effect of administering either intravenously (group I) or intragastrically (group II) a glucose – amino acid total parenteral nutrition diet over a 12-day period upon plasma glucose and insulin responses was examined in adolescent rats. Infusion of the 25% glucose – 12.2% amino acid diet at a rate of 300 kCal∙kg body weight−1∙24 h−1 supported normal weight gain over the 12-day study period in both intravenously (group I) and intragastrically (group II) alimented rats. Mean plasma glucose levels rose dramatically in both groups by the end of day 1; group I had significantly higher mean plasma insulin levels. By day 3, the group I mean plasma glucose value decreased significantly while the group II mean glucose value remained virtually unchanged. Mean plasma insulin values more than doubled in both groups with the group I level still remaining significantly above the group II level. At days 6 and 12, group I mean plasma glucose levels were significantly below group II while both groups had similar plasma insulin levels. Data from this 12-day intravenous–intragastric alimentation study reveals quite different metabolic responses compared with acute (120–180 min) studies of the enteroinsular axis.

Recycling of an amino acid label with prolonged isotope infusion: implications for kinetic studies

1985 ◽  
Vol 248 (4) ◽  
pp. E482-E487 ◽  
Author(s):  
W. F. Schwenk ◽  
E. Tsalikian ◽  
B. Beaufrere ◽  
M. W. Haymond
Keyword(s):  
Amino Acids ◽  
Steady State ◽  
Amino Acid ◽  
Infusion Rate ◽  
Kinetic Studies ◽  
Intracellular Pool ◽  
Group I ◽  
Group Ii ◽  
Plasma Leucine ◽  
Amino Acid Label

To investigate whether recycling of a labeled amino acid would occur after 24 h of infusion, two groups of normal volunteers were infused with [3H]leucine and alpha-[14C]-ketoisocaproate for 4 h and [2H3]leucine for either 4 or 24 h (groups I and II, respectively). Entry of [2H3 )leucine at steady state into the plasma space was indistinguishable from its infusion rate for group I but 30% higher (P less than 0.001) than this rate for group II, demonstrating significant recycling of label. After discontinuation of the infusions, isotope disappearance from the plasma space was followed for 2 h. The 3H and 14C decay data for both groups suggest that plasma leucine and alpha-ketoisocaproate are derived from a single intracellular pool in the postabsorptive state. In group I, the 3H and 2H labels decayed identically; whereas, in group II, the decay of [2H3]-leucine and alpha-[2H3]ketoisocaproate was slower (P less than 0.01) than the decay of [3H]leucine and alpha-[3H]ketoisocaproate, confirming re-entry of label after a 24-h infusion. Therefore kinetic values calculated from models assuming no recycling of labeled amino acids are most likely not quantitative and must be interpreted with care when flux does not change or decreases.

scholarly journals Amino Acid Starvation Enhances Programmed Ribosomal Frameshift in Metavirus Ty3 of Saccharomyces cerevisiae

2016 ◽  
Vol 2016 ◽  
pp. 1-6
Author(s):  
Sezai Türkel
Keyword(s):  
Amino Acid ◽  
Amino Acid Starvation ◽  
Yeast Cells ◽  
Dependent Manner ◽  
Coding Region ◽  
Coding Regions ◽  
In The Wild ◽  
Amino Acid Depletion ◽  
A Site ◽  
Wild Type Yeast

Ty3 is a retroviral-like element and propagates with a retroviral-like mechanism within the yeast cells. Ty3 mRNA contains two coding regions, which are GAG3 and POL3. The coding region POL3 is translated as a GAG3-POL3 fusion protein by a +1 programmed frameshift. In this study, it was shown that the Ty3 frameshift frequency is significantly increased by amino acid starvation in a Gcn2p complex dependent manner. When the yeast cells were subjected to amino acid starvation, the frameshift frequency of Ty3 increased more than 2-fold in the wild-type yeast cells, mostly independent of Gcn4p. However, Ty3 frameshift frequency remained at basal level in the gcn1, gcn20, or gcn2 mutant yeast cells in amino acid starved yeasts. Gcn1p forms a complex with Gcn2p and Gcn20p and is involved in the sensing of uncharged tRNAs on the ribosomal A-site during translation. Increases in uncharged tRNA levels due to amino acid depletion lead to ribosomal pauses. These ribosomal pauses are significant actors in the regulation of Ty3 frameshift frequency. Results of this research revealed that frameshift frequency in Ty3 is regulated by the Gcn2p complex in response to amino acid starvation in yeast.

Coding Region of IRF6 Gene May Not Be Causal for Van Der Woude Syndrome in Cases from India

2009 ◽  
Vol 46 (5) ◽  
pp. 541-544 ◽  
Author(s):  
Akhtar Ali ◽  
Subodh Kumar Singh ◽  
Rajiva Raman
Keyword(s):  
Present Report ◽  
Direct Sequencing ◽  
Geographical Area ◽  
Point Mutations ◽  
Coding Region ◽  
Van Der Woude Syndrome ◽  
Coding Regions ◽  
Irf6 Gene ◽  
Novel Variants ◽  
History Of

Objective: Evaluation of the IRF6 gene in Van der Woude syndrome cases from an Indian population. Subjects: Nine affected and four unaffected individuals from seven families with Van der Woude syndrome as well as five normal controls (with no history of Van der Woude or any other congenital malformation and belonging to the same geographical area as the families with Van der Woude syndrome). Method: Direct sequencing of all coding regions and exon-intron boundaries of the IRF6 gene. Results: Five novel variants: IVS1+3900 A>G, 191 T>C, IVS4+775 C>T, IVS8+218 C>T, 1511 T>A (Ser 416 Arg) and two known variants: IVS6+27 C>G, 1083 G>A (V274I) were detected. Except for one, all were in noncoding regions either in 3′UTR or in introns. There was only one mutation in the coding region, detected in a normal control. Conclusion: The present report indicates that point mutations in the coding region of the IRF6 gene may not be a major cause of Van der Woude syndrome in Indian populations.

scholarly journals Boundaries of somatic mutation in rearranged immunoglobulin genes: 5' boundary is near the promoter, and 3' boundary is approximately 1 kb from V(D)J gene.

1990 ◽  
Vol 172 (6) ◽  
pp. 1717-1727 ◽  
Author(s):  
S G Lebecque ◽  
P J Gearhart
Keyword(s):  
Structural Information ◽  
Gene Segment ◽  
Point Mutations ◽  
Sequence Motif ◽  
Immunoglobulin Gene ◽  
Coding Region ◽  
Nucleotide Substitutions ◽  
Coding Regions ◽  
Dna Strands ◽  
Transcriptional State

To investigate why somatic mutations are spatially restricted to a region around the rearranged V(D)J immunoglobulin gene, we compared the distribution of mutations flanking murine V gene segments that had rearranged next to either proximal or distal J gene segments. 124 nucleotide substitutions, nine deletions, and two insertions were identified in 32,481 bp of DNA flanking the coding regions from 17 heavy and kappa light chain genes. Most of the mutations occurred within a 2-kb region centered around the V(D)J gene, regardless of which J gene segment was used, suggesting that the structural information for mutation is located in sequences around and within the V(D)J gene, and not in sequences downstream of the J gene segments. The majority of mutations were found within 300 bp of DNA flanking the 5' side of the V(D)J gene and 850 bp flanking the 3' side at a frequency of 0.8%, which was similar to the frequency in the coding region. The frequency of flanking mutations decreased as a function of distance from the gene. There was no evidence for hot spots in that every mutation was unique and occurred at a different position. No mutations were found upstream of the promoter region, suggesting that the promoter delimits a 5' boundary, which provides strong evidence that transcription is necessary to generate mutation. The 3' boundary was approximately 1 kb from the V(D)J gene and was not associated with a DNA sequence motif. Occasional mutations were located in the nuclear matrix association and enhancer regions. The pattern of substitutions suggests that there is discrimination between the two DNA strands during mutation, in that the four bases were mutated with different frequencies on each strand. The high frequency of mutations in the 3' flanking region and the uniqueness of each mutation argues against templated gene conversion as a mechanism for generating somatic diversity in murine V(D)J genes. Rather, the data support a model for random point mutations where the mechanism is linked to the transcriptional state of the gene.

scholarly journals Mitochondrial Translation of Saccharomyces cerevisiae COX2 mRNA Is Controlled by the Nucleotide Sequence Specifying the Pre-Cox2p Leader Peptide

2001 ◽  
Vol 21 (7) ◽  
pp. 2359-2372 ◽  
Author(s):  
Nathalie Bonnefoy ◽  
Nada Bsat ◽  
Thomas D. Fox
Keyword(s):  
Amino Acid ◽  
Mitochondrial Gene ◽  
Large Subunit ◽  
Point Mutations ◽  
Regulatory Elements ◽  
Leader Peptide ◽  
Mrna Sequence ◽  
Coding Region ◽  
Mitochondrial Translation

ABSTRACT The mitochondrial gene encoding yeast cytochrome oxidase subunit II (Cox2p) specifies a precursor protein with a 15-amino-acid leader peptide. Deletion of the entire leader peptide coding region is known to block Cox2p accumulation posttranscriptionally. Here, we examined in vivo the role of the pre-Cox2p leader peptide and the mRNA sequence that encodes it in the expression of a mitochondrial reporter gene,ARG8m , fused to the 91st codon ofCOX2. We found within the coding sequence antagonistic elements that control translation: the positive element includes sequences in the first 14 codons specifying the leader peptide, while the negative element appears to be within codons 15 to 91. Partial deletions, point mutations, and local frameshifts within the leader peptide coding region were placed in both thecox2::ARG8m reporter and inCOX2 itself. Surprisingly, the mRNA sequence of the first six codons specifying the leader peptide plays an important role in positively controlling translation, while the amino acid sequence of the leader peptide itself is relatively unconstrained. Two mutations that partially block translation can be suppressed by nearby sequence substitutions that weaken a predicted stem structure and by overproduction of either the COX2 mRNA-specific translational activator Pet111p or the large-subunit mitochondrial ribosomal protein MrpL36p. We propose that regulatory elements embedded in the translated COX2 mRNA sequence could play a role, together with trans-acting factors, in coupling regulated synthesis of nascent pre-Cox2p to its insertion in the mitochondrial inner membrane.

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