Effects of Amino Acid Dialysis Compared to Dextrose Dialysis in Children on Continuous Cycling Peritoneal Dialysis

1999 ◽  
Vol 19 (3) ◽  
pp. 237-247 ◽  
Author(s):  
Izhar U. Qamar ◽  
Donna Secker ◽  
Leo Levin ◽  
Judith A. Balfe ◽  
Stanley Zlotkin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Peritoneal Dialysis ◽  
Amino Acid ◽  
Creatinine Clearance ◽  
Single Amino Acid ◽  
Fasting Plasma ◽  
Continuous Cycling Peritoneal Dialysis ◽  
Total Plasma Protein ◽  
Continuous Cycling ◽  
Total Body

Objective To compare the biochemical and nutritional effects of amino acid dialysis with dextrose dialysis in children receiving continuous cycling peritoneal dialysis (CCPD). Design A prospective randomized cross-over study. Setting Nonhospitalized patients. Patients Seven children aged 1.8 to 16.0 years (mean 8.1 years) with end-stage renal disease who were receiving CCPD. Interventions Each patient received nighttime automated CCPD of dextrose, plus a single daytime dwell of either amino acid dialysate or dextrose dialysate. After 3 months, subjects crossed over to the alternative regimen for a subsequent 3 months. Main Outcome Measures Creatinine clearance, ultra-filtration, urea, creatinine, electrolytes, total protein, albumin, fasting plasma amino acids, anthropometrics, total body nitrogen. Results Amino acid dialysis was comparable to dextrose dialysis for creatinine clearance and ultrafiltration. Plasma urea concentrations were higher during amino acid dialysis. No clinical side effects or worsening of metabolic acidosis was observed. Caloric intake increased and protein intake improved. Appetite and total body nitrogen increased in at least half the children during amino acid dialysis. Total plasma protein and albumin concentrations did not change significantly. Fasting plasma concentrations of amino acids after 3 months of amino acid dialysis were comparable to baseline values. For several amino acids, the dose-response curve was blunted after a single amino acid exchange following 3 months of amino acid dialysis, which may, in part, be due to the induction of hepatic enzyme synthesis. Conclusions Amino acid dialysis is an efficient form of peritoneal dialysis that should be considered for children with poor nutritional status for whom enteral nutrition supplementation has been unsuccessful. Further study is needed to determine the optimal amount of amino acids to deliver, the best time to administer the amino acid dialysis fluid, and the benefits of adding dextrose to the amino acid solution.

Effects of 3-Month Amino Acid Dialysis Compared to Dextrose Dialysis in Children on Continuous Ambulatory Peritoneal Dialysis

1994 ◽  
Vol 14 (1) ◽  
pp. 34-41 ◽  
Author(s):  
Izhar U. Qamar ◽  
Leo Levin ◽  
J. Williamson Balfe ◽  
Judith A. Balfe ◽  
Donna Secker ◽  
...  
Keyword(s):  
Peritoneal Dialysis ◽  
Amino Acid ◽  
Continuous Ambulatory Peritoneal Dialysis ◽  
Tertiary Care ◽  
Pediatric Nephrology ◽  
Biochemical Data ◽  
Single Amino Acid ◽  
Biochemical Effects ◽  
Total Plasma Protein ◽  
Amino Acid Levels

Objectives To compare the nutritional and biochemical effects of amino acid dialysis to dextrose dialysis in children receiving continuous ambulatory peritoneal dialysis (CAPD). Design Prospective randomized crossover study. Setting Pediatric Nephrology Unit in a tertiary care, teaching hospital of the University of Toronto. Patients Seven children aged 0.7–16.5 years receiving CAPD. All patients had poor linear growth, with 5 patients showing evidence of energy deficit. Interventions Each patient received either amino acid or dextrose dialysate for 3 months, then crossed over to the alternate regimen for a subsequent 3 months. Main Outcome Measures Nutritional and biochemical data were obtained on each patient during each dialysis regimen. Results Analysis of the patients’ nutritional data showed comparable weight gain with both regimens but no significant improvement in lean body mass with either regimen. Appetite improved in most patients during amino acid dialysis. Biochemical data during amino acid dialysis showed a tendency to higher plasma potassium and urea levels with no clinical side effects or worsening of acidosis; however, there was a reduced anion gap and increased total plasma protein, due mostly to a rise in plasma albumin and a smaller increase in immunoglobulins. With the exception of tryptophan, fasting amino acid levels at the start and end of amino acid dialysis did not show any significant change. An interesting phenomenon of early blunting of the rise in amino acid levels, following a single amino acid dialysate exchange, was noticed at the end of the amino acid dialysis period. This newly described phenomenon could have been due to tolerance or hepatic enzyme induction. Conclusions Overall amino acid dialysis was comparable to dextrose dialysis with no additional proven nutritional benefit, was equally effective in ultrafiltration and creatinine clearance, and produced no adverse clinical or biochemical effects.

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

scholarly journals Phylogenetic analysis and predicted functional effect of protein mutations of E6 and E7 HPV16 strains isolated in Indonesia

2015 ◽  
Vol 24 (4) ◽  
pp. 197-205
Author(s):  
Dwi Wulandari ◽  
Lisnawati Rachmadi ◽  
Tjahjani M. Sudiro
Keyword(s):  
Amino Acids ◽  
Phylogenetic Analysis ◽  
Amino Acid ◽  
Asian American ◽  
Protein Function ◽  
Single Amino Acid ◽  
Hpv16 E6 ◽  
E6 And E7 ◽  
Neutral Mutations

Background: E6 and E7 are oncoproteins of HPV16. Natural amino acid variation in HPV16 E6 can alter its carcinogenic potential. The aim of this study was to analyze phylogenetically E6 and E7 genes and proteins of HPV16 from Indonesia and predict the effects of single amino acid substitution on protein function. This analysis could be used to reduce time, effort, and research cost as initial screening in selection of protein or isolates to be tested in vitro or in vivo.Methods: In this study, E6 and E7 gene sequences were obtained from 12 samples of  Indonesian isolates, which  were compared with HPV16R (prototype) and 6 standard isolates in the category of European (E), Asian (As), Asian-American (AA), African-1 (Af-1), African-2 (Af-2), and North American (NA) branch from Genbank. Bioedit v.7.0.0 was used to analyze the composition and substitution of single amino acids. Phylogenetic analysis of E6 and E7 genes and proteins was performed using Clustal X (1.81) and NJPLOT softwares. Effects of single amino acid substitutions on protein function of E6 and E7 were analysed by SNAP.Results: Java variants and isolate ui66* belonged to European branch, while the others belonged to Asian and African branches. Twelve changes of amino acids were found in E6 and one in E7 proteins. SNAP analysis showed two non neutral mutations, i.e. R10I and C63G in E6 proteins. R10I mutations were found in Af-2 genotype (AF472509) and Indonesian isolates (Af2*), while C63G mutation was found only in Af2*.Conclusion: E6 proteins of HPV16 variants were more variable than E7. SNAP analysis showed that only E6 protein of African-2 branch had functional differences compared to HPV16R.

scholarly journals Transforming growth factor alpha: mutation of aspartic acid 47 and leucine 48 results in different biological activities.

1988 ◽  
Vol 8 (3) ◽  
pp. 1247-1252 ◽  
Author(s):  
E Lazar ◽  
S Watanabe ◽  
S Dalton ◽  
M B Sporn
Keyword(s):  
Amino Acids ◽  
Biological Activity ◽  
Amino Acid ◽  
Growth Factor ◽  
Aspartic Acid ◽  
Transforming Growth Factor ◽  
Biologically Active ◽  
Single Amino Acid ◽  
Transforming Growth Factor Alpha ◽  
Factor Alpha

To study the relationship between the primary structure of transforming growth factor alpha (TGF-alpha) and some of its functional properties (competition with epidermal growth factor (EGF) for binding to the EGF receptor and induction of anchorage-independent growth), we introduced single amino acid mutations into the sequence for the fully processed, 50-amino-acid human TGF-alpha. The wild-type and mutant proteins were expressed in a vector by using a yeast alpha mating pheromone promoter. Mutations of two amino acids that are conserved in the family of the EGF-like peptides and are located in the carboxy-terminal part of TGF-alpha resulted in different biological effects. When aspartic acid 47 was mutated to alanine or asparagine, biological activity was retained; in contrast, substitutions of this residue with serine or glutamic acid generated mutants with reduced binding and colony-forming capacities. When leucine 48 was mutated to alanine, a complete loss of binding and colony-forming abilities resulted; mutation of leucine 48 to isoleucine or methionine resulted in very low activities. Our data suggest that these two adjacent conserved amino acids in positions 47 and 48 play different roles in defining the structure and/or biological activity of TGF-alpha and that the carboxy terminus of TGF-alpha is involved in interactions with cellular TGF-alpha receptors. The side chain of leucine 48 appears to be crucial either indirectly in determining the biologically active conformation of TGF-alpha or directly in the molecular recognition of TGF-alpha by its receptor.

Five years' experience with continuous ambulatory or continuous cycling peritoneal dialysis in children

1987 ◽  
Vol 111 (4) ◽  
pp. 513-518 ◽  
Author(s):  
Tassilo von Lilien ◽  
Isidro B. Salusky ◽  
Ines Boechat ◽  
Robert B. Ettenger ◽  
Richard N. Fine
Keyword(s):  
Peritoneal Dialysis ◽  
Continuous Cycling Peritoneal Dialysis ◽  
Continuous Cycling

Acquisition of NFKB1-selective DNA binding by substitution of four amino acid residues from NFKB1 into RelA

1993 ◽  
Vol 13 (7) ◽  
pp. 3850-3859
Author(s):  
T A Coleman ◽  
C Kunsch ◽  
M Maher ◽  
S M Ruben ◽  
C A Rosen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dna Binding ◽  
Fusion Protein ◽  
Binding Specificity ◽  
Single Amino Acid ◽  
Nf Kappa B ◽  
Dna Binding Specificity ◽  
Dna Motif ◽  
Single Amino Acid Change

The subunits of NF-kappa B, NFKB1 (formerly p50) and RelA (formerly p65), belong to a growing family of transcription factors that share extensive similarity to the c-rel proto-oncogene product. The homology extends over a highly conserved stretch of approximately 300 amino acids termed the Rel homology domain (RHD). This region has been shown to be involved in both multimerization (homo- and heterodimerization) and DNA binding. It is now generally accepted that homodimers of either subunit are capable of binding DNA that contains a kappa B site originally identified in the immunoglobulin enhancer. Recent studies have demonstrated that the individual subunits of the NF-kappa B transcription factor complex can be distinguished by their ability to bind distinct DNA sequence motifs. By using NFKB1 and RelA subunit fusion proteins, different regions within the RHD were found to confer DNA-binding and multimerization functions. A fusion protein that contains 34 N-terminal amino acids of NFKB1 and 264 amino acids of RelA displayed preferential binding to an NFKB1-selective DNA motif while dimerizing with the characteristics of RelA. Within the NFKB1 portion of this fusion protein, a single amino acid change of His to Arg altered the DNA-binding specificity to favor interaction with the RelA-selective DNA motif. Furthermore, substitution of four amino acids from NFKB1 into RelA was able to alter the DNA-binding specificity of the RelA protein to favor interaction with the NFKB1-selective site. Taken together, these findings demonstrate the presence of a distinct subdomain within the RHD involved in conferring the DNA-binding specificity of the Rel family of proteins.

Continuous Cycling Peritoneal Dialysis Wet Is Better Than Dry

1990 ◽  
pp. 259-263 ◽  
Author(s):  
J. A. Diaz-Buxo ◽  
C. D. Farmer ◽  
J. T. Chandler ◽  
P. J. Walker ◽  
W. P. Burgess
Keyword(s):  
Peritoneal Dialysis ◽  
Continuous Cycling Peritoneal Dialysis ◽  
Continuous Cycling ◽  
Better Than

scholarly journals Identification of separate domains in the adenovirus E1A gene for immortalization activity and the activation of virus early genes.

1986 ◽  
Vol 6 (10) ◽  
pp. 3470-3480 ◽  
Author(s):  
E Moran ◽  
B Zerler ◽  
T M Harrison ◽  
M B Mathews
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Point Mutations ◽  
Apparent Molecular Weight ◽  
Amino Acid Position ◽  
Cysteine Residue ◽  
Transformation Function ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
E1a Gene

The transformation and early adenovirus gene transactivation functions of the E1A region were analyzed with deletion and point mutations. Deletion of amino acids from position 86 through 120 had little effect on the lytic or transforming functions of the E1A products, while deletion of amino acids from position 121 through 150 significantly impaired both functions. The sensitivity of the transformation function to alterations in the region from amino acid position 121 to 150 was further indicated by the impairment of transforming activity resulting from single amino acid substitutions at positions 124 and 135. Interestingly, conversion of a cysteine residue at position 124 to glycine severely impaired the transformation function without affecting the early adenovirus gene activating functions. Single amino acid substitutions in a different region of the E1A gene had the converse effect. All the mutants produced polypeptides of sufficient stability to be detected by Western immunoblot analysis. The single amino acid substitutions at positions 124 and 135, although impairing the transformation functions, did not detectably alter the formation of the higher-apparent-molecular-weight forms of the E1A products.

Single amino acid substitution of rat MRP2 results in acquired transport activity for taurocholate

2001 ◽  
Vol 281 (4) ◽  
pp. G1034-G1043 ◽  
Author(s):  
Kousei Ito ◽  
Hiroshi Suzuki ◽  
Yuichi Sugiyama
Keyword(s):  
Amino Acids ◽  
Multidrug Resistance ◽  
Amino Acid ◽  
Membrane Vesicles ◽  
Single Amino Acid ◽  
Sf9 Cells ◽  
Transport Activity ◽  
Wild Type ◽  
Cationic Amino Acids ◽  
The Difference

Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). The difference in TC transport activity between rat MRP2 and MRP3 was studied, focusing on the cationic amino acids in the transmembrane domains. For analysis, transport into membrane vesicles from Sf9 cells expressing wild-type and mutated MRP2 was examined. Substitution of Arg at position 586 with Leu and Ile and substitution of Arg at position 1096 with Lys, Leu, and Met resulted in the acquisition of TC transport activity, while retaining transport activity for glutathione and glucuronide conjugates. Substitution of Leu at position 1084 of rat MRP3 (which corresponds to Arg-1096 in rat MRP2) with Lys, but not with Val or Met, resulted in the loss of transport activity for TC and glucuronide conjugates. These results suggest that the presence of the cationic charge at Arg-586 and Arg-1096 in rat MRP2 prevents the transport of TC, whereas the presence of neutral amino acids at the corresponding position of rat MRP3 is required for the transport of substrates.

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