Developmental modulation of protein synthetic patterns by the human malarial parasite Plasmodium falciparum

1983 ◽  
Vol 61 (12) ◽  
pp. 1304-1314 ◽  
Author(s):  
David R. Allred ◽  
Irwin W. Sherman
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Acetylcholinesterase Activity ◽  
Amino Acid Mixture ◽  
Malarial Parasite ◽  
Acid Mixture ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Developmental Modulation

Under conditions of in vitro culture, Plasmodium falciparum incorporated amino acids into particulate (membrane) and soluble proteins in a pattern which changed sequentially and which was dependent upon the stage of parasite maturation. Synchronized cultures pulse labeled with a mixture of 15 14C-labeled amino acids or [14C]histidine alone displayed stage-related patterns of polypeptide biosynthesis. Certain plasmodial proteins were associated with both particulate (membrane) and soluble fractions, whereas others appeared to be specific to a given fraction. Proteolysis of intact infected cells with pronase under conditions which removed 97 ± 2.2% of the endogenous red cell acetylcholinesterase activity did not cause the apparent removal of any radiolabeled proteins; this suggests the absence of externally exposed, parasite-synthesized proteins in the infected red cell membrane. Such a result was consistent whether the radiolabel was [14C]histidine or the 14C-labeled amino acid mixture. These results indicate that specific modulation of parasite biosynthetic patterns occurs during the asexual reproductive cycle and is probably one mechanism whereby parasite differentiation occurs. Despite the formation of surface excrescences on infected red cells containing mature parasites, results of surface digestion experiments failed to demonstrate the presence of surface-exposed plasmodial proteins.

FACTORS INFLUENCING THE NUTRITIONAL VALUE OF FISH FLOUR: III. FURTHER STUDIES ON AVAILABILITY OF AMINO ACIDS

1963 ◽  
Vol 41 (7) ◽  
pp. 1589-1594 ◽  
Author(s):  
A. B. Morrison
Keyword(s):  
Amino Acids ◽  
Nutritional Value ◽  
Chloride Content ◽  
In Vitro Digestion ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Deficient Diet ◽  
Weight Gains ◽  
Flour Sample

Weight gains of male weanling rats given fish flour sample X were significantly increased by addition to the diet of methionine, histidine, threonine, and tryptophan. When histidine or methionine were omitted from the amino acid mixture, weight gains were similar to those found with the unsupplemented flour, and the combination of methionine and histidine was as effective as the four amino acids. Supplements of histidine and methionine had no effect on weight gains of rats given fish flour sample CFF, which was of high nutritional value. Sample X contained methionine in an amount similar to that of sample CFF, and somewhat less histidine. The amounts of methionine and histidine released during in vitro digestion with pancreatin were much less for sample X than for sample CFF. Steaming sample X for 30 minutes significantly increased its gross protein value determined in a methionine-deficient diet, but had no effect on the total or organic chloride content. It was concluded that sample X contained unavailable methionine and histidine.

Perturbation of red cell membrane structure during intracellular maturation of Plasmodium falciparum

Science ◽  
1986 ◽  
Vol 232 (4746) ◽  
pp. 102-104 ◽  
Author(s):  
TF Taraschi ◽  
A Parashar ◽  
M Hooks ◽  
H Rubin
Keyword(s):  
Plasmodium Falciparum ◽  
Malarial Parasite ◽  
Erythrocyte Membranes ◽  
Resonance Spectroscopy ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Structural Modifications ◽  
Spin Resonance ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

An experimental approach, which in this study was applied to the malarial system, can be used to analyze the molecular structure and organization of individual phospholipids in a wide variety of biological membranes. Electron spin resonance spectroscopy was used to investigate the structural modifications of the major red cell phospholipids that occur in erythrocyte membranes infected with the human malarial parasite, Plasmodium falciparum. These modifications were correlated with the intracellular developmental stage of the parasite. Phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine were increasingly disordered (fluidized) as infection progressed. This disordering occurred at different rates and to varying extents.

New Insights into the Function of N-Terminal 11 Amino Acids of Band 3 from Structural and Functional Study of a Naturally Occuring Band 3 Variant.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 577-577 ◽  
Author(s):  
Silverio Perrotta ◽  
Borriello Adriana ◽  
Lucia De Franceschi ◽  
Bruno Nobili ◽  
Achille Iolascon ◽  
...  
Keyword(s):  
Amino Acids ◽  
Band 3 ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Exon 2 ◽  
Protein 4.2 ◽  
Membrane Bound ◽  
Terminal Amino ◽  
Intron 2

Abstract The 911 amino acid human erythroid AE1 (eAE1) Cl-/HCO3- exchanger SLC4A1 (usually called band 3) is the major intrinsic membrane protein of red cells. The N-terminal cytoplasmic domain of AE1 represents the anchoring site for membrane-associated proteins such as ankyrin, protein 4.2, protein 4.1, glycolytic enzymes (including aldolase and glyceraldeyde-3-phosphate dehydrogenase (GAPDH) and hemoglobin. We identified marked band 3 deficiency in the second son of a consanguineous marriage with a life-threatening nonimmune hemolytic anemia. The patient was transfusion-dependent prior to splenectomy. SDS-PAGE and immunoblotting analysis of the proband red cell membrane proteins showed approximately 12±4% of band 3 and protein 4.2 compared to controls. Direct nucleotide sequence of SLC4A1 gene showed a single base substitution (T->C) at position +2 in the donor splice site of intron 2 (Band 3 Neapolis). Functionally, the mutation causes an altered splicing with the consequent formation of two different mature mRNAs, one including intron 2 and one skipping exon 2. While intron 2 retention leads to premature translation termination, exon 2 skipping causes the loss of the normal start site of eAE1 protein translation. The purification of mutant band 3 and its characterization by MALDI mass spectrometry demonstrated the lack of the first 11 amino acids due to the usage of second in frame start site. Real-time RT-PCR analyses of reticulocyte mRNA showed a marked decrement in band 3 transcription accounting for protein deficiency. The lack of the 11 N-terminal amino acids resulted in complete absence of membrane bound aldolase while other glycolitic enzymes (for example GAPDH) were membrane bound. Syk tyrosine kinase recognized the truncated band 3 as a substrate in vitro. In spite of this ability to be phosphorylated by Syk and to recruit Lyn tyrosine kinase in vitro, we were unable to demonstrate Tyr-phosphorylation of mutant band 3 in intact erythrocytes following stimulation by oxidative stress. This finding implies a requirement for the 11 N-terminal amino acids for the sequential Tyr-phosphorylation of band 3 in intact red cell membranes. The mutant band 3 was largely present in the high molecular weight aggregate fraction (about 5.2 fold higher than control), indicating its increased tendency to cluster in the membrane. The spontaneous clustering of truncated band 3 strongly suggests that the negatively charged N-terminal domain may regulate oligomeric state of band 3 in the membrane. Biophysical characterization showed that band 3 deficiency resulted in decreased cohesion between lipid bilyer and spectrin based membrane skeleton accounting for membrane loss. The structural and functional characterization of the naturally occuring mutant band 3 has enabled us to identify a significant role for the 11 N-terminal amino acids in band 3 function and in red cell membrane physiology.

Evidence for Active Transport of the Dipeptide Carnosine (β-Alanyl-l-Histidine) by Hamster Jejunum in Vitro

1974 ◽  
Vol 46 (6) ◽  
pp. 693-705 ◽  
Author(s):  
D. M. Matthews ◽  
Jill M. Addison ◽  
D. Burston
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Active Transport ◽  
Amino Acid Mixture ◽  
Intestinal Wall ◽  
Free Form ◽  
Acid Mixture ◽  
Total Uptake ◽  
Hydrolysis Of

1. The characteristics of intestinal transport and hydrolysis of carnosine (β-alanyl-l-histidine) have been studied in rings of everted hamster jejunum in vitro. 2. During incubation with carnosine, large amounts of intact peptide appeared in the intestinal wall, accompanied by small amounts of the constituent amino acids in the free form. Although there was some extracellular hydrolysis, the free amino acids appearing in the intestinal wall were almost entirely derived from intracellular hydrolysis of the peptide. Incubation in l-alanyl-l-histidine resulted in uptake of the constituent amino acids in the free form without appearance of intact peptide in the intestinal wall. 3. Total uptake of β-alanine (both peptide-bound and free) and total uptake of histidine were greater from a low concentration (1 μmol/ml) of carnosine than uptake of these amino acids from the equivalent amino acid mixture. At a high concentration of carnosine (20 μmol/ml), total uptake of β-alanine was greater from the peptide than from the equivalent amino acid mixture but total uptake of histidine was less. At this concentration, total uptake of β-alanine plus total uptake of histidine from the peptide was approximately the same as from the amino acid mixture. 4. Uptake of carnosine by jejunal rings was the result of a saturable process (Kt 9·4 μmol/ml, Vmax. 2·7 μmol g−1 initial wet wt. min−1). Intact carnosine was concentrated in the intestinal wall, the concentration ratio between intracellular fluid and incubation medium being up to 3·4/1. Uptake of carnosine was reduced by anoxia, metabolic inhibitors and replacement of medium Na+. Na+-dependent active transport was shown to be involved in uptake of carnosine by hamster jejunum in vitro.

Flow cytometric assessment of oxidant stress in age-fractionated thalassaemic trait erythrocytes and its relationship to in vitro growth of Plasmodium falciparum

Parasitology ◽  
1998 ◽  
Vol 116 (1) ◽  
pp. 1-6 ◽  
Author(s):  
A. C. SENOK ◽  
K. LI ◽  
E. A. S. NELSON ◽  
M. ARUMANAYAGAM ◽  
C. K. LI
Keyword(s):  
Plasmodium Falciparum ◽  
Oxidant Stress ◽  
Inverse Correlation ◽  
Malarial Parasite ◽  
Red Cell ◽  
Flow Cytometric ◽  
Age Related ◽  
Cell Age

The role of oxidant stress in mediating the protection against malaria in thalassaemic red blood cells (RBC) has been hypothesized. In this study we have assessed the relationship between oxidant stress, red cell age and malarial parasite activity in thalassaemic RBC. Using a flow cytometric method to assess lipid peroxidation, we have shown that the age-related increase in sensitivity to oxidative stress previously demonstrated in normal RBC also occurs in thalassaemic RBC. Invasion and growth of Plasmodium falciparum was also shown to deteriorate with increasing RBC age. This effect was more pronounced in thalassaemic RBC with associated schizont maturation arrest and abnormal parasite morphology. In addition, there was a slight but consistent inverse correlation between sensitivity to oxidant stress and parasite activity (R=−0·43; P=0·03 for normal RBC and R=−0·42; P=0·01 for thalassaemic RBC). Our findings indicate an association between red cell age, oxidant stress and P. falciparum growth, providing further support for the role of oxidant stress in mediating the protective effect against malaria in thalassaemic RBC.

FACTORS INFLUENCING THE NUTRITIONAL VALUE OF FISH FLOUR: III. FURTHER STUDIES ON AVAILABILITY OF AMINO ACIDS

1963 ◽  
Vol 41 (1) ◽  
pp. 1589-1594 ◽  
Author(s):  
A. B. Morrison
Keyword(s):  
Amino Acids ◽  
Nutritional Value ◽  
Chloride Content ◽  
In Vitro Digestion ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Deficient Diet ◽  
Weight Gains ◽  
Flour Sample

Weight gains of male weanling rats given fish flour sample X were significantly increased by addition to the diet of methionine, histidine, threonine, and tryptophan. When histidine or methionine were omitted from the amino acid mixture, weight gains were similar to those found with the unsupplemented flour, and the combination of methionine and histidine was as effective as the four amino acids. Supplements of histidine and methionine had no effect on weight gains of rats given fish flour sample CFF, which was of high nutritional value. Sample X contained methionine in an amount similar to that of sample CFF, and somewhat less histidine. The amounts of methionine and histidine released during in vitro digestion with pancreatin were much less for sample X than for sample CFF. Steaming sample X for 30 minutes significantly increased its gross protein value determined in a methionine-deficient diet, but had no effect on the total or organic chloride content. It was concluded that sample X contained unavailable methionine and histidine.

scholarly journals Localization of ferrochelatase in Plasmodium falciparum

2004 ◽  
Vol 384 (2) ◽  
pp. 429-436 ◽  
Author(s):  
Sundaramurthy VARADHARAJAN ◽  
B. K. Chandrashekar SAGAR ◽  
Pundi N. RANGARAJAN ◽  
Govindarajan PADMANABAN
Keyword(s):  
Plasmodium Falciparum ◽  
De Novo ◽  
Enzymic Activity ◽  
Malarial Parasite ◽  
Parasite Genome ◽  
Marker Proteins ◽  
Parasite Plasmodium ◽  
Theoretical Predictions ◽  
Parasite Plasmodium Falciparum

Our previous studies have demonstrated de novo haem biosynthesis in the malarial parasite (Plasmodium falciparum and P. berghei). It has also been shown that the first enzyme of the pathway is the parasite genome-coded ALA (δ-aminolaevulinate) synthase localized in the parasite mitochondrion, whereas the second enzyme, ALAD (ALA dehydratase), is accounted for by two species: one species imported from the host red blood cell into the parasite cytosol and another parasite genome-coded species in the apicoplast. In the present study, specific antibodies have been raised to PfFC (parasite genome-coded ferrochelatase), the terminal enzyme of the haem-biosynthetic pathway, using recombinant truncated protein. With the use of these antibodies as well as those against the hFC (host red cell ferrochelatase) and other marker proteins, immunofluorescence studies were performed. The results reveal that P. falciparum in culture manifests a broad distribution of hFC and a localized distribution of PfFC in the parasite. However, PfFC is not localized to the parasite mitochondrion. Immunoelectron-microscopy studies reveal that PfFC is indeed localized to the apicoplast, whereas hFC is distributed in the parasite cytoplasm. These results on the localization of PfFC are unexpected and are at variance with theoretical predictions based on leader sequence analysis. Biochemical studies using the parasite cytosolic and organellar fractions reveal that the cytosol containing hFC accounts for 80% of FC enzymic activity, whereas the organellar fraction containing PfFC accounts for the remaining 20%. Interestingly, both the isolated cytosolic and organellar fractions are capable of independent haem synthesis in vitro from [4-14C]ALA, with the cytosol being three times more efficient compared with the organellar fraction. With [2-14C]glycine, most of the haem is synthesized in the organellar fraction. Thus haem is synthesized in two independent compartments: in the cytosol, using the imported host enzymes, and in the organellar fractions, using the parasite genome-coded enzymes.

scholarly journals Effect of co-ingestion of amino acids with rice on glycaemic and insulinaemic response

2015 ◽  
Vol 114 (11) ◽  
pp. 1845-1851 ◽  
Author(s):  
Yean Yean Soong ◽  
Joseph Lim ◽  
Lijuan Sun ◽  
Christiani Jeyakumar Henry
Keyword(s):  
Amino Acids ◽  
Blood Glucose ◽  
Amino Acid ◽  
Glycaemic Index ◽  
Amino Acid Mixture ◽  
Postprandial Blood Glucose ◽  
Acid Mixture ◽  
White Rice ◽  
Amino Acid Mixtures

AbstractConsumption of high glycaemic index (GI) and glycaemic response (GR) food such as white rice has been implicated in the development of type 2 diabetes. Previous studies have reported the ability of individual amino acids to reduce GR of carbohydrate-rich foods. Because of the bitter flavour of amino acids, they have rarely been used to reduce GR. We now report the use of a palatable, preformed amino acid mixture in the form of essence of chicken. In all, sixteen healthy male Chinese were served 68 or 136 ml amino acid mixture together with rice, or 15 or 30 min before consumption of white rice. Postprandial blood glucose and plasma insulin concentrations were measured at fasting and every 15 min after consumption of the meal until 60 min after the consumption of the white rice. Subsequent blood samples were taken at 30-min intervals until 210 min. The co-ingestion of 68 ml of amino acid mixture with white rice produced the best results in reducing the peak blood glucose and GR of white rice without increasing the insulinaemic response. It is postulated that amino acid mixtures prime β-cell insulin secretion and peripheral tissue uptake of glucose. The use of ready-to-drink amino acid mixtures may be a useful strategy for lowering the high-GI rice diets consumed in Asia.

Liver extract and its free amino acids equally stimulate gastric acid secretion

1980 ◽  
Vol 239 (6) ◽  
pp. G493-G496 ◽  
Author(s):  
E. J. Feldman ◽  
M. I. Grossman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Secretion ◽  
Gastric Acid Secretion ◽  
Free Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Liver Extract ◽  
Amino Acid Mixture ◽  
Acid Mixture

Using intragastric titration in dogs with gastric fistulas, dose-response studies were carried out with liver extract and with a mixture of amino acids that matched the free amino acids found in liver extract. All solutions were adjusted to pH 7.0 and osmolality to 290 mosmol x kg-1. Doses are expressed as the sum of the concentrations of all free amino acids. At each dose studied (free amino acid concentration: 2.8, 5.6, 11, 23, and 45 mM), acid secretion in response to the free amino acid mixture was not significantly different from that of liver extract. The peak response to both liver extract and the free amino acid mixture occurred with the 23-mM dose and represented about 60% of the maximal response to histamine. The serum concentrations of gastrin after liver extract and the amino acid mixture were not significantly different. It is concluded that in dogs with gastric fistula, gastric acid secretion and release of gastrin were not significantly different in response to liver extract and to a mixture of amino acids that simulated the free amino acid content of liver extract.

An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein

1997 ◽  
Vol 273 (1) ◽  
pp. E122-E129 ◽  
Author(s):  
G. Biolo ◽  
K. D. Tipton ◽  
S. Klein ◽  
R. R. Wolfe
Keyword(s):  
Amino Acids ◽  
Blood Flow ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Protein Kinetics ◽  
Amino Acid Infusion

Six normal untrained men were studied during the intravenous infusion of a balanced amino acid mixture (approximately 0.15 g.kg-1.h-1 for 3 h) at rest and after a leg resistance exercise routine to test the influence of exercise on the regulation of muscle protein kinetics by hyperaminoacidemia. Leg muscle protein kinetics and transport of selected amino acids (alanine, phenylalanine, leucine, and lysine) were isotopically determined using a model based on arteriovenous blood samples and muscle biopsy. The intravenous amino acid infusion resulted in comparable increases in arterial amino acid concentrations at rest and after exercise, whereas leg blood flow was 64 +/- 5% greater after exercise than at rest. During hyperaminoacidemia, the increases in amino acid transport above basal were 30-100% greater after exercise than at rest. Increases in muscle protein synthesis were also greater after exercise than at rest (291 +/- 42% vs. 141 +/- 45%). Muscle protein breakdown was not significantly affected by hyperminoacidemia either at rest or after exercise. We conclude that the stimulatory effect of exogenous amino acids on muscle protein synthesis is enhanced by prior exercise, perhaps in part because of enhanced blood flow. Our results imply that protein intake immediately after exercise may be more anabolic than when ingested at some later time.

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