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Amino Acids - Current Research Articles


 
Current research articles about the chemistry of the amino acids published in online journals.

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On this page considered biochemistry journals:


Amino Acids - published by Springer -
... publishes contributions from all fields of amino acid and protein research: analysis, separation, synthesis, biosynthesis, cross linking amino acids, racemization/enantiomers, modification of amino acids as phosphorylation, methylation, acetylation, glycosylation and nonenzymatic glycosylation, new roles for amino acids in physiology and pathophysiology, biology, amino acid analogues and derivatives, polyamines, radiated amino acids, peptides, stable isotopes and isotopes of amino acids. Applications in medicine, food chemistry, nutrition, gastroenterology, nephrology, neurochemistry, pharmacology, excitatory amino acids are just some of the topics covered.



Current research articles of the mentioned journals:


Dietary l -arginine supplementation alleviates immunosuppression induced by cyclophosphamide in weaned pigs

Abstract  A study was conducted to investigate the effects of l-arginine (Arg) on performance and immune function in cyclophosphamide (CY) immunosuppressed weaned pigs. The weaned pigs were allotted randomly into one of three treatments, including: (1) non-challenged control; (2) CY-challenged group; and (3) CY + 0.5% Arg. On days 14 and 21 of the trial, pigs were injected with CY or sterile saline. Blood samples were obtained on days 21 and 28 of the trial for further analysis. On day 28, delayed-type hypersensitivity reaction was evaluated. Arg alleviated the decrease of average daily gain (P < 0.05) induced by CY challenge from days 21 to 28. Arg mitigated the CY-induced decrease of total white blood cell numbers (P < 0.05) on day 28 and improved the lymphocyte percentage on day 21 (P < 0.05). Arg increased the delayed-type hypersensitivity reaction (P < 0.05), and attenuated the decrease of bovine serum albumin antibody level caused by CY treatment (P < 0.05) on day 28. In addition, Arg elevated the levels of serum interleukin-2 and interferon-γ (P < 0.05) on day 28, and mitigated the decrease of serum interferon-γ level on day 21 (P < 0.05). These results indicate that Arg supplementation has beneficial effects in attenuating the immunosuppressive effects of CY challenge, therefore improving growth performance of young pigs.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0184-9
  • Authors
    • J. Han, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • Y. L. Liu, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • W. Fan, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • J. Chao, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • Y. Q. Hou, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • Y. L. Yin, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • H. L. Zhu, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • G. Q. Meng, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • Z. Q. Che, Wuhan Polytechnic University Hubei Key Laboratory of Animal Nutrition and Feed Science Changqing Garden 430023 Wuhan Hubei People’s Republic of China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 28 Sep 2008 | 8:43 pm CEST

Using multidimensional patterns of amino acid attributes for QSAR analysis of peptides

Abstract  On the basis of exploratory factor analysis, six multidimensional patterns of 516 amino acid attributes, namely, factor analysis scales of generalized amino acid information (FASGAI) involving hydrophobicity, alpha and turn propensities, bulky properties, compositional characteristics, local flexibility and electronic properties, are proposed to represent structures of 48 bitter-tasting dipeptides and 58 angiotensin-converting enzyme inhibitors. Characteristic parameters related to bioactivities of the peptides studied are selected by genetic algorithm, and quantitative structure–activity relationship (QSAR) models are constructed by partial least square (PLS). Our results by a leave-one-out cross validation are compared with the previously known structure representation method and are shown to give slightly superior or comparative performance. Further, two data sets are divided into training sets and test sets to validate the characterization repertoire of FASGAI. Performance of the PLS models developed by training samples by a leave-one-out cross validation and external validation for test samples are satisfying. These results demonstrate that FASGAI is an effective representation technique of peptide structures, and that FASGAI vectors have many preponderant characteristics such as straightforward physicochemical information, high characterization competence and easy manipulation. They can be further applied to investigate the relationship between structures and functions of various peptides, even proteins.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0177-8
  • Authors
    • G. Liang, Chongqing University College of Bioengineering 400030 Chongqing China
    • L. Yang, Chongqing University College of Bioengineering 400030 Chongqing China
    • L. Kang, Chongqing University College of Bioengineering 400030 Chongqing China
    • H. Mei, Chongqing University College of Bioengineering 400030 Chongqing China
    • Z. Li, Chongqing University College of Chemistry and Chemical Engineering Chongqing China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 28 Sep 2008 | 8:43 pm CEST

Chronic methionine load-induced hyperhomocysteinemia impairs the relaxation induced by bradykinin in the isolated rat carotid

Abstract  This study investigates the effects of chronic methionine intake on bradykinin (BK)-relaxation. Vascular reactivity experiments were performed on carotid rings from male Wistar rats. Treatment with methionine (0.1, 1 or 2 g kg−1 per day) for 8 and 16 weeks, but not for 2 and 4 weeks, reduced the relaxation induced by BK. Indomethacin, a non-selective cyclooxygenase (COX) inhibitor, and SQ29548, a selective thromboxane A2 (TXA2)/prostaglandin H2 (PGH2) receptor antagonist prevented the reduction in BK-relaxation observed in the carotid from methionine-treated rats. Conversely, AH6809, a selective prostaglandin F (PGF) receptor antagonist did not alter BK-relaxation in the carotid from methionine-treated rats. The nitric oxide synthase (NOS) inhibitors L-NAME, L-NNA and 7-nitroindazole reduced the relaxation induced by BK in carotids from control and methionine-treated rats. In summary, we found that chronic methionine intake impairs the endothelium-dependent relaxation induced by BK and this effect is due to an increased production of endothelial vasoconstrictor prostanoids (possibly TXA2) that counteracts the relaxant action displayed by the peptide.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0181-z
  • Authors
    • Daniella Bonaventura, University of São Paulo (USP) Laboratory of Pharmacology, Department of Physics and Chemistry, Faculty of Pharmaceutical Sciences Avenida do Café s/n Ribeirão Preto SP CEP 14040-903 Brazil
    • Carlos R. Tirapelli, University of São Paulo (USP) Laboratory of Pharmacology, Department of Psychiatry Nursing and Human Sciences, College of Nursing of Ribeirão Preto Ribeirão Preto SP Brazil
    • Ana Maria de Oliveira, University of São Paulo (USP) Laboratory of Pharmacology, Department of Physics and Chemistry, Faculty of Pharmaceutical Sciences Avenida do Café s/n Ribeirão Preto SP CEP 14040-903 Brazil
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 28 Sep 2008 | 8:43 pm CEST

d -Aspartate affects secretory activity in rat Harderian gland: molecular mechanism and functional significance

Abstract  In this paper, the role of d-aspartate in the rat Harderian gland (HG) was investigated by histochemical, ultrastructural, and biochemical analyses. In this gland, substantial amounts of endogenous d-Asp were detected, along with aspartate racemases that convert d-Asp to l-Asp and vice versa. We found that the gland was capable of uptaking and accumulating exogenously administered d-Asp. d-Asp acute treatment markedly increased lipid and porphyrin secretion and induced a powerful hyperaemia in inter-acinar interstitial tissue. Since d-Asp is known to be recognized by NMDA receptors, the expression of such receptors in rat HG led us to the hypothesis that d-Asp acute treatment induced the activation of the extracellular signal-regulated protein kinase (ERK) and nitric oxide synthase (NOS) pathways mediated by NMDA. Interestingly, as a result of enhanced oxidative stress due to increased porphyrin secretion, the revealed activation of the stress-activated protein kinase/c-jun N-terminal kinase (SAPK/JNK) pro-apoptotic pathway was probably triggered by the gland itself to preserve its cellular integrity.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0185-8
  • Authors
    • Rossella Monteforte, Seconda Università degli Studi di Napoli Dipartimento di Scienze della Vita via Vivaldi 43-81100 Caserta Italy
    • Alessandra Santillo, Seconda Università degli Studi di Napoli Dipartimento di Scienze della Vita via Vivaldi 43-81100 Caserta Italy
    • Marcello Di Giovanni, Seconda Università degli Studi di Napoli Dipartimento di Scienze della Vita via Vivaldi 43-81100 Caserta Italy
    • Antimo D’Aniello, Stazione Zoologica “A. Dohrn” villa Comunale Naples Italy
    • Antimo Di Maro, Seconda Università degli Studi di Napoli Dipartimento di Scienze della Vita via Vivaldi 43-81100 Caserta Italy
    • Gabriella Chieffi Baccari, Seconda Università degli Studi di Napoli Dipartimento di Scienze della Vita via Vivaldi 43-81100 Caserta Italy
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 27 Sep 2008 | 4:06 pm CEST

Regulation of muscle protein degradation, not synthesis, by dietary leucine in rats fed a protein-deficient diet

Abstract  The aim of this study was to elucidate the effects of long-term intake of leucine in dietary protein malnutrition on muscle protein synthesis and degradation. A reduction in muscle mass was suppressed by leucine-supplementation (1.5% leucine) in rats fed protein-free diet for 7 days. Furthermore, the rate of muscle protein degradation was decreased without an increase in muscle protein synthesis. In addition, to elucidate the mechanism involved in the suppressive effect of leucine, we measured the activities of degradation systems in muscle. Proteinase activity (calpain and proteasome) and ubiquitin ligase mRNA (Atrogin-1 and MuRF1) expression were not suppressed in animals fed a leucine-supplemented diet, whereas the autophagy marker, protein light chain 3 active form (LC3-II), expression was significantly decreased. These results suggest that the protein-free diet supplemented with leucine suppresses muscle protein degradation through inhibition of autophagy rather than protein synthesis.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0180-0
  • Authors
    • Takayuki Sugawara, Iwate University United Graduate School of Agricultural Sciences Morioka, Iwate 020-8550 Japan
    • Yoshiaki Ito, Iwate University Biological Chemistry and Food Science, Faculty of Agriculture Morioka, Iwate 020-8550 Japan
    • Naoyuki Nishizawa, Iwate University Biological Chemistry and Food Science, Faculty of Agriculture Morioka, Iwate 020-8550 Japan
    • Takashi Nagasawa, Iwate University Biological Chemistry and Food Science, Faculty of Agriculture Morioka, Iwate 020-8550 Japan
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 12 Sep 2008 | 9:48 am CEST

The level of sulfane sulfur in the fungus Aspergillus nidulans wild type and mutant strains

Abstract  The interdependence of the sulfane sulfur metabolism and sulfur amino acid metabolism was studied in the fungus Aspergillus nidulans wild type strain and in mutants impaired in genes encoding enzymes involved in the synthesis of cysteine (a precursor of sulfane sulfur) or in regulatory genes of the sulfur metabolite repression system. It was found that a low concentration of cellular cysteine leads to elevation of two sulfane sulfurtransferases, rhodanase and cystathionine γ-lyase, while the level of 3-mercaptopyruvate sulfurtransferase remains largely unaffected. In spite of drastic differences in the levels of biosynthetic enzymes and of sulfur amino acids due to mutations or sulfur supplementation of cultures, the level of total sulfane sulfur is fairly stable. This stability confirms the crucial role of sulfane sulfur as a fine-tuning regulator of cellular metabolism.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0175-x
  • Authors
    • Maria Wróbel, Jagiellonian University Chair of Medical Biochemistry, Collegium Medicum Kopernika 7 31-034 Cracow Poland
    • Irmina Lewandowska, PAS Institute of Biochemistry and Biophysics Pawinskiego 5A 02-106 Warsaw Poland
    • Patrycja Bronowicka-Adamska, Jagiellonian University Chair of Medical Biochemistry, Collegium Medicum Kopernika 7 31-034 Cracow Poland
    • Andrzej Paszewski, PAS Institute of Biochemistry and Biophysics Pawinskiego 5A 02-106 Warsaw Poland
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 10 Sep 2008 | 10:39 am CEST

Dietary supplementation with Chinese herbal powder enhances ileal digestibilities and serum concentrations of amino acids in young pigs

Abstract  This study was designed to determine the effect of ultra-fine Chinese herbal powder as a dietary additive on serum concentrations and apparent ileal digestibilities (AID) of amino acids (AA) in young pigs. In Experiment 1, 60 Duroc × Landrace × Yorkshire piglets weaned at 21 days of age were randomly assigned to one of three treatments, representing supplementation with 0 or 2 g/kg of the powder, or 0.2 g/kg of colistin (an antibiotic) to corn- and soybean meal-based diets (n = 20 per group). Blood samples from five piglets per group were collected on days 7, 14, and 28 to determine serum AA concentrations. In Experiment 2, 12 barrows with an average initial body weight of 7.64 kg were randomly assigned to one of the three dietary treatments, followed by surgical placement of a simple T-cannula at the terminal ileum. All of the diets contained 0.1% titanium oxide as a digestibility marker. The samples of terminal ileal digesta were collected on day 7 for determining AID of AA. Results show that dietary supplementation with the herbal powder increased (P < 0.05) serum concentrations and AID of most AA by 10–50% and 10–16%, respectively. As an indicator of improved intestinal function, AID values of calcium were also enhanced in piglets supplemented with the herbal powder. Dietary supplementation of colistin increased serum concentrations and AID values of some AA by 8–44% and 10–15%, respectively, in comparison with the non-supplemented group. These novel findings demonstrate that the herbal powder can enhance the digestibility of dietary protein and the intestinal absorption of AA into the systemic circulation in post-weaning pigs, therefore providing a new mechanism for its growth- and immunity-promoting efficacy.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0176-9
  • Authors
    • X. F. Kong, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • Y. L. Yin, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • Q. H. He, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • F. G. Yin, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • H. J. Liu, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • T. J. Li, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • R. L. Huang, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • M. M. Geng, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • Z. Ruan, Nanchang University State Key Laboratory of Food Science and Technology 330047 Nanchang Jiangxi China
    • Z. Y. Deng, Nanchang University State Key Laboratory of Food Science and Technology 330047 Nanchang Jiangxi China
    • M. Y. Xie, Nanchang University State Key Laboratory of Food Science and Technology 330047 Nanchang Jiangxi China
    • G. Wu, Institute of Subtropical Agriculture, the Chinese Academy of Sciences Key Laboratory of Animal Nutrition Metabolism and Regulation 410125 Changsha Hunan China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 2 Sep 2008 | 9:41 am CEST

New developments in fish amino acid nutrition: towards functional and environmentally oriented aquafeeds

Abstract  Recent evidence shows that some amino acids and their metabolites are important regulators of key metabolic pathways that are necessary for maintenance, growth, feed intake, nutrient utilization, immunity, behavior, larval metamorphosis, reproduction, as well as resistance to environmental stressors and pathogenic organisms in various fishes. Therefore, conventional definitions on essential and nonessential amino acids for fish are challenged by numerous discoveries that taurine, glutamine, glycine, proline and hydroxyproline promote growth, development, and health of aquatic animals. On the basis of their crucial roles in cell metabolism and physiology, we anticipate that dietary supplementation with specific amino acids may be beneficial for: (1) increasing the chemo-attractive property and nutritional value of aquafeeds with low fishmeal inclusion; (2) optimizing efficiency of metabolic transformation in juvenile and sub-adult fishes; (3) surpressing aggressive behaviors and cannibalism; (4) increasing larval performance and survival; (5) mediating timing and efficiency of spawning; (6) improving fillet taste and texture; and (7) enhancing immunity and tolerance to environmental stresses. Functional amino acids hold great promise for development of balanced aquafeeds to enhance the efficiency and profitability of global aquaculture production.

  • Content Type Journal Article
  • Category Review Article
  • DOI 10.1007/s00726-008-0171-1
  • Authors
    • Peng Li, Texas A&M University Department of Animal Science College Station TX 77843-2471 USA
    • Kangsen Mai, Ocean University of China The Key Laboratory of Mariculture (Ministry of Education) 5 Yushan Rd Qingdao 266003 People’s Republic of China
    • Jesse Trushenski, Southern Illinois University Fisheries and Aquaculture Center Carbondale IL 62901-6501 USA
    • Guoyao Wu, Texas A&M University Department of Animal Science College Station TX 77843-2471 USA
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 27 Aug 2008 | 5:25 pm CEST

Side-chain oxidative damage to cysteine on a glassy carbon electrode

Abstract  In this paper, oxidative damage to the cysteine (CySH) side-chain on a glassy carbon electrode (GCE) was investigated. Voltammetric studies show that there are three anodic peaks for the oxidation of CySH, which arise from (1) the oxidation of the –SH side-chain, forming cystine (0.71 V, vs. SCE) and (2) CySO x H, x = 2, 3 (0.98 V vs. SCE), and (3) the oxidation of the amino acid carboxyl group (around 1.51 V vs. SCE). The influence of dissolved oxygen, pH, scan rate, scan time, temperature and CySH concentration were investigated and the oxidative mechanism proposed. The peaks near 0.71 and 0.98 V are the promising candidates for measuring the oxidation of CySH on the GCE. This paper provides a new strategy for researching oxidative damage of amino acids, sulfur-containing peptides and proteins.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0173-z
  • Authors
    • Wansong Zong, Shandong University School of Environmental Science and Engineering 27# Shanda South Road 250100 Jinan People’s Republic of China
    • Rutao Liu, Shandong University School of Environmental Science and Engineering 27# Shanda South Road 250100 Jinan People’s Republic of China
    • Lingzi Zhao, Shandong University School of Environmental Science and Engineering 27# Shanda South Road 250100 Jinan People’s Republic of China
    • Yanmin Tian, Shandong University School of Environmental Science and Engineering 27# Shanda South Road 250100 Jinan People’s Republic of China
    • Dong Yuan, Shandong University School of Environmental Science and Engineering 27# Shanda South Road 250100 Jinan People’s Republic of China
    • Canzhu Gao, Shandong University School of Environmental Science and Engineering 27# Shanda South Road 250100 Jinan People’s Republic of China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 25 Aug 2008 | 3:37 pm CEST

Glutamate is the chemotaxis-inducing factor in placental extracts

Abstract  Human placental extracts are known to help wound healing. Rapid migration of neutrophils to the wound site is a prerequisite to the wound healing process. Gel filtration analysis of heat-treated placental extract gave the initial cue to the small nature of the migration promoting factor of the extract. HPLC analysis of the extract revealed glutamate to be the predominant free amino acid. Our studies show that glutamate at an optimum concentration of 8 μM induced phenotypic neutrophil chemotaxis, as seen in the time lapse and transwell assays. Glutamate was also found to induce chemokinesis of the neutrophil, though the stimulation of chemotaxis was more pronounced. The glutamate induced chemotaxis was accompanied by polarization of the actin cytoskeleton, and by polymerization of F-actin. These data indicate that glutamate has a strong chemotactic functionality in the neutrophil, which could be of interest both therapeutically and in further investigation of the molecular basis of chemotaxis.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0162-2
  • Authors
    • Rahul Gupta, University of Calcutta Department of Biochemistry, Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology 35 Ballygunje Circular Road Kolkata 700 019 West Bengal India
    • Dhrubajyoti Chattopadhyay, University of Calcutta Department of Biochemistry, Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology 35 Ballygunje Circular Road Kolkata 700 019 West Bengal India
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 24 Aug 2008 | 6:54 pm CEST

Prediction of protein structural classes by Chou’s pseudo amino acid composition: approached using continuous wavelet transform and principal component analysis

Abstract  A prior knowledge of protein structural classes can provide useful information about its overall structure, so it is very important for quick and accurate determination of protein structural class with computation method in protein science. One of the key for computation method is accurate protein sample representation. Here, based on the concept of Chou’s pseudo-amino acid composition (AAC, Chou, Proteins: structure, function, and genetics, 43:246–255, 2001), a novel method of feature extraction that combined continuous wavelet transform (CWT) with principal component analysis (PCA) was introduced for the prediction of protein structural classes. Firstly, the digital signal was obtained by mapping each amino acid according to various physicochemical properties. Secondly, CWT was utilized to extract new feature vector based on wavelet power spectrum (WPS), which contains more abundant information of sequence order in frequency domain and time domain, and PCA was then used to reorganize the feature vector to decrease information redundancy and computational complexity. Finally, a pseudo-amino acid composition feature vector was further formed to represent primary sequence by coupling AAC vector with a set of new feature vector of WPS in an orthogonal space by PCA. As a showcase, the rigorous jackknife cross-validation test was performed on the working datasets. The results indicated that prediction quality has been improved, and the current approach of protein representation may serve as a useful complementary vehicle in classifying other attributes of proteins, such as enzyme family class, subcellular localization, membrane protein types and protein secondary structure, etc.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0170-2
  • Authors
    • Zhan-Chao Li, Sun Yat-Sen University School of Chemistry and Chemical Engineering Guangzhou People’s Republic of China
    • Xi-Bin Zhou, Sun Yat-Sen University School of Chemistry and Chemical Engineering Guangzhou People’s Republic of China
    • Zong Dai, Sun Yat-Sen University School of Chemistry and Chemical Engineering Guangzhou People’s Republic of China
    • Xiao-Yong Zou, Sun Yat-Sen University School of Chemistry and Chemical Engineering Guangzhou People’s Republic of China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 24 Aug 2008 | 6:54 pm CEST

A complexity-based method for predicting protein subcellular location

Abstract  A complexity-based approach is proposed to predict subcellular location of proteins. Instead of extracting features from protein sequences as done previously, our approach is based on a complexity decomposition of symbol sequences. In the first step, distance between each pair of protein sequences is evaluated by the conditional complexity of one sequence given the other. Subcellular location of a protein is then determined using the k-nearest neighbor algorithm. Using three widely used data sets created by Reinhardt and Hubbard, Park and Kanehisa, and Gardy et al., our approach shows an improvement in prediction accuracy over those based on the amino acid composition and Markov model of protein sequences.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0172-0
  • Authors
    • Xiaoqi Zheng, Dalian University of Technology Department of Applied Mathematics 116024 Dalian China
    • Taigang Liu, Dalian University of Technology College of Advanced Science and Technology 116024 Dalian China
    • Jun Wang, Dalian University of Technology College of Advanced Science and Technology 116024 Dalian China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 22 Aug 2008 | 11:27 am CEST

Mutant rat strain lacking d -amino-acid oxidase

Abstract   d-Amino-acid oxidase (DAO) is known to be associated with schizophrenia. Since the expression of DAO gene had been reported to be very low in LEA rats, we examined LEA/SENDAI rats in detail. These rats did not have DAO activity, enzyme protein or mRNA encoding this enzyme. Sequencing of the 5′-upstream region of the DAO gene revealed the deletion of one triplet in the 15 TAA repeats approximately 700-bp upstream of the transcription start point. A 1.3-kb upstream fragment containing the TAA repeats and the transcription start point was inserted into a reporter vector and was transfected into COS-1, NRK-52E and CCL-PK1 cells. Although the fragments containing 15 or 14 repeats had high promoter activity, the fragment containing 13 repeats had very weak activity. Electrophoretic mobility-shift assays showed that the nuclear extracts from COS-1 and COS-7 cells had proteins that bound to the oligonucleotides containing the TAA repeats. These results suggest that the TAA repeats are important for expression of the DAO gene. The LEA/SENDAI rats lacking DAO would be a useful tool for the investigations aimed at the elucidation of the relationships between this flavoenzyme and schizophrenia.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0163-1
  • Authors
    • Ryuichi Konno, International University of Health and Welfare Center for Medical Science Kitakanemaru Ohtawara Tochigi 324-8501 Japan
    • Tadashi Okamura, Research Institute, International Medical Center of Japan Division of Animal Models, Department of Infectious Diseases Tokyo Japan
    • Noriyuki Kasai, Institute for Animal Experimentation, Tohoku University Graduate School of Medicine Sendai Japan
    • Karl H. Summer, Institute of Toxicology, GSF-National Research Center for Environment and Health Neuherberg Germany
    • Akira Niwa, International University of Health and Welfare Center for Medical Science Kitakanemaru Ohtawara Tochigi 324-8501 Japan
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 21 Aug 2008 | 11:27 am CEST

Dietary l -arginine supplementation enhances the immune status in early-weaned piglets

Abstract  This study was conducted to test the hypothesis that dietary L-arginine supplementation enhances immunity in early weaned piglets. Seventy piglets weaned at 7 days of age were assigned to five groups (14 pigs/group), representing supplementation of 0.0, 0.2, 0.4, 0.6, and 0.8% l-arginine to a milk-based formula. On Day 7 after initiation of treatment, spleen weight in piglets supplemented with 0.2 and 0.8% arginine was heavier and thymus size was larger in piglets supplemented with 0.6% arginine, whereas serum concentration of immunoglobulin (Ig) M was higher but that of IL-8 was lower in piglets supplemented with 0.6 and 0.8% arginine, compared with the control group. Dietary supplementation with 0.8% arginine increased the numbers of white blood cells and granulocytes, and gene expression of interleukin (IL)-8 in spleen. On Day 14, compared with control piglets, granulocyte numbers were greater but lymphocyte numbers were lower in piglets supplemented with 0.2 and 0.4% arginine, whereas splenic expression of IL-8 and tumor necrosis factor-α genes was increased in piglets supplemented with 0.8% arginine. Additionally, IgG and IgM concentrations in serum and growth performance were greater in piglets supplemented with 0.4–0.8% arginine, compared with unsupplemented piglets. Collectively, dietary supplementation with 0.4–0.8% l-arginine for 2 weeks enhances both cellular and humoral immunity in piglets by modulating the production of leukocytes, cytokines and antibodies. These results indicate that increasing l-arginine provision is beneficial for optimal immune responses in young pigs and also have important implications for designing the next generation of improved formula for human infants.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0155-1
  • Authors
    • Bie Tan, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Xinguo G. Li, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Xiangfeng Kong, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Ruilin Huang, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Zheng Ruan, Nanchang University Key Laboratory of Food Science of The Ministry of Education, Department of Food Science and Engineering 330047 Nanchang China
    • Kang Yao, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Zeyuan Deng, Nanchang University Key Laboratory of Food Science of The Ministry of Education, Department of Food Science and Engineering 330047 Nanchang China
    • Mingyong Xie, Nanchang University Key Laboratory of Food Science of The Ministry of Education, Department of Food Science and Engineering 330047 Nanchang China
    • Izuru Shinzato, Ajinomoto Inc Department of Animal Nutrition Tokyo 104-8135 Japan
    • Yulong Yin, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Guoyao Wu, The Chinese Academy of Sciences Laboratory of Animal Nutrition and Health, Institute of Subtropical Agriculture 410125 Changsha Hunan China
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 19 Aug 2008 | 7:22 pm CEST

Altered urinary polyamine patterns of cancer patients under acupuncture therapy

Abstract  The reduction of elevated polyamine (PA) levels in biological fluids of cancer patients were known to be correlated with remission following diverse therapeutic treatments. In this study, altered urinary PA levels from three different cancer cases were monitored at different intervals during the long-term weekday acupuncture treatments. Nine urinary PA levels from 16 normal and three cancer patients with different types were measured by gas chromatography–mass spectrometry in selected ion monitoring mode as N-ethoxycarbonyl-N-pentafluoropropionyl derivatives. Their levels measured at three follow-up stages for each patient were then normalized to the corresponding normal group means and plotted into star symbol patterns. Large alterations of PA levels were observed for each patient. Each normalized concentration displayed elevation of the PA levels in multiples (0.0–57.7) of the respective normal mean values. The normalized PA values were transformed into distorted star patterns which were characteristic of each follow-up stage and of cancer type.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0169-8
  • Authors
    • M. J. Paik, School of Medicine, Ajou University Metabolomic Analysis Laboratory, Institute for Neuroregeneration and Stem Cell Research Suwon 443-721 Republic of Korea
    • D. Kuon, Jaesun Acupuncture Clinics and Dawnting Cancer Research Institute Seoul 100-823 Republic of Korea
    • J. Cho, Sookmyung Women’s University Analytical Chemometrics Laboratory, College of Pharmacy Seoul 140-742 Republic of Korea
    • K.-R. Kim, Sungkyunkwan University Biometabolite Analysis Laboratory, College of Pharmacy Suwon 440-746 Republic of Korea
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 19 Aug 2008 | 7:22 pm CEST

A conceptual model of the polyamine binding site of N 1-acetylpolyamine oxidase developed from a study of polyamine derivatives

Abstract  We used various polyamine derivatives to study the substrate binding site of N 1-acetylpolyamine oxidase (PAO) that was partially purified from rat liver. The substrate activities of acetylpolyamines indicated the presence of two anionic centers corresponding to the 1,3-diaminopropane (1,3-DAP) structure and a hydrophobic region in addition to the cleavage site of the acetamidopropyl group. Based on the results of the inhibitory activities of 1,3-DAP derivatives, we developed a conceptual model of the polyamine binding site of PAO. We used this model to identify a potent competitive inhibitor, N 1,N 7-dihexyl-1,7-diamino-4-azaheptane, and to develop an affinity column, 1,16-diamino4,13-diazahexadecane–linked Sepharose, which was useful for the purification of PAO.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0168-9
  • Authors
    • Koichi Takao, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Satoko Shibata, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Tomohiro Ozawa, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Makiko Wada, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Yoshiaki Sugitia, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Keijiro Samejima, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Akira Shirahata, Josai University Faculty of Pharmaceutical Sciences 1-1 Keyakidai Sakado Saitama 350-0295 Japan
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 19 Aug 2008 | 7:22 pm CEST

Comment on “Cleavage mechanism of the H5N1 hemagglutinin by trypsin and furin” [Amino Acids 2008, January 31, Doi: 10.1007/s00726-007-0611-3]

Summary.  Recently, Guo et al. have reported structural as well as the binding energy data of the particular interactions between the cleavage sites of hemagglutinin and serine proteases, trypsin and furin, using molecular docking approach. Due to a wrong assignment of protonation state on the histidine, one of the catalytic triad in the active site of both enzymes, their docking results are contradictory with the fundamental principle and previous theoretical studies of the known cleavage mechanism in serine proteases.

  • Content Type Journal Article
  • DOI 10.1007/s00726-008-0638-0
  • Authors
    • T. Rungrotmongkol, Chulalongkorn University Department of Chemistry, Faculty of Science Patumwan Bangkok Thailand
    • P. Decha, Chulalongkorn University Department of Chemistry, Faculty of Science Patumwan Bangkok Thailand
    • M. Malaisree, Chulalongkorn University Department of Chemistry, Faculty of Science Patumwan Bangkok Thailand
    • P. Sompornpisut, Chulalongkorn University Department of Chemistry, Faculty of Science Patumwan Bangkok Thailand
    • S. Hannongbua, Chulalongkorn University Department of Chemistry, Faculty of Science Patumwan Bangkok Thailand

Source: Amino Acids | 15 Aug 2008 | 8:45 am CEST

l -Proline is a sedative regulator of acute stress in the brain of neonatal chicks

Abstract  The purpose of the present study was to clarify the central nervous system function of amino acids during acute stress. In Experiment 1, changes in free amino acid pattern were investigated in the brain of neonatal chicks exposed to either restraint with isolation-induced or fasting stress. l-Proline and l-arginine were decreased in the telencephalon and diencephalon under any stress. Since the central nervous system functions of l-arginine during the stress response has recently been reported, in Experiment 2, the effect of intracerebroventricular injection of l-proline (0.5, 1.0, 2.0 μmol) during isolation-induced stress was investigated. l-Proline induced sedative and hypnotic effects in a dose-dependent manner. It is suggested that l-proline may have an important role to attenuate the stress response in the central nervous system of chicks.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0164-0
  • Authors
    • K. Hamasu, Kyushu University Laboratory of Advanced Animal and Marine Bioresources, Graduate School of Bioresource and Bioenvironmental Sciences Fukuoka 812-8581 Japan
    • T. Haraguchi, Kyushu University Laboratory of Advanced Animal and Marine Bioresources, Graduate School of Bioresource and Bioenvironmental Sciences Fukuoka 812-8581 Japan
    • Y. Kabuki, Kyushu University Laboratory of Advanced Animal and Marine Bioresources, Graduate School of Bioresource and Bioenvironmental Sciences Fukuoka 812-8581 Japan
    • N. Adachi, Kyushu University Laboratory of Advanced Animal and Marine Bioresources, Graduate School of Bioresource and Bioenvironmental Sciences Fukuoka 812-8581 Japan
    • S. Tomonaga, Kyushu University Laboratory of Advanced Animal and Marine Bioresources, Graduate School of Bioresource and Bioenvironmental Sciences Fukuoka 812-8581 Japan
    • H. Sato, Ajinomoto Co., Inc Kawasaki-ku Kawasaki 210-8681 Japan
    • D. M. Denbow, Virginia Polytechnic Institute and State University Department of Animal and Poultry Sciences Blacksburg VA 24061-0306 USA
    • M. Furuse, Kyushu University Laboratory of Advanced Animal and Marine Bioresources, Graduate School of Bioresource and Bioenvironmental Sciences Fukuoka 812-8581 Japan
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 12 Aug 2008 | 9:35 am CEST

Protein–polyamine conjugates by transglutaminase 2 as potential markers for antineoplastic screening of natural compounds

Abstract  The role of post-translational modification of cell proteins with polyamines, a reaction catalyzed by a tissue tranglutaminase (TG, EC 2.3.2.13), in the induction of cell differentiation, represents an intriguing strategy to control cell proliferation and metastatic ability of different tumor cell lines. In this review, we focus our attention on the metabolic aspects of some natural compounds (methylxantines, retinoids and flavonoids) responsible of their antitumor effects exerted through the induction of TG activity in cancer cells.

  • Content Type Journal Article
  • Category Review Article
  • DOI 10.1007/s00726-008-0157-z
  • Authors
    • A. Lentini, University “Tor Vergata” Department of Biology Via della Ricerca Scientifica 00133 Rome Italy
    • B. Provenzano, University “Tor Vergata” Department of Biology Via della Ricerca Scientifica 00133 Rome Italy
    • C. Tabolacci, University “Tor Vergata” Department of Biology Via della Ricerca Scientifica 00133 Rome Italy
    • S. Beninati, University “Tor Vergata” Department of Biology Via della Ricerca Scientifica 00133 Rome Italy
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 12 Aug 2008 | 9:35 am CEST

Unfolding studies of tissue transglutaminase

Abstract  Activation of tissue transglutaminase by calcium involves a conformational change which allows exposition of the active site to the substrate via movements of domains 3 and 4 that lead to an increase of the inter-domain distance. The inhibitor GTP counteracts these changes. Here we investigate the possible existence of non-native conformational states still compatible with the enzyme activity produced by chemical and thermal perturbations. The results indicate that chemical denaturation is reversible at low guanidine concentrations but irreversible at high concentrations of guanidine. Indeed, at low guanidine concentrations tissue TG-ase exists in a non-native state which is still affected by the ligands as in the native form. In contrast, thermal unfolding is always irreversible, with aggregation and protein self-crosslinkage in the presence of calcium. DSC thermograms of the native protein in the absence of ligands consist of two partly overlapped transitions, which weaken in the presence of calcium and merge together and strengthen in the presence of GTP. Overall, the present work shows, for the first time, the reversible denaturation of a TG-ase isoenzyme and suggests the possibility that also in in vivo, the enzyme may acquire non-native conformations relevant to its patho-physiological functions.

  • Content Type Journal Article
  • Category Original Article
  • DOI 10.1007/s00726-008-0161-3
  • Authors
    • Carlo Cervellati, University of Ferrara Department of Biochemistry and Molecular Biology, Interdisciplinary Centre for Study of Inflammation Via L. Borsari 46 44100 Ferrara Italy
    • Lorella Franzoni, University of Parma Department of Experimental Medicine, Section of Chemistry and Structural Biochemistry Parma Italy
    • Monica Squerzanti, University of Ferrara Department of Biochemistry and Molecular Biology, Interdisciplinary Centre for Study of Inflammation Via L. Borsari 46 44100 Ferrara Italy
    • Carlo M. Bergamini, University of Ferrara Department of Biochemistry and Molecular Biology, Interdisciplinary Centre for Study of Inflammation Via L. Borsari 46 44100 Ferrara Italy
    • Francesco Spinozzi, Marche Polytechnic University Department of Applied Science for Complex Systems Ancona Italy
    • Paolo Mariani, Marche Polytechnic University Department of Applied Science for Complex Systems Ancona Italy
    • Vincenzo Lanzara, University of Ferrara Department of Biochemistry and Molecular Biology, Interdisciplinary Centre for Study of Inflammation Via L. Borsari 46 44100 Ferrara Italy
    • Alberto Spisni, University of Parma Department of Experimental Medicine, Section of Chemistry and Structural Biochemistry Parma Italy
    • Journal Amino Acids
    • Online ISSN 1438-2199
    • Print ISSN 0939-4451

Source: Amino Acids | 12 Aug 2008 | 9:35 am CEST


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