Journal of Amino AcidsPub Date : 2014-01-01Epub Date: 2014-02-20DOI: 10.1155/2014/283962
Daniel A Sáenz, Mónica S Chianelli, Carlos A Stella
{"title":"L-Phenylalanine Transport in Saccharomyces cerevisiae: Participation of GAP1, BAP2, and AGP1.","authors":"Daniel A Sáenz, Mónica S Chianelli, Carlos A Stella","doi":"10.1155/2014/283962","DOIUrl":"https://doi.org/10.1155/2014/283962","url":null,"abstract":"<p><p>We focused on the participation of GAP1, BAP2, and AGP1 in L-phenylalanine transport in yeast. In order to study the physiological functions of GAP1, BAP2, and AGP1 in L-phenylalanine transport, we examined the kinetics, substrate specificity, and regulation of these systems, employing isogenic haploid strains with the respective genes disrupted individually and in combination. During the characterization of phenylalanine transport, we noted important regulatory phenomena associated with these systems. Our results show that Agp1p is the major transporter of the phenylalanine in a gap1 strain growing in synthetic media with leucine present as an inducer. In a wild type strain grown in the presence of leucine, when ammonium ion was the nitrogen source, Bap2p is the principal phenylalanine carrier. </p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2014 ","pages":"283962"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2014/283962","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32236496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-10-24DOI: 10.1155/2013/407616
Tatyana A Dzimbova, Peter B Milanov, Tamara I Pajpanova
{"title":"Long-lasting effects of oxy- and sulfoanalogues of L-arginine on enzyme actions.","authors":"Tatyana A Dzimbova, Peter B Milanov, Tamara I Pajpanova","doi":"10.1155/2013/407616","DOIUrl":"https://doi.org/10.1155/2013/407616","url":null,"abstract":"<p><p>Arginine residues are very important for the structure of proteins and their action. Arginine is essential for many natural processes because it has unique ionizable group under physiological conditions. Numerous mimetics of arginine were synthesized and their biological effects were evaluated, but the mechanisms of actions are still unknown. The aim of this study is to see if oxy- and sulfoanalogues of arginine can be recognized by human arginyl-tRNA synthetase (HArgS)-an enzyme responsible for coupling of L-arginine with its cognate tRNA in a two-step catalytic reaction. We make use of modeling and docking studies of adenylate kinase (ADK) to reveal the effects produced by the incorporation of the arginine mimetics on the structure of ADK and its action. Three analogues of arginine, L-canavanine (Cav), L-norcanavanine (NCav), and L-sulfoarginine (sArg), can be recognized as substrates of HArgS when incorporated in different peptide and protein sequences instead of L-arginine. Mutation in the enzyme active center by arginine mimetics leads to conformational changes, which produce a decrease the rate of the enzyme catalyzed reaction and even a loss of enzymatic action. All these observations could explain the long-lasting nature of the effects of the arginine analogues. </p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"407616"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/407616","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31908077","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-02-25DOI: 10.1155/2013/979016
Francesco Merlino, Salvatore Di Maro, Ali Munaim Yousif, Michele Caraglia, Paolo Grieco
{"title":"Urotensin-II Ligands: An Overview from Peptide to Nonpeptide Structures.","authors":"Francesco Merlino, Salvatore Di Maro, Ali Munaim Yousif, Michele Caraglia, Paolo Grieco","doi":"10.1155/2013/979016","DOIUrl":"https://doi.org/10.1155/2013/979016","url":null,"abstract":"<p><p>Urotensin-II was originally isolated from the goby urophysis in the 1960s as a vasoactive peptide with a prominent role in cardiovascular homeostasis. The identification of human isoform of urotensin-II and its specific UT receptor by Ames et al. in 1999 led to investigating the putative role of the interaction U-II/UT receptor in multiple pathophysiological effects in humans. Since urotensin-II is widely expressed in several peripheral tissues including cardiovascular system, the design and development of novel urotensin-II analogues can improve knowledge about structure-activity relationships (SAR). In particular, since the modulation of the U-II system offers a great potential for therapeutic strategies related to the treatment of several diseases, like cardiovascular diseases, the research of selective and potent ligands at UT receptor is more fascinating. In this paper, we review the developments of peptide and nonpeptide U-II structures so far developed in order to contribute also to a more rational and detectable design and synthesis of new molecules with high affinity at the UT receptor.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"979016"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/979016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40229760","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"DTNQ-Pro, a Mimetic Dipeptide, Sensitizes Human Colon Cancer Cells to 5-Fluorouracil Treatment.","authors":"Isabel Gomez-Monterrey, Pietro Campiglia, Ilaria Scognamiglio, Daniela Vanacore, Alessandra Dicitore, Angela Lombardi, Michele Caraglia, Ettore Novellino, Paola Stiuso","doi":"10.1155/2013/509056","DOIUrl":"https://doi.org/10.1155/2013/509056","url":null,"abstract":"<p><p>The resistance of growing human colon cancer cells to chemotherapy agents has been correlated to endogenous overexpression of stress proteins including the family of heat shock proteins (HSPs). Previously, we have demonstrated that a quinone-based mimetic dipeptide, named DTNQ-Pro, induced differentiation of growing Caco-2 cells through inhibition of HSP70 and HSP90. In addition, our product induced a HSP27 and vimentin intracellular redistribution. In the present study, we have evaluated whether a decrease of stress proteins induced by DTNQ-Pro in Caco-2 cells could sensitize these cells to treatment with 5-fluorouracil (5-FU) cytotoxicity. The pretreatment of Caco-2 with 500 nM of DTNQ-Pro increases lipid peroxidation and decreases expression of p38 mitogen-activated protein kinase (MAPK) and FOXO3a. At the same experimental conditions, an increase of the 5-FU-induced growth inhibition of Caco-2 cells was recorded. These effects could be due to enhanced DTNQ-Pro-induced membrane lipid peroxidation that, in turn, causes the sensitization of cancer cells to the cytotoxicity mediated by 5-FU.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"509056"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/509056","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31459248","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-02-17DOI: 10.1155/2013/569527
Shamkant B Badgujar, Raghunath T Mahajan
{"title":"Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch.-Ham.","authors":"Shamkant B Badgujar, Raghunath T Mahajan","doi":"10.1155/2013/569527","DOIUrl":"https://doi.org/10.1155/2013/569527","url":null,"abstract":"<p><p>A new cysteine protease named Nivulian-II has been purified from the latex of Euphorbia nivulia Buch.-Ham. The apparent molecular mass of Nivulian-II is 43670.846 Da (MALDI TOF/MS). Peptide mass fingerprint analysis revealed peptide matches to Maturase K (Q52ZV1_9MAGN) of Banksia quercifolia. The N-terminal sequence (DFPPNTCCCICC) showed partial homology with those of other cysteine proteinases of biological origin. This is the first paper to characterize a Nivulian-II of E. nivulia latex with respect to amino acid sequencing.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"569527"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/569527","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31296157","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-11-06DOI: 10.1155/2013/872058
Janneth Gonzalez, George E Barreto
{"title":"In silico insights of L-glutamate: structural features in vacuum and in complex with its receptor.","authors":"Janneth Gonzalez, George E Barreto","doi":"10.1155/2013/872058","DOIUrl":"https://doi.org/10.1155/2013/872058","url":null,"abstract":"<p><p>Structural properties of the glutamate in vacuum and in complex with its receptor were analyzed. The analysis was focused on global properties, attempting to characterize features such as overall flexibility and common trends in the conformation set. The glutamate, as other ligands in complex with the receptor, adopts a spatial conformation that corresponds to one of the possible molecular equilibrium states in physiological conditions. The glutamate forms an extended structure for all cases, but the energy of the glutamate round out form is lower than the extended glutamate form. The results showed the glutamate as a flexible molecule, which can easily adapt to different interacting environments, and it can be considered as an approximation to address why glutamate interacts with a great number of molecules. </p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"872058"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/872058","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31928955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-02-26DOI: 10.1155/2013/606282
Ermelinda Vernieri, Isabel Gomez-Monterrey, Ciro Milite, Paolo Grieco, Simona Musella, Alessia Bertamino, Ilaria Scognamiglio, Stefano Alcaro, Anna Artese, Francesco Ortuso, Ettore Novellino, Marina Sala, Pietro Campiglia
{"title":"Design, Synthesis, and Evaluation of New Tripeptides as COX-2 Inhibitors.","authors":"Ermelinda Vernieri, Isabel Gomez-Monterrey, Ciro Milite, Paolo Grieco, Simona Musella, Alessia Bertamino, Ilaria Scognamiglio, Stefano Alcaro, Anna Artese, Francesco Ortuso, Ettore Novellino, Marina Sala, Pietro Campiglia","doi":"10.1155/2013/606282","DOIUrl":"10.1155/2013/606282","url":null,"abstract":"<p><p>Cyclooxygenase (COX) is a key enzyme in the biosynthetic pathway leading to the formation of prostaglandins, which are mediators of inflammation. It exists mainly in two isoforms COX-1 and COX-2. The conventional nonsteroidal anti-inflammatory drugs (NSAIDs) have gastrointestinal side effects because they inhibit both isoforms. Recent data demonstrate that the overexpression of these enzymes, and in particular of cyclooxygenases-2, promotes multiple events involved in tumorigenesis; in addition, numerous studies show that the inhibition of cyclooxygenases-2 can delay or prevent certain forms of cancer. Agents that inhibit COX-2 while sparing COX-1 represent a new attractive therapeutic development and offer a new perspective for a further use of COX-2 inhibitors. The present study extends the evaluation of the COX activity to all 20(3) possible natural tripeptide sequences following a rational approach consisting in molecular modeling, synthesis, and biological tests. Based on data obtained from virtual screening, only those peptides with better profile of affinity have been selected and classified into two groups called S and E. Our results suggest that these novel compounds may have potential as structural templates for the design and subsequent development of the new selective COX-2 inhibitors drugs.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"606282"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3600326/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40229758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-06-26DOI: 10.1155/2013/615754
Francesco Di Pierro, Giuseppe Rossoni
{"title":"An amino acids mixture improves the hepatotoxicity induced by acetaminophen in mice.","authors":"Francesco Di Pierro, Giuseppe Rossoni","doi":"10.1155/2013/615754","DOIUrl":"10.1155/2013/615754","url":null,"abstract":"<p><p>Acetaminophen (APAP) is a widely used analgesic and antipyretic drug, but at high dose it leads to undesirable side effects, such as hepatotoxicity and nephrotoxicity. The aim of this study was to evaluate the protective role of DDM-GSH, a mixture of L-cysteine, L-methionine, and L-serine in a weight ratio of 2 : 1 : 1, in comparison to N-acetylcysteine (NAC), against acetaminophen- (APAP-) induced hepatotoxicity in mice. Toxicity was induced in mice by the intraperitoneal (ip) administration of low dose (2 mmol/kg) or high dose (8 mmol/kg) of APAP. DDM-GSH (0.4 to 1.6 mmol/kg) was given ip to mice 1 h before the APAP administration. The same was done with NAC (0.9 to 3.6 mmol/kg), the standard antidote of APAP toxicity. Mice were sacrificed 8 h after the APAP injection to determine liver weight, serum alanine aminotransferase (ALT), and total glutathione (GSH) depletion and malondialdehyde (MDA) accumulation in liver tissues. DDM-GSH improved mouse survival rates better than NAC against a high dose of APAP. Moreover, DDM-GSH significantly reduced in a dose-dependent manner not only APAP-induced increases of ALT but also APAP-induced hepatic GSH depletion and MDA accumulation. Our results suggest that DDM-GSH may be more potent than NAC in protecting the liver from APAP-induced liver injury. </p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"615754"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3710638/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31600149","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-02-04DOI: 10.1155/2013/461901
John S Hothersall, Aamir Ahmed
{"title":"Metabolic fate of the increased yeast amino Acid uptake subsequent to catabolite derepression.","authors":"John S Hothersall, Aamir Ahmed","doi":"10.1155/2013/461901","DOIUrl":"https://doi.org/10.1155/2013/461901","url":null,"abstract":"<p><p>Catabolite repression (CCR) regulates amino acid permeases in Saccharomyces cerevisiae via a TOR-kinase mediated mechanism. When glucose, the preferred fuel in S. cerevisiae, is substituted by galactose, amino acid uptake is increased. Here we have assessed the contribution and metabolic significance of this surfeit of amino acid in yeast undergoing catabolite derepression (CDR). L-[U-(14)C]leucine oxidation was increased 15 ± 1 fold in wild type (WT) strain grown in galactose compared to glucose. Under CDR, leucine oxidation was (i) proportional to uptake, as demonstrated by decreased uptake and oxidation of leucine in strains deleted of major leucine permeases and (ii) entirely dependent upon the TCA cycle, as cytochrome c1 (Cyt1) deleted strains could not grow in galactose. A regulator of amino acid carbon entry into the TCA cycle, branched chain ketoacid dehydrogenase, was also increased 29 ± 3 fold under CCR in WT strain. Protein expression of key TCA cycle enzymes, citrate synthase (Cs), and Cyt1 was increased during CDR. In summary, CDR upregulation of amino acid uptake is accompanied by increased utilization of amino acids for yeast growth. The mechanism for this is likely to be an increase in protein expression of key regulators of the TCA cycle.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"461901"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/461901","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31348451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-07-29DOI: 10.1155/2013/964637
Jennifer F Iverson, Mary C Gannon, Frank Q Nuttall
{"title":"Ingestion of leucine + phenylalanine with glucose produces an additive effect on serum insulin but less than additive effect on plasma glucose.","authors":"Jennifer F Iverson, Mary C Gannon, Frank Q Nuttall","doi":"10.1155/2013/964637","DOIUrl":"https://doi.org/10.1155/2013/964637","url":null,"abstract":"<p><p>Most individual amino acids stimulate insulin secretion and attenuate the plasma glucose response when ingested with glucose. We determined whether ingestion of two amino acids simultaneously with glucose would result in an additive effect on the glucose area response compared with ingestion of amino acids individually. Leucine and phenylalanine were chosen because they were two of the most potent glucose-lowering amino acids when given individually. Eight healthy subjects were studied on four separate days. Test meals were given at 0800. The first meal was a water control. Subjects then received 25 g glucose or leucine + phenylalanine (1 mmol/kg fat free body mass each) ±25 g glucose in random order. Glucose, insulin and glucagon were measured frequently for 2.5 hours thereafter. Net areas under the curves were calculated using the mean fasting value as baseline. The insulin response to leucine + phenylalanine was additive. In contrast, the decrease in glucose response to leucine + phenylalanine + glucose was less than additive compared to the individual amino acids ingested with glucose. Interestingly, the insulin response to the combination was largely due to the leucine component, whereas the glucose response was largely due to the phenylalanine component. Glucose was unchanged when leucine or phenylalanine, alone or in combination, was ingested without glucose. This trial is registered with ClinicalTrials.gov NCT01471509. </p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"964637"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/964637","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31689921","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}