Journal of Amino AcidsPub Date : 2013-01-01Epub Date: 2013-05-15DOI: 10.1155/2013/568953
Paola Stiuso, Michele Caraglia, Giuseppe De Rosa, Antonio Giordano
{"title":"Bioactive peptides in cancer: therapeutic use and delivery strategies.","authors":"Paola Stiuso, Michele Caraglia, Giuseppe De Rosa, Antonio Giordano","doi":"10.1155/2013/568953","DOIUrl":"https://doi.org/10.1155/2013/568953","url":null,"abstract":"Human cancer is one of the most important causes of death in western and industrialized countries. In advanced stages, therapeutic opportunities are still limited due to the difficulty to target specifically only cancer cells sparing healthy ones. Cancer often has specific molecular alterations of signal transduction pathway or of other molecules linked to the proliferation and wide spreading of tumour cells. Several peptides have been isolated from natural products and/or physiological sources and several of them have biological activity on cancer cells. This special issue addresses the role of these natural peptides and of their synthetic derivatives in cancer therapy, alone or in combination with other anticancer agents. \u0000 \u0000One of the most interesting peptides of natural origin is Urotensin-II (U-II) originally isolated from the goby urophysis and subsequently identified in humans. It binds a specific receptor (UTR) that mediates a very strong contraction of vessel muscle cells. 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 UTR is more fascinating. Finally, it was recently reported by several groups a potential role of U-II and its receptor in the regulation of cancer biology. The paper by F. Merlino et al. discusses peptide and nonpeptide U-II and UTR structures that have led to a more rational and detectable design and synthesis of new molecules with high affinity for UTR. Other peptides with anticancer properties are peptide hormones acting on the pituitary axis in the treatment of endocrinological cancers such as breast and prostate cancer and peptides acting on neuroendocrine receptors such as somatostatin and BN/GRP (bombesin/gastrin-releasing peptide). The paper by J. Thundimadathil discussed the role of luteinizing hormone-releasing hormone (LHRH) agonists and antagonists and on the possible action of somatostatin analogues as radioisotope or cytotoxic drug carriers in the treatment of somatostatin receptor expressing tumours. Finally, the possible use of peptides in cancer vaccine or anti-angiogenic strategies is also described. \u0000 \u0000Food is another important source for proteins and peptides with potential anticancer activity. Bovine milk is an important component of the human diet, and it contains several proteins formed by two major families: caseins (insoluble) and whey proteins (soluble). The latter are β-lactoglobulin, α-lactalbumin, bovine serum albumin, and lactoferrin while the predominant forms of the caseins in ruminant milk are αS1, αS2, β, and κ. The paper by Pepe et al. describes the main evidences on the anticancer activity of some of these proteins on human cancer cell cultures. Another important function of certain peptides in cancer cell biology is the potential interference with the oxidative processes that are, in turn, strictly implica","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"568953"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/568953","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31691290","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: 2013-09-08DOI: 10.1155/2013/864757
Angelos K Sikalidis, Kevin M Mazor, Minji Kang, Hongyun Liu, Martha H Stipanuk
{"title":"Total 4EBP1 Is Elevated in Liver of Rats in Response to Low Sulfur Amino Acid Intake.","authors":"Angelos K Sikalidis, Kevin M Mazor, Minji Kang, Hongyun Liu, Martha H Stipanuk","doi":"10.1155/2013/864757","DOIUrl":"https://doi.org/10.1155/2013/864757","url":null,"abstract":"<p><p>Translation initiation is known to be regulated by the binding of eukaryotic initiation factor 4E (eIF4E) by binding proteins (4EBPs), and there is evidence that amino acid deprivation and other cellular stresses upregulate 4EBP1 expression. To pursue the question of whether diets limited in an essential amino acid lead to induction of 4EBP1 expression in vivo, diets that varied in methionine and cystine content were fed to rats for 7 days, and 4EBP1 mRNA and protein levels and 4EBP1 phosphorylation state were determined. Total 4EBP1 mRNA and protein abundance increased in liver of rats with severely deficient intakes of sulfur amino acids (0.23% or 0.11% methionine without cystine) but not in animals with a less restricted intake of sulfur amino acids (0.11% methionine plus 0.35% cystine) but a similarly restricted intake of total diet (53 to 62% of control). The amount of 4EBP1 binding activity ( α + β forms) was elevated in liver of rats fed sulfur amino acid-deficient diets, whereas the hyperphosphorylation of 4EBP1 was not affected by dietary treatment. Results suggest that changes in total 4EBP1 expression should be considered when examining mechanisms that attenuate protein synthesis during amino acid deficiency states. </p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2013 ","pages":"864757"},"PeriodicalIF":0.0,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/864757","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31777511","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":"Erratum to “Decreased Phosphorylation and Increased Methionine Oxidation of α-Synuclein in the Methionine Sulfoxide Reductase A Knockout Mouse”","authors":"D. Oien, G. Carrasco, J. Moskovitz","doi":"10.1155/2012/415713","DOIUrl":"https://doi.org/10.1155/2012/415713","url":null,"abstract":"On page 4 of this published article an error in Figure 2(a) has occurred. Accordingly, Figure 2(a) has been replaced with a corrected version of the figure as shown below. \u0000 \u0000 \u0000 \u0000Figure 2 \u0000 \u0000Phosphorylation of α-synuclein in MsrA−/− and wild-type (WT) brain extracts. (a) Tris-soluble and Urea-soluble brain extracts (40 μg protein) of both mouse types were prepared as described in Section 2. These extracts ...","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"44 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2012-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80247492","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of Amino AcidsPub Date : 2012-01-01Epub Date: 2011-10-23DOI: 10.1155/2012/650840
Nina A Filenko, Dmytro B Palets, Yuri L Lyubchenko
{"title":"Structure and dynamics of dinucleosomes assessed by atomic force microscopy.","authors":"Nina A Filenko, Dmytro B Palets, Yuri L Lyubchenko","doi":"10.1155/2012/650840","DOIUrl":"https://doi.org/10.1155/2012/650840","url":null,"abstract":"<p><p>Dynamics of nucleosomes and their interactions are important for understanding the mechanism of chromatin assembly. Internucleosomal interaction is required for the formation of higher-order chromatin structures. Although H1 histone is critically involved in the process of chromatin assembly, direct internucleosomal interactions contribute to this process as well. To characterize the interactions of nucleosomes within the nucleosome array, we designed a dinucleosome and performed direct AFM imaging. The analysis of the AFM data showed dinucleosomes are very dynamic systems, enabling the nucleosomes to move in a broad range along the DNA template. Di-nucleosomes in close proximity were observed, but their population was low. The use of the zwitterionic detergent, CHAPS, increased the dynamic range of the di-nucleosome, facilitating the formation of tight di-nucleosomes. The role of CHAPS and similar natural products in chromatin structure and dynamics is also discussed.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"650840"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/650840","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968192","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 : 2012-01-01Epub Date: 2012-04-18DOI: 10.1155/2012/382107
Jeffrey M Dale, Michael L Garcia
{"title":"Neurofilament Phosphorylation during Development and Disease: Which Came First, the Phosphorylation or the Accumulation?","authors":"Jeffrey M Dale, Michael L Garcia","doi":"10.1155/2012/382107","DOIUrl":"https://doi.org/10.1155/2012/382107","url":null,"abstract":"<p><p>Posttranslational modification of proteins is a ubiquitous cellular mechanism for regulating protein function. Some of the most heavily modified neuronal proteins are cytoskeletal proteins of long myelinated axons referred to as neurofilaments (NFs). NFs are type IV intermediate filaments (IFs) that can be composed of four subunits, neurofilament heavy (NF-H), neurofilament medium (NF-M), neurofilament light (NF-L), and α-internexin. Within wild type axons, NFs are responsible for mediating radial growth, a process that determines axonal diameter. NFs are phosphorylated on highly conserved lysine-serine-proline (KSP) repeats located along the C-termini of both NF-M and NF-H within myelinated axonal regions. Phosphorylation is thought to regulate aspects of NF transport and function. However, a key pathological hallmark of several neurodegenerative diseases is ectopic accumulation and phosphorylation of NFs. The goal of this review is to provide an overview of the posttranslational modifications that occur in both normal and diseased axons. We review evidence that challenges the role of KSP phosphorylation as essential for radial growth and suggests an alternative role for NF phosphorylation in myelinated axons. Furthermore, we demonstrate that regulation of NF phosphorylation dynamics may be essential to avoiding NF accumulations.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2012 ","pages":"382107"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/382107","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30604492","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 : 2012-01-01Epub Date: 2012-09-11DOI: 10.1155/2012/493209
Sushma Gurung, Michael F Cohen, Jon Fukuto, Hideo Yamasaki
{"title":"Polyamine-Induced Rapid Root Abscission in Azolla pinnata.","authors":"Sushma Gurung, Michael F Cohen, Jon Fukuto, Hideo Yamasaki","doi":"10.1155/2012/493209","DOIUrl":"10.1155/2012/493209","url":null,"abstract":"<p><p>Floating ferns of the genus Azolla detach their roots under stress conditions, a unique adaptive response termed rapid root abscission. We found that Azolla pinnata plants exhibited dose-dependent rapid root abscission in response to the polyamines spermidine and spermine after a substantial time lag (>20 min). The duration of the time lag decreased in response to high pH and high temperature whereas high light intensity increased the time lag and markedly lowered the rate of abscission. The oxidation products of polyamines, 1,3-diaminopropane, β-alanine and hydrogen peroxide all failed to initiate root abscission, and hydroxyethyl hydrazine, an inhibitor of polyamine oxidase, did not inhibit spermine-induced root abscission. Exposure of A. pinnata to the polyamines did not result in detectable release of NO and did not affect nitrite-dependent NO production. The finding of polyamine-induced rapid root abscission provides a facile assay for further study of the mode of action of polyamines in plant stress responses.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2012 ","pages":"493209"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3446730/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30919333","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 : 2012-01-01Epub Date: 2012-05-29DOI: 10.1155/2012/831759
Yumi Takemoto
{"title":"Amino acids that centrally influence blood pressure and regional blood flow in conscious rats.","authors":"Yumi Takemoto","doi":"10.1155/2012/831759","DOIUrl":"10.1155/2012/831759","url":null,"abstract":"<p><p>Functional roles of amino acids have increasingly become the focus of research. This paper summarizes amino acids that influence cardiovascular system via the brain of conscious rats. This paper firstly describes why amino acids are selected and outlines how the brain regulates blood pressure and regional blood flow. This section includes a concise history of amino acid neurotransmitters in cardiovascular research and summarizes brain areas where chemical stimulations produce blood pressure changes mainly in anesthetized animals. This is followed by comments about findings regarding several newly examined amino acids with intracisternal stimulation in conscious rats that produce changes in blood pressure. The same pressor or depressor response to central amino acid stimulations can be produced by distinct mechanisms at central and peripheral levels, which will be briefly explained. Thereafter, cardiovascular actions of some of amino acids at the mechanism level will be discussed based upon findings of pharmacological and regional blood flow measurements. Several examined amino acids in addition to the established neurotransmitter amino acids appear to differentially activate brain structures to produce changes in blood pressure and regional blood flows. They may have physiological roles in the healthy brain, but pathological roles in the brain with cerebral vascular diseases such as stroke where the blood-brain barrier is broken.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2012 ","pages":"831759"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/831759","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30685929","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 : 2012-01-01Epub Date: 2012-02-08DOI: 10.1155/2012/206520
Yoichi Matsunaga, Midori Suenaga
{"title":"Environmental factors preceding aβ40 monomer to oligomers and the detection of oligomers in Alzheimer's disease patient serum.","authors":"Yoichi Matsunaga, Midori Suenaga","doi":"10.1155/2012/206520","DOIUrl":"https://doi.org/10.1155/2012/206520","url":null,"abstract":"<p><p>We present here environmental factors including pH shifts, temperature, and metal ions surrounding Aβ40 monomer to precede the oligomers. We also suggest a new idea to detect Aβ40 oligomers with anti-Aβ40 monoclonal antibody using enzyme-linked immunosorbent assay. This method involves the different sensitivity of the thermal shifts between Aβ40 monomer and the oligomers. The idea is useful for the diagnostics of Alzheimer's disease to detect Aβ40 oligomers in the serum from the patients.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"206520"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/206520","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40174120","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 : 2012-01-01Epub Date: 2012-02-28DOI: 10.1155/2012/816032
Markus Ritzefeld, Norbert Sewald
{"title":"Real-Time Analysis of Specific Protein-DNA Interactions with Surface Plasmon Resonance.","authors":"Markus Ritzefeld, Norbert Sewald","doi":"10.1155/2012/816032","DOIUrl":"https://doi.org/10.1155/2012/816032","url":null,"abstract":"<p><p>Several proteins, like transcription factors, bind to certain DNA sequences, thereby regulating biochemical pathways that determine the fate of the corresponding cell. Due to these key positions, it is indispensable to analyze protein-DNA interactions and to identify their mode of action. Surface plasmon resonance is a label-free method that facilitates the elucidation of real-time kinetics of biomolecular interactions. In this article, we focus on this biosensor-based method and provide a detailed guide how SPR can be utilized to study binding of proteins to oligonucleotides. After a description of the physical phenomenon and the instrumental realization including fiber-optic-based SPR and SPR imaging, we will continue with a survey of immobilization methods. Subsequently, we will focus on the optimization of the experiment, expose pitfalls, and introduce how data should be analyzed and published. Finally, we summarize several interesting publications of the last decades dealing with protein-DNA and RNA interaction analysis by SPR.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2012 ","pages":"816032"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/816032","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30572144","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 : 2012-01-01Epub Date: 2012-08-22DOI: 10.1155/2012/837932
Laura Valdés-Santiago, José Antonio Cervantes-Chávez, Claudia Geraldine León-Ramírez, José Ruiz-Herrera
{"title":"Polyamine metabolism in fungi with emphasis on phytopathogenic species.","authors":"Laura Valdés-Santiago, José Antonio Cervantes-Chávez, Claudia Geraldine León-Ramírez, José Ruiz-Herrera","doi":"10.1155/2012/837932","DOIUrl":"https://doi.org/10.1155/2012/837932","url":null,"abstract":"<p><p>Polyamines are essential metabolites present in all living organisms, and this subject has attracted the attention of researchers worldwide interested in defining their mode of action in the variable cell functions in which they are involved, from growth to development and differentiation. Although the mechanism of polyamine synthesis is almost universal, different biological groups show interesting differences in this aspect that require to be further analyzed. For these studies, fungi represent interesting models because of their characteristics and facility of analysis. During the last decades fungi have contributed to the understanding of polyamine metabolism. The use of specific inhibitors and the isolation of mutants have allowed the manipulation of the pathway providing information on its regulation. During host-fungus interaction polyamine metabolism suffers striking changes in response to infection, which requires examination. Additionally the role of polyamine transporter is getting importance because of its role in polyamine regulation. In this paper we analyze the metabolism of polyamines in fungi, and the difference of this process with other biological groups. Of particular importance is the difference of polyamine biosynthesis between fungi and plants, which makes this process an attractive target for the control of phytopathogenic fungi.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":"2012 ","pages":"837932"},"PeriodicalIF":0.0,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2012/837932","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30887856","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}