ISRN biochemistryPub Date : 2013-09-12eCollection Date: 2013-01-01DOI: 10.1155/2013/598251
Ahmed H Mekkawy, David L Morris
{"title":"Human sprouty1 suppresses urokinase receptor-stimulated cell migration and invasion.","authors":"Ahmed H Mekkawy, David L Morris","doi":"10.1155/2013/598251","DOIUrl":"https://doi.org/10.1155/2013/598251","url":null,"abstract":"<p><p>The urokinase-type plasminogen activator receptor (uPAR) has been implicated in several processes in tumor progression including cell migration and invasion in addition to initiation of signal transduction. Since uPAR lacks a transmembrane domain, it uses the interaction with other proteins to modulate intracellular signal transduction. We have previously identified hSpry1 as a partner protein of uPAR, suggesting a physiological role for hSpry1 in the regulation of uPAR signal transduction. In this study, hSpry1 was found to colocalize with uPAR upon stimulation with epidermal growth factor (EGF), urokinase (uPA), or its amino terminal fragment (uPA-ATF), implicating a physiological role of hSpry1 in regulation of uPAR signalling pathway. Moreover, hSpry1 was able to inhibit uPAR-stimulated cell migration in HEK293/uPAR, breast carcinoma, and colorectal carcinoma cells. In addition, hSpry1 was found to inhibit uPAR-stimulated cell invasion in breast carcinoma and osteosarcoma cell lines. Increasing our understanding of how hSpry1 negatively regulates uPAR-stimulated cellular functions may determine a distinctive role for hSpry1 in tumour suppression. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"598251"},"PeriodicalIF":0.0,"publicationDate":"2013-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4393002/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33272051","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":"A sequence-specific nicking endonuclease from streptomyces: purification, physical and catalytic properties.","authors":"Peechapack Somyoonsap, Vichein Kitpreechavanich, Somchai Pornbanlualap","doi":"10.1155/2013/287158","DOIUrl":"https://doi.org/10.1155/2013/287158","url":null,"abstract":"<p><p>A sequence-specific nicking endonuclease from Streptomyces designated as DC13 was purified to near homogeneity. Starting with 30 grams of wet cells, the enzyme was purified by ammonium sulfate fractionation, DEAE cellulose, and phenyl-Sepharose chromatography. The purified protein had a specific activity 1000 units/mg and migrated on SDS-PAGE gel with an estimated molecular weight of 71 kDa. Determination of subunit composition by gel filtration chromatography indicated that the native enzyme is a monomer. When incubated with different DNA substrates including pBluescript II KS, pUC118, pET-15b, and pET-26b, the enzyme converted these supercoiled plasmids to a mixture of open circular and linear DNA products, with the open circular DNA as the major cleavage product. Analysis of the kinetic of DNA cleavage showed that the enzyme appeared to cleave super-coiled plasmid in two distinct steps: a rapid cleavage of super-coiled plasmid to an open circular DNA followed a much slower step to linear DNA. The DNA cleavage reaction of the enzyme required Mg(2+) as a cofactor. Based on the monomeric nature of the enzyme, the kinetics of DNA cleavage exhibited by the enzyme, and cofactor requirement, it is suggested here that the purified enzyme is a sequence-specific nicking endonuclease that is similar to type IIS restriction endonuclease. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"287158"},"PeriodicalIF":0.0,"publicationDate":"2013-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/287158","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33272048","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}
ISRN biochemistryPub Date : 2013-08-07eCollection Date: 2013-01-01DOI: 10.1155/2013/198065
Nadeem A Ansari, Debabrata Dash
{"title":"Biochemical Studies on Methylglyoxal-Mediated Glycated Histones: Implications for Presence of Serum Antibodies against the Glycated Histones in Patients with Type 1 Diabetes Mellitus.","authors":"Nadeem A Ansari, Debabrata Dash","doi":"10.1155/2013/198065","DOIUrl":"10.1155/2013/198065","url":null,"abstract":"<p><p>Reactive carbonyl species (RCS) mainly reacts with lysine and arginine residues of proteins to form advanced glycation end products (AGEs). Histone was glycoxidated with glyoxal and methylglyoxal. It was characterized by polyacrylamide gel electrophoresis and quenching studies involving penicillamine and aminoguanidine as carbonyl scavengers. Further characterization of histone modified with methylglyoxal was done by UV, fluorescence, and IR spectrophotometry. Spectral analysis of the protein clearly demonstrates structural perturbation in the histone by methylglyoxal. Methylglyoxal-induces cross-linking in the protein leading to aggregation. Role of methylglyoxal mediated glycoxidation of histone in type 1 diabetes was also undertaken. Antibodies were detected against glycoxidated histone in sera of type 1 diabetes patients by solid-phase enzyme immunoassay. The findings indicate that as a result of structural perturbation in histone by methylglyoxal, the modified histone may be involved in production of serum antibodies in the diabetes patients. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"198065"},"PeriodicalIF":0.0,"publicationDate":"2013-08-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4392999/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33272047","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":"Cellular and Biochemical Mechanisms of the Retroviral Restriction Factor SAMHD1.","authors":"Li Wu","doi":"10.1155/2013/728392","DOIUrl":"https://doi.org/10.1155/2013/728392","url":null,"abstract":"<p><p>Replication of HIV-1 and other retroviruses is dependent on numerous host proteins in the cells. Some of the host proteins, however, function as restriction factors to block retroviral infection of target cells. The host protein SAMHD1 has been identified as the first mammalian deoxynucleoside triphosphate triphosphohydrolase (dNTPase), which blocks the infection of HIV-1 and other retroviruses in non-cycling immune cells. SAMHD1 protein is highly expressed in human myeloid-lineage cells and CD4<sup>+</sup> T-lymphocytes, but its retroviral restriction function is only observed in non-cycling cells. Recent studies have revealed biochemical mechanisms of SAMHD1-mediated retroviral restriction. In this review, the latest progress on SAMHD1 research is summarized and the mechanisms by which SAMHD1 mediates retroviral restriction are analyzed. Although the physiological function of SAMHD1 is largely unknown, this review provides perspectives about the role of endogenous SAMHD1 protein in maintaining normal cellular function, such as nucleic acid metabolism and the proliferation of cells.</p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2013-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/728392","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32112460","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}
ISRN biochemistryPub Date : 2013-05-21eCollection Date: 2013-01-01DOI: 10.1155/2013/238428
Massimo Masserini
{"title":"Nanoparticles for brain drug delivery.","authors":"Massimo Masserini","doi":"10.1155/2013/238428","DOIUrl":"10.1155/2013/238428","url":null,"abstract":"<p><p>The central nervous system, one of the most delicate microenvironments of the body, is protected by the blood-brain barrier (BBB) regulating its homeostasis. BBB is a highly complex structure that tightly regulates the movement of ions of a limited number of small molecules and of an even more restricted number of macromolecules from the blood to the brain, protecting it from injuries and diseases. However, the BBB also significantly precludes the delivery of drugs to the brain, thus, preventing the therapy of a number of neurological disorders. As a consequence, several strategies are currently being sought after to enhance the delivery of drugs across the BBB. Within this review, the recently born strategy of brain drug delivery based on the use of nanoparticles, multifunctional drug delivery systems with size in the order of one-billionth of meters, is described. The review also includes a brief description of the structural and physiological features of the barrier and of the most utilized nanoparticles for medical use. Finally, the potential neurotoxicity of nanoparticles is discussed, and future technological approaches are described. The strong efforts to allow the translation from preclinical to concrete clinical applications are worth the economic investments. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"238428"},"PeriodicalIF":0.0,"publicationDate":"2013-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4392984/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33272049","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}
ISRN biochemistryPub Date : 2013-05-12eCollection Date: 2013-01-01DOI: 10.1155/2013/463527
Nikolai M Soldatov
{"title":"Cav1.2, cell proliferation, and new target in atherosclerosis.","authors":"Nikolai M Soldatov","doi":"10.1155/2013/463527","DOIUrl":"https://doi.org/10.1155/2013/463527","url":null,"abstract":"<p><p>Cav1.2 calcium channels are the principal proteins involved in electrical, mechanical, and/or signaling functions of the cell. Cav1.2 couples membrane depolarization to the transient increase in intracellular Ca(2+) concentration that is a trigger for muscle contraction and CREB-dependent transcriptional activation. The CACNA1C gene coding for the Cav1.2 pore-forming α 1C subunit is subject to extensive alternative splicing. This review is the first attempt to follow the association between cell proliferation, Cav1.2 expression and splice variation, and atherosclerosis. Based on insights into the association between the atherosclerosis-induced molecular remodeling of Cav1.2, proliferation of vascular smooth muscle cells, and CREB-dependent transcriptional signaling, this review will give a perspective outlook for the use of the CACNA1C exon skipping as a new potential gene therapy approach to atherosclerosis. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"463527"},"PeriodicalIF":0.0,"publicationDate":"2013-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/463527","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33272050","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}
ISRN biochemistryPub Date : 2013-02-18eCollection Date: 2013-01-01DOI: 10.1155/2013/645983
Kazuyuki Shimizu
{"title":"Metabolic Regulation of a Bacterial Cell System with Emphasis on Escherichia coli Metabolism.","authors":"Kazuyuki Shimizu","doi":"10.1155/2013/645983","DOIUrl":"10.1155/2013/645983","url":null,"abstract":"<p><p>It is quite important to understand the overall metabolic regulation mechanism of bacterial cells such as Escherichia coli from both science (such as biochemistry) and engineering (such as metabolic engineering) points of view. Here, an attempt was made to clarify the overall metabolic regulation mechanism by focusing on the roles of global regulators which detect the culture or growth condition and manipulate a set of metabolic pathways by modulating the related gene expressions. For this, it was considered how the cell responds to a variety of culture environments such as carbon (catabolite regulation), nitrogen, and phosphate limitations, as well as the effects of oxygen level, pH (acid shock), temperature (heat shock), and nutrient starvation. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"645983"},"PeriodicalIF":0.0,"publicationDate":"2013-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4393010/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33273615","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}
ISRN biochemistryPub Date : 2013-01-28eCollection Date: 2013-01-01DOI: 10.1155/2013/762412
Meenakshi Thakur, Baldev Singh Sohal
{"title":"Role of Elicitors in Inducing Resistance in Plants against Pathogen Infection: A Review.","authors":"Meenakshi Thakur, Baldev Singh Sohal","doi":"10.1155/2013/762412","DOIUrl":"10.1155/2013/762412","url":null,"abstract":"<p><p>Disease control is largely based on the use of fungicides, bactericides, and insecticides-chemical compounds toxic to plant invaders, causative agents, or vectors of plant diseases. However, the hazardous effect of these chemicals or their degradation products on the environment and human health strongly necessitates the search for new, harmless means of disease control. There must be some natural phenomenon of induced resistance to protect plants from disease. Elicitors are compounds, which activate chemical defense in plants. Various biosynthetic pathways are activated in treated plants depending on the compound used. Commonly tested chemical elicitors are salicylic acid, methyl salicylate, benzothiadiazole, benzoic acid, chitosan, and so forth which affect production of phenolic compounds and activation of various defense-related enzymes in plants. Their introduction into agricultural practice could minimize the scope of chemical control, thus contributing to the development of sustainable agriculture. This paper chiefly highlights the uses of elicitors aiming to draw sufficient attention of researchers to the frontier research needed in this context. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"762412"},"PeriodicalIF":0.0,"publicationDate":"2013-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4393000/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33298674","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}
ISRN biochemistryPub Date : 2013-01-10eCollection Date: 2013-01-01DOI: 10.1155/2013/913273
Toshitsugu Fujita, Hodaka Fujii
{"title":"Locus-specific biochemical epigenetics/chromatin biochemistry by insertional chromatin immunoprecipitation.","authors":"Toshitsugu Fujita, Hodaka Fujii","doi":"10.1155/2013/913273","DOIUrl":"https://doi.org/10.1155/2013/913273","url":null,"abstract":"<p><p>Comprehensive understanding of regulation mechanisms of biological phenomena mediated by functions of genomic DNA requires identification of molecules bound to genomic regions of interest in vivo. However, nonbiased methods to identify molecules bound to specific genomic loci in vivo are limited. To perform biochemical and molecular biological analysis of specific genomic regions, we developed the insertional chromatin immunoprecipitation (iChIP) technology to purify the genomic regions of interest. We applied iChIP to direct identification of components of insulator complexes, which function as boundaries of chromatin domain, showing that it is feasible to directly identify proteins and RNA bound to a specific genomic region in vivo by using iChIP. In addition, recently, we succeeded in identifying proteins and genomic regions interacting with a single copy endogenous locus. In this paper, we will discuss the application of iChIP to epigenetics and chromatin research. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2013 ","pages":"913273"},"PeriodicalIF":0.0,"publicationDate":"2013-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2013/913273","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33298676","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}
ISRN biochemistryPub Date : 2012-12-19eCollection Date: 2012-01-01DOI: 10.5402/2012/506160
Thomas Kolter
{"title":"Ganglioside biochemistry.","authors":"Thomas Kolter","doi":"10.5402/2012/506160","DOIUrl":"https://doi.org/10.5402/2012/506160","url":null,"abstract":"<p><p>Gangliosides are sialic acid-containing glycosphingolipids. They occur especially on the cellular surfaces of neuronal cells, where they form a complex pattern, but are also found in many other cell types. The paper provides a general overview on their structures, occurrence, and metabolism. Key functional, biochemical, and pathobiochemical aspects are summarized. </p>","PeriodicalId":90189,"journal":{"name":"ISRN biochemistry","volume":"2012 ","pages":"506160"},"PeriodicalIF":0.0,"publicationDate":"2012-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5402/2012/506160","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33298675","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}