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Beyond the Genome 2000: The 18th International Congress of Biochemistry and Molecular Biology

Wixon, Jo; Brancia, Francesco
Fonte: Hindawi Publishing Corporation Publicador: Hindawi Publishing Corporation
Tipo: Artigo de Revista Científica
Publicado em //2000 EN
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The meeting was held on 16–20 July 2000 at the International Convention Centre in Birmingham, UK, and was co-organized by the International Union of Biochemistry and Molecular Biology (IUBMB) and the Federation of European Biochemical Societies (FEBS). Although the meeting had a broad subject area, the emphasis was firmly placed on post-genomic studies, and hence several sessions should be of interest to our readers. We provide highlights of these sessions, bringing you a report on the most exciting and informative presentations.

Founding, early history, and transformation of the Journal for Lipid Research to an American Society of Biochemistry and Molecular Biology journal1

Dennis, Edward A.
Fonte: American Society for Biochemistry and Molecular Biology Publicador: American Society for Biochemistry and Molecular Biology
Tipo: Artigo de Revista Científica
Publicado em /04/2009 EN
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The Journal of Lipid Research was founded in October, 1959 and has had a long and distinguished history. It evolved from an initial concept of a loose-leaf methodology handbook to a major journal for the lipid field. Its growth has in many ways paralleled the growth and expansion of lipid research. Today, it is operated as a journal of the American Society for Biochemistry and Molecular Biology at the forefront of biomedical research on lipids.

Thematic Minireview Series: Single-molecule Measurements in Biochemistry and Molecular Biology*

Allewell, Norma M.
Fonte: American Society for Biochemistry and Molecular Biology Publicador: American Society for Biochemistry and Molecular Biology
Tipo: Artigo de Revista Científica
EN
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Utilization of Electrochemical Sensors and Biosensors in Biochemistry and Molecular Biology

Adam, Vojtech; Kizek, Rene
Fonte: Molecular Diversity Preservation International (MDPI) Publicador: Molecular Diversity Preservation International (MDPI)
Tipo: Artigo de Revista Científica
Publicado em 01/10/2008 EN
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A special issue of Sensors entitled “Utilization of Electrochemical Sensors and Biosensors in Biochemistry and Molecular Biology” has been prepared over a period of three years. In this Editorial Note we would like to highlight one of the possible directions for electrochemical sensor and biosensor research resulting from the ideas of Czechoslovakian Nobel Prize winner Jaroslav Heyrovsky and his colleague Rudolf Brdicka.

7.013 Introductory Biology, Spring 2005; Introductory Biology

Sive, Hazel L.; Jacks, Tyler; Gardel, Claudette L.
Fonte: MIT - Massachusetts Institute of Technology Publicador: MIT - Massachusetts Institute of Technology
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The MIT Biology Department core courses, 7.012, 7.013, and 7.014, all cover the same core material, which includes the fundamental principles of biochemistry, genetics, molecular biology, and cell biology. Biological function at the molecular level is particularly emphasized and covers the structure and regulation of genes, as well as, the structure and synthesis of proteins, how these molecules are integrated into cells, and how these cells are integrated into multicellular systems and organisms. In addition, each version of the subject has its own distinctive material. 7.014 focuses on the application of the fundamental principles toward an understanding of human biology. Topics include genetics, cell biology, molecular biology, disease (infectious agents, inherited diseases and cancer), developmental biology, neurobiology and evolution.

Molecular interactions of biglycan and decorin with elastic fiber components - Biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein

Reinboth, B.; Hanssen, E.; Cleary, E.; Gibson, M.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2002 EN
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The interactions of the dermatan sulfate proteoglycans biglycan and decorin have been investigated with the elastic fiber components, tropoelastin, fibrillin-containing microfibrils, and microfibril-associated glycoproteins (MAGP) 1 and 2. Both proteoglycans were found to bind tropoelastin and fibrillin-containing microfibrils but not MAGPs 1 and 2 in solid phase binding assays. The specificity of the binding of biglycan and decorin to tropoelastin was confirmed by co-immunoprecipitation experiments and by the blocking of the interactions with elastin-derived peptides. Isolated core proteins from biglycan and decorin bound to tropoelastin more strongly than the intact proteoglycans, and there were no differences in the tropoelastin binding characteristics of distinct glucuronate-rich and iduronate-rich glycoforms of biglycan. These findings indicated that the binding sites were contained in the protein cores of the proteoglycans rather than the glycosaminoglycan side chains. Scatchard analysis showed that biglycan bound more avidly than decorin to tropoelastin with Kd values estimated as 1.95 × 107 M and 5.3 × 107 M, respectively. In blocking experiments each proteoglycan showed extensive inhibition of binding of the other to tropoelastin but was most effective at blocking its own binding. This result suggested that biglycan and decorin had closely spaced but distinct binding sites on tropoelastin. Addition of the elastin-binding protein MAGP-1 to the assays enhanced the binding of biglycan to tropoelastin but had no effect on the decorin-tropoelastin interaction. Co-immunoprecipitation experiments showed that MAGP-1 interacted with biglycan but not decorin in the solution phase. The results indicated that biglycan specifically formed a ternary complex with tropoelastin and MAGP-1. Overall the study supports the concept that biglycan may have a specific role in the elastinogenic phase of elastic fiber formation.; Betty Reinboth...

Novel DNA binding by a basic helix-loop-helix protein - The role of the dioxin receptor PAS domain

Chapman-Smith, A.; Whitelaw, M.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2006 EN
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Central issues surrounding the basic helix-loop-helix (bHLH) superfamily of dimeric transcription factors concern how specificity of partner selection and DNA binding are achieved. bHLH proteins bind DNA through the basic sequence that is contiguous with a helix-loop-helix dimerization domain. For the two subgroups within the family, dimerization is further regulated by an adjacent Per-Arnt-Sim homology (PAS) or leucine zipper (LZ) domain. We provide evidence that for the bHLH·PAS transcription factors Dioxin Receptor (DR) and Arnt, the DR PAS A domain has a unique interaction with the bHLH region that underpins both dimerization strength and affinity for an atypical E-box DNA sequence. A PAS swap heterodimer, where the DR bHLH domain was fused to Arnt PAS A and the Arnt bHLH fused to DR PAS A, gave strong DNA binding, but dimerization was only effective with the native arrangement, suggesting the PAS A domain is critical for each process via distinct mechanisms. LZ domains, which regulate heterodimerization for the bHLH·LZ family members Myc and Max, could not replace the PAS domains for either dimerization or DNA binding in the DR/Arnt heterodimer. In vitro footprinting revealed that the PAS domains influence the conformation of target DNA in a manner consistent with DNA bending. These results provide the first insights for understanding mechanisms of selective dimerization and DNA interaction that distinguish bHLH·PAS proteins from the broader bHLH superfamily.; © 2006 by The American Society for Biochemistry and Molecular Biology

Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains

Polyak, S.; Chapman-Smith, A.; Mulhern, T.; Cronan Jr., J.; Wallace, J.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2001 EN
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Biotinylation in vivo is an extremely selective post-translational event where the enzyme biotin protein ligase (BPL) catalyzes the covalent attachment of biotin to one specific and conserved lysine residue of biotin-dependent enzymes. The biotin-accepting lysine, present in a conserved Met-Lys-Met motif, resides in a structured domain that functions as the BPL substrate. We have employed phage display coupled with a genetic selection to identify determinants of the biotin domain (yPC-104) of yeast pyruvate carboxylase 1 (residues 1075-1178) required for interaction with BPL. Mutants isolated using this strategy were analyzed by in vivo biotinylation assays performed at both 30 °C and 37 °C. The temperature-sensitive substrates were reasoned to have structural mutations, leading to compromised conformations at the higher temperature. This interpretation was supplemented by molecular modeling of yPC-104, since these mutants mapped to residues involved in defining the structure of the biotin domain. In contrast, substitution of the Met residue N-terminal to the target lysine with either Val or Thr produced mutations that were temperature-insensitive in the in vivo assay. Furthermore, these two mutant proteins and wild-type yPC-104 showed identical susceptibility to trypsin...

The solution structure and intramolecular associations of the Tec kinase Src homology 3 domain

Pursglove, S.; Mulhern, T.; Mackay, J.; Hinds, M.; Booker, G.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2002 EN
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Tec is the prototypic member of a family of intracellular tyrosine kinases that includes Txk, Bmx, Itk, and Btk. Tec family kinases share similarities in domain structure with Src family kinases, but one of the features that differentiates them is a proline-rich region (PRR) preceding their Src homology (SH) 3 domain. Evidence that the PRR of Itk can bind in an intramolecular fashion to its SH3 domain and the lack of a regulatory tyrosine in the C terminus indicates that Tec kinases must be regulated by a different set of intramolecular interactions to the Src kinases. We have determined the solution structure of the Tec SH3 domain and have investigated interactions with its PRR, which contains two SH3-binding sites. We demonstrate that in vitro, the Tec PRR can bind in an intramolecular fashion to the SH3. However, the affinity is lower than that for dimerization via reciprocal PRR-SH3 association. Using site-directed mutagenesis we show that both sites can bind the Tec SH3 domain; site 1 (155KTLPPAP161) binds intramolecularly, while site 2 (165KRRPPPPIPP174) cannot and binds in an intermolecular fashion. These distinct roles for the SH3 binding sites in Tec family kinases could be important for protein targeting and enzyme activation.; Sharon E. Pursglove...

Inhibition of generation of cytotoxic T lymphocyte activity by a CCL19/macrophage inflammatory protein (MIP)-3beta antagonist

Pilkington, K.; Clark-Lewis, I.; McColl, S.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2004 EN
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Chemokines constitute a group of over 40 secreted peptides that are important for the control of leukocyte migration both during homeostasis and inflammation. Recent studies have implicated the ligands CCL19 and CCL21 and their receptor, CCR7, in the specific migration of naïve lymphocytes and mature dendritic cells to secondary lymphoid organs during immune homeostasis. However, the role that these molecules play during immune priming is not well understood. In this study, using CCL19(8–83), a novel N-terminal truncation mutant, we have investigated the role of CCL19 in a primary allogeneic immune response, a response of particular relevance to transplant rejection. This antagonist specifically inhibited wild type CCL19-induced chemotaxis and intracellular calcium mobilization without affecting that of CCL21. The treatment of mice with CCL19(8–83) did not globally inhibit the recruitment of cells into lymph nodes; however, it inhibited the generation of cytotoxic T lymphocytes toward allogeneic dendritic cells. This is the first evidence that CCL19 plays a role in immune priming.; Katherine R. Pilkington, Ian Clark-Lewis, and Shaun R. McColl; Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.

Mildly acidic pH activates the extracellular molecular chaperone clusterin

Poon, S.; Rybchyn, M.; Eastbrook-Smith, S.; Carver, J.; Pankhurst, G.; Wilson, M.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2002 EN
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Many features of the chaperone action of clusterin are similar to those of the intracellular small heat shock proteins (sHSPs) that, like clusterin, exist in solution as heterogeneous aggregates. Increased temperature induces dissociation of some sHSP aggregates and an enhanced chaperone action, suggesting that a dissociated form is the active chaperone species. We recently reported that clusterin aggregates dissociate at mildly acidic pH. To further explore the similarities between clusterin and the sHSPs, we tested the effects of temperature and pH on the structure of clusterin and its chaperone action. Our results demonstrate that increased temperature does not induce dissociation of clusterin aggregates, or other major structural changes, and has little effect on its chaperone action. However, we show that the chaperone action of clusterin is enhanced at mildly acidic pH. Clusterin is the first chaperone shown to be activated by reduced pH. This unique mode of activation appears to result from an increase in regions of solvent-exposed hydrophobicity, which is independent of any major changes in secondary or tertiary structure. We propose a model in which low pH-induced dissociation of clusterin aggregates increases the abundance of the heterodimeric chaperone-active species...

The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity

Devlin, G.; Carver, J.; Bottomley, S.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2003 EN
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Glyn L. Devlin, John A. Carver and Stephen P. Bottomley; Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.

The molecular chaperone, α-crystallin, inhibits amyloid formation by apolipoprotein C-II; The molecular chaperone, alpha-crystallin, inhibits amyloid formation by apolipoprotein C-II

Hatters, D.; Lindner, R.; Carver, J.; Howlett, G.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2001 EN
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Under lipid-free conditions, human apolipoprotein C-II (apoC-II) exists in an unfolded conformation that over several days forms amyloid ribbons. We examined the influence of the molecular chaperone, α-crystallin, on amyloid formation by apoC-II. Time-dependent changes in apoC-II turbidity (at 0.3 mg/ml) were suppressed potently by substoichiometric subunit concentrations of α-crystallin (1-10 μg/ml). α-Crystallin also inhibits time-dependent changes in the CD spectra, thioflavin T binding, and sedimentation coefficient of apoC-II. This contrasts with stoichiometric concentrations of α-crystallin required to suppress the amorphous aggregation of stressed proteins such as reduced α-lactalbumin. Two pieces of evidence suggest that α-crystallin directly interacts with amyloidogenic intermediates. First, sedimentation equilibrium and velocity experiments exclude high affinity interactions between α-crystallin and unstructured monomeric apoC-II. Second, the addition of α-crystallin does not lead to the accumulation of intermediate sized apoC-II species between monomer and large aggregates as indicated by gel filtration and sedimentation velocity experiments, suggesting that α-crystallin does not inhibit the relatively rapid fibril elongation upon nucleation. We propose that α-crystallin interacts stoichiometrically with partly structured amyloidogenic precursors...

Sulfonation and Phosphorylation of Regions of the Dioxin Receptor Susceptible to Methionine Modifications

Dave, K.; Whelan, F.; Bindloss, C.; Furness, S.; Chapman-Smith, A.; Whitelaw, M.; Gorman, J.
Fonte: American Society for Biochemistry and Molecular Biology, Inc. Publicador: American Society for Biochemistry and Molecular Biology, Inc.
Tipo: Artigo de Revista Científica
Publicado em //2009 EN
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Tagged murine dioxin receptor was purified from mammalian cells, digested with trypsin, and analyzed by capillary HPLC-MALDI-TOF/TOF-MS and -MS/MS. Several chromatographically distinct semitryptic peptides matching two regions spanning residues Glu(409)-Arg(424) and Ser(547)-Arg(555) of the dioxin receptor were revealed by de novo sequencing. Methionine residues at 418 and 548 were detected in these peptides as either unmodified or modified by moieties of 16 (oxidation) or 57 amu (S-carboxamidomethylation) or in a form corresponding to degradative removal of 105 amu from the S-carboxamidomethylated methionine. MS/MS spectra revealed that the peptides containing modified methionine residues also existed in forms with a modification of +80 amu on serine residues 411, 415, and 547. The MS/MS spectra of these peptide ions also revealed diagnostic neutral loss fragment ions of 64, 98, and/or 80 amu, and in some instances combinations of these neutral losses were apparent. Taken together, these data indicated that serines 411 and 547 of the dioxin receptor were sulfonated and serine 415 was phosphorylated. Separate digests of the dioxin receptor were prepared in H(2)(16)O and H(2)(18)O, and enzymatic dephosphorylation was subsequently performed on the H(2)(16)O digest only. The digests were mixed in equal proportions and analyzed by capillary HPLC-MALDI-TOF/TOF-MS and -MS/MS. This strategy confirmed assignment of sulfonation as the cause of the +80-amu modifications on serines 411 and 547 and phosphorylation as the predominant cause of the +80-amu modification of serine 415. The relative quantitation of phosphorylation and sulfonation enabled by this differential phosphatase strategy also suggested the presence of sulfonation on a serine other than residue 411 within the sequence spanning Glu(409)-Arg(424). This represents the first description of post-translational sulfonation sites and identification of a new phosphorylation site of the latent dioxin receptor. Furthermore this is only the second report of serine sulfonation of eukaryotic proteins. Mutagenesis studies are underway to assess the functional consequences of these modifications.; Keyur A. Dave...

Identification and characterization of Ambroxol as an enzyme enhancement agent for Gaucher Disease

Maegawa, G.; Tropak, M.; Buttner, J.; Rigat, B.; Fuller, M.; Pandit, D.; Tang, L.; Kornhaber, G.; Hamuro, Y.; Clarke, J.; Mahuran, D.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2009 EN
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Gaucher disease (GD), the most prevalent lysosomal storage disease, is caused by a deficiency of glucocerebrosidase (GCase). The identification of small molecules acting as agents for enzyme enhancement therapy is an attractive approach for treating different forms of GD. A thermal denaturation assay utilizing wild type GCase was developed to screen a library of 1,040 Food and Drug Administration-approved drugs. Ambroxol (ABX), a drug used to treat airway mucus hypersecretion and hyaline membrane disease in newborns, was identified and found to be a pH-dependent, mixed-type inhibitor of GCase. Its inhibitory activity was maximal at neutral pH, found in the endoplasmic reticulum, and undetectable at the acidic pH of lysosomes. The pH dependence of ABX to bind and stabilize the enzyme was confirmed by monitoring the rate of hydrogen/deuterium exchange at increasing guanidine hydrochloride concentrations. ABX treatment significantly increased N370S and F213I mutant GCase activity and protein levels in GD fibroblasts. These increases were primarily confined to the lysosome-enriched fraction of treated cells, a finding confirmed by confocal immunofluorescence microscopy. Additionally, enhancement of GCase activity and a reduction in glucosylceramide storage was verified in ABX-treated GD lymphoblasts (N370S/N370S). Hydrogen/deuterium exchange mass spectrometry revealed that upon binding of ABX...

Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding 'Thumb' structure

Solbiati, J.; Chapman-Smith, A.; Cronan Jr., J.
Fonte: Amer Soc Biochemistry Molecular Biology Inc Publicador: Amer Soc Biochemistry Molecular Biology Inc
Tipo: Artigo de Revista Científica
Publicado em //2002 EN
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We previously reported (Chapman-Smith, A., Forbes, B. E., Wallace, J. C., and Cronan, J. E., Jr. (1997) J. Biol. Chem. 272, 26017-26022) that the biotinylated (holo) species of the biotin carboxyl carrier protein (BCCP) biotinoyl domain is much more resistant to chemical modification and proteolysis than the unbiotinylated (apo) form. We hypothesized that the increased stability was due to a conformational change engendered by interaction of the domain with biotin protein ligase, the enzyme that attaches the biotin moiety. We now report that a BCCP-87 species to which the biotin moiety was attached by chemical acylation rather than by biotin protein ligase showed the characteristically greater stability of the holo biotinoyl domain. This result demonstrates that our hypothesis was incorrect; the attached biotin is solely responsible for the increased stability. The bacterial and chloroplast multisubunit acetyl-CoA carboxylases are unusual in that the highly symmetrical and conserved structure of the biotinoyl domain of the BCCP subunit is disrupted by a structured loop called the "thumb" that protrudes from body of the domain. Prior structural work showed that the thumb interacts with uriedo ring of the attached biotin moiety. We have tested whether the thumb-biotin interactions are responsible for the greater holo form stability by examination of two BCCP-87 species that lack the thumb. These BCCP species were produced in both the apo and holo forms...

BioMoleculesAlive.org: the biochemistry and molecular biology digital library

Craig, Paul
Fonte: Elsevier: Biochemistry and Molecular Biology Education Publicador: Elsevier: Biochemistry and Molecular Biology Education
Tipo: Artigo de Revista Científica Formato: 46888 bytes; application/pdf
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BioMoleculesAlive.org: the biochemistry and molecular biology digital library update

Craig, Paul
Fonte: Elsevier: Biochemistry and Molecular Biology Education Publicador: Elsevier: Biochemistry and Molecular Biology Education
Tipo: Artigo de Revista Científica Formato: 32362 bytes; application/pdf
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BioMoleculesAlive.org is a collection of digital resources sponsored by the American Society for Biochemistry and Molecular Biology. It is part of a larger effort called the BioSciEdNet (BEN) initiative (www.biosciednet.org). The collection will include resources in five areas: software, visual resources, curriculum resources, reviews, and articles from Biochemistry and Molecular Biology Education. Efforts on the web interface, database design, and tools and guidelines for submission to BioMoleculesAlive.org are ongoing. We hope to be open for submissions by April 2003. Please plan to attend our session at the American Society for Biochemistry and Molecular Biology (ASBMB) meeting in San Diego (12 noon on Saturday, April 12, 2003) where you will be able to hear about our progress and to meet some of the members of the steering committee. In the meantime, we have identified several examples of the types of resources we are seeking in the areas of molecular visualization, software, and curriculum. Please check out these exemplary websites for ideas on BioMoleculesAlive.org submissions of your own.

Molecular Cloning of Mouse Amino Acid Transport System B 0 , a Neutral Amino Acid Transporter Related to Hartnup Disorder

Broer, Angelika; Klingel, Karen; Kowalczuk, Sonja; Rasko, John Edward; Cavanaugh, Juleen; Broer, Stefan
Fonte: American Society for Biochemistry and Molecular Biology Inc Publicador: American Society for Biochemistry and Molecular Biology Inc
Tipo: Artigo de Revista Científica
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Resorption of amino acids in kidney and intestine is mediated by transporters, which prefer groups of amino acids with similar physico-chemical properties. It is generally assumed that most neutral amino acids are transported across the apical membrane of epithelial cells by system B 0. Here we have characterized a novel member of the Na +-dependent neurotransmitter transporter family (B0AT1) isolated from mouse kidney, which shows all properties of system B0. Flux experiments showed that the transporter is Na+-dependent, electrogenic, and actively transports most neutral amino acids but not anionic or cationic amino acids. Superfusion of mB0AT1-expressing oocytes with neutral amino acids generated inward currents, which were proportional to the fluxes observed with labeled amino acids. In situ hybridization showed strong expression in intestinal microvilli and in the proximal tubule of the kidney. Expression of mouse B0AT1 was restricted to kidney, intestine, and skin. It is generally assumed that mutations of the system B 0 transporter underlie autosomal recessive Hartnup disorder. In support of this notion mB0AT1 is located on mouse chromosome 13 in a region syntenic to human chromosome 5p15, the locus of Hartnup disorder. Thus...

Third Jesús Culebras Lecture: Molecular Biology and Clinical Nutrition; ¿where do we stand and where do we go?

Gil,Ángel
Fonte: Nutrición Hospitalaria Publicador: Nutrición Hospitalaria
Tipo: info:eu-repo/semantics/article; journal article; info:eu-repo/semantics/publishedVersion Formato: text/html; application/pdf
Publicado em 01/04/2013 ENG
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Nutrition plays a fundamental role in the maintenance of health and the treatment of disease, and serves as the crossroads for many disciplines. Biochemistry and Molecular Biology represents a key brand of science to ascertain the mechanism of action of nutrients and other food bioactive compounds in health and disease. The aim of the present Jesús M. Culebras lecture is to consider the future of the relationships between Molecular Biology and Clinical Nutrition and to discuss the use of molecular and genetic tools to study molecular responses to dietary factors and the metabolic consequences of food and to consider major challenges on human nutrition sciences in the 21st century. Particular emphasis is given to the identification and use of novel biomarkers in inflammatory diseases. Likewise, the importance of the human microbiome and how microorganisms can be safely utilized in the prevention and management of infectious and chronic diseases are discussed. Moreover, the key role of nutrigenetics, nutrigenomics and epigenetics in the new era of nutrition is considered. Nutrigenetics refers to the role of DNA sequence variation in the responses to nutrients, whereas nutrigenomics is the study of the role of nutrients in gene expression. Epigenetics is the study of mitotically heritable alterations in gene expression potential that are not caused by DNA sequence alterations. In the past decade...