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  1. Article ; Online: Rapid and parallel changes in activity and mRNA of intestinal peptidase to match altered dietary protein levels in juvenile house sparrows (

    Brun, Antonio / Magallanes, Melisa E / Karasov, William H / Caviedes-Vidal, Enrique

    The Journal of experimental biology

    2021  Volume 224, Issue Pt 3

    Abstract: Although dietary flexibility in digestive enzyme activity (i.e. reaction rate) is widespread in vertebrates, mechanisms are poorly understood. When laboratory rats are switched to a higher protein diet, the activities of apical intestinal peptidases ... ...

    Abstract Although dietary flexibility in digestive enzyme activity (i.e. reaction rate) is widespread in vertebrates, mechanisms are poorly understood. When laboratory rats are switched to a higher protein diet, the activities of apical intestinal peptidases increase within 15 h, in some cases by rapid increase in enzyme transcription followed by rapid translation and translocation to the intestine's apical, brush-border membrane (BBM). Focusing on aminopeptidase-N (APN), we studied intestinal digestive enzyme flexibility in birds, relying on activity and mRNA data from the same animals. Our model was nestling house sparrows (
    MeSH term(s) Animals ; Dietary Proteins ; Digestion ; Peptide Hydrolases ; RNA, Messenger/genetics ; Sparrows
    Chemical Substances Dietary Proteins ; RNA, Messenger ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2021-02-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218085-6
    ISSN 1477-9145 ; 0022-0949
    ISSN (online) 1477-9145
    ISSN 0022-0949
    DOI 10.1242/jeb.234708
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2629: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Opportunities Lost? Evolutionary Causes and Ecological Consequences of the Absence of Trehalose Digestion in Birds.

    Brun, Antonio / Gutiérrez-Guerrero, Yocelyn / Magallanes, Melisa E / Caviedes-Vidal, Enrique / Karasov, William H / Martínez Del Rio, Carlos

    Physiological and biochemical zoology : PBZ

    2022  Volume 95, Issue 4, Page(s) 340–349

    Abstract: AbstractTrehalose is a nonreducing disaccharide that is a primary storage and energy source in prokaryotes, yeasts, fungi, and invertebrates. Vertebrates digest trehalose with the intestinal brush border membrane (BBM) enzyme trehalase. Intestinal ... ...

    Abstract AbstractTrehalose is a nonreducing disaccharide that is a primary storage and energy source in prokaryotes, yeasts, fungi, and invertebrates. Vertebrates digest trehalose with the intestinal brush border membrane (BBM) enzyme trehalase. Intestinal trehalase activity is reported to be either very low or absent in several bird species. We assayed trehalase activity in 19 avian species, used proteomic analysis to quantify its abundance in the intestinal BBM, and used analyses of available genomes to detect the presence of the gene that codes for trehalase (
    MeSH term(s) Animals ; Birds ; Digestion ; Proteomics ; Trehalase/genetics ; Trehalose ; Vertebrates
    Chemical Substances Trehalose (B8WCK70T7I) ; Trehalase (EC 3.2.1.28)
    Language English
    Publishing date 2022-05-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1473845-4
    ISSN 1537-5293 ; 1522-2152
    ISSN (online) 1537-5293
    ISSN 1522-2152
    DOI 10.1086/720232
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Dietary adaptation to high starch involves increased relative abundance of sucrase-isomaltase and its mRNA in nestling house sparrows.

    Brun, Antonio / Magallanes, Melisa E / Barrett-Wilt, Gregory A / Karasov, William H / Caviedes-Vidal, Enrique

    American journal of physiology. Regulatory, integrative and comparative physiology

    2020  Volume 320, Issue 2, Page(s) R195–R202

    Abstract: Dietary flexibility in digestive enzyme activity is widespread in vertebrates but mechanisms are poorly understood. When laboratory rats are switched to a higher carbohydrate diet, the activities of the apical intestinal α-glucosidases (AGs) increase ... ...

    Abstract Dietary flexibility in digestive enzyme activity is widespread in vertebrates but mechanisms are poorly understood. When laboratory rats are switched to a higher carbohydrate diet, the activities of the apical intestinal α-glucosidases (AGs) increase within 6-12 h, mainly by rapid increase in enzyme transcription, followed by rapid translation and translocation to the intestine's apical, brush-border membrane (BBM). We performed the first unified study of the overall process in birds, relying on activity, proteomic, and transcriptomic data from the same animals. Our avian model was nestling house sparrows (
    MeSH term(s) Adaptation, Physiological/drug effects ; Aging ; Animal Feed ; Animals ; Diet/veterinary ; Dietary Carbohydrates/pharmacology ; Gene Expression Regulation, Enzymologic/drug effects ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Sparrows/physiology ; Starch/administration & dosage ; Starch/pharmacology ; Sucrase-Isomaltase Complex/genetics ; Sucrase-Isomaltase Complex/metabolism
    Chemical Substances Dietary Carbohydrates ; RNA, Messenger ; Starch (9005-25-8) ; Sucrase-Isomaltase Complex (EC 3.2.1.-)
    Language English
    Publishing date 2020-11-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 603839-6
    ISSN 1522-1490 ; 0363-6119
    ISSN (online) 1522-1490
    ISSN 0363-6119
    DOI 10.1152/ajpregu.00181.2020
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.89: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: A Fast and Accurate Method to Identify and Quantify Enzymes in Brush-Border Membranes: In Situ Hydrolysis Followed by Nano LC-MS/MS.

    Brun, Antonio / Magallanes, Melisa E / Martínez Del Rio, Carlos / Barrett-Wilt, Gregory A / Karasov, William H / Caviedes-Vidal, Enrique

    Methods and protocols

    2020  Volume 3, Issue 1

    Abstract: A simple method for the identification of brush-border membrane α-glucosidases is described. The proteins were first solubilized and separated in a gel under native, non-denaturing, conditions. The gel was then incubated in substrate solutions (maltose ... ...

    Abstract A simple method for the identification of brush-border membrane α-glucosidases is described. The proteins were first solubilized and separated in a gel under native, non-denaturing, conditions. The gel was then incubated in substrate solutions (maltose or sucrose), and the product (glucose) exposed in situ by the oxidation of o-dianisidine, which yields a brown-orange color. Nano-liquid chromatography coupled to mass spectrometry analyses of proteins (nano LC-MS/MS) present in the colored bands excised from the gels, was used to confirm the presence of the enzymes. The stain is inexpensive and the procedure permits testing several substrates in the same gel. Once enzymes are identified, their abundance, relative to that of other proteins in the brush border, can be semi-quantified using nano LC-MS/MS.
    Language English
    Publishing date 2020-02-10
    Publishing country Switzerland
    Document type Journal Article
    ISSN 2409-9279
    ISSN (online) 2409-9279
    DOI 10.3390/mps3010015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Duplications and Functional Convergence of Intestinal Carbohydrate-Digesting Enzymes.

    Brun, Antonio / Mendez-Aranda, Daniel / Magallanes, Melisa E / Karasov, William H / Martínez Del Rio, Carlos / Baldwin, Maude W / Caviedes-Vidal, Enrique

    Molecular biology and evolution

    2020  Volume 37, Issue 6, Page(s) 1657–1666

    Abstract: Vertebrate diets and digestive physiologies vary tremendously. Although the contribution of ecological and behavioral features to such diversity is well documented, the roles and identities of individual intestinal enzymes shaping digestive traits remain ...

    Abstract Vertebrate diets and digestive physiologies vary tremendously. Although the contribution of ecological and behavioral features to such diversity is well documented, the roles and identities of individual intestinal enzymes shaping digestive traits remain largely unexplored. Here, we show that the sucrase-isomaltase (SI)/maltase-glucoamylase (MGAM) dual enzyme system long assumed to be the conserved disaccharide and starch digestion framework in all vertebrates is absent in many lineages. Our analyses indicate that independent duplications of an ancestral SI gave rise to the mammalian-specific MGAM, as well as to other duplicates in fish and birds. Strikingly, the duplicated avian enzyme exhibits similar activities to MGAM, revealing an unexpected case of functional convergence. Our results highlight digestive enzyme variation as a key uncharacterized component of dietary diversity in vertebrates.
    MeSH term(s) Animals ; Carbohydrate Metabolism/genetics ; Chickens ; Evolution, Molecular ; Gene Duplication ; Mice ; Rats ; Songbirds ; Vertebrates/genetics ; Vertebrates/metabolism ; alpha-Glucosidases/genetics ; alpha-Glucosidases/metabolism
    Chemical Substances alpha-Glucosidases (EC 3.2.1.20)
    Language English
    Publishing date 2020-03-17
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 998579-7
    ISSN 1537-1719 ; 0737-4038
    ISSN (online) 1537-1719
    ISSN 0737-4038
    DOI 10.1093/molbev/msaa034
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2137: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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