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Efficient Procedure for N-Glycan Analyses and Detection of Endo H-Like Activity in Human Tumor Specimens

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F65269705%3A_____%2F16%3A00066754" target="_blank" >RIV/65269705:_____/16:00066754 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14740/16:00088140

  • Result on the web

    <a href="https://pubs.acs.org/doi/abs/10.1021/acs.jproteome.6b00346" target="_blank" >https://pubs.acs.org/doi/abs/10.1021/acs.jproteome.6b00346</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jproteome.6b00346" target="_blank" >10.1021/acs.jproteome.6b00346</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Efficient Procedure for N-Glycan Analyses and Detection of Endo H-Like Activity in Human Tumor Specimens

  • Original language description

    Although the importance of glycosylation has been thoroughly recognized in association with a number of biological processes, efficient assessments of glycans have been hampered by both the limited size of specimens and lengthy sample preparations, particularly in clinical settings. Here we report a simple preparative method for N-glycan analyses. It involves only short one-step chloroform methanol extraction in presence or absence of water prior to PNGase F deglycosylation. The procedure was successfully applied to the investigation of N-glycans obtained from small numbers of in vitro cultured cancer cells (&lt;= 1 x 10(5)) and to tumor tissues, including patient biopsies of small size. MALDI-MS analysis confirmed the efficient release of all N-glycan types including complex forms with poly-N-acetyllactosamine chains. In addition, nonaqueous extraction of specimens from several established cancer cell lines, as well as patient tumor tissues, yielded high-mannose glycans with one G1cNAc moiety (Man(3-9)GlcNAc), strongly suggesting preservation of enzymatic activity analogous to Endo H enzyme. In summary, the method is both a step toward the practical use of glycan profiling and a way to detect Endo H-like activity in cancer specimens.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30200 - Clinical medicine

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Proteome Research

  • ISSN

    1535-3893

  • e-ISSN

  • Volume of the periodical

    15

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    2777-2786

  • UT code for WoS article

    000381235900039

  • EID of the result in the Scopus database

    2-s2.0-84981298723