Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry.

Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Abstract Text:

    benjamin a garciaBenjamin A Garcia,mark d plattMark D Platt,timothy l bornTimothy L Born,jeffrey shabanowitzJeffrey Shabanowitz,norman a marcusNorman A Marcus,donald f huntDonald F Hunt,

    Articular cartilage contains both chondrocyte cells and extracellular matrix (ECM) components. Currently, comprehensive information concerning the protein composition of human articular cartilage tissue is somewhat lacking. In this report we detail the use of tandem mass spectrometry (MS/MS) for a preliminary global identification of proteins from human articular knee cartilage tissue from patients diagnosed with osteoarthritis. Knee cartilage supernatant was fractionated using one-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis (1D-SDS-PAGE), in-gel digested and peptide sequences were then determined by performing on-line nano-liquid chromatography (LC)/MS/MS experiments using an ion trap mass spectrometer. Altogether, over 100 different proteins from nearly 700 unique peptide sequences were detected by MS/MS. The majority of the proteins identified are involved in ECM organization (35%), signal transduction and cell communication (14%), immune response (11%) and metabolism and energy pathways (11%). Proteins observed included several well-known cartilage components as well as lower abundant lesser known ECM proteins. Possible degradation products in the cartilage sample, such as from cartilage link protein, could also be detected by our mass spectrometry methods. We show here that mass spectrometry can be utilized as a tool for a fast, accurate and sensitive analysis of a complex mixture of cartilage proteins. It is believed that this type of proteomic analysis will aid future work centered on investigating the pathology of this and other related joint diseases.

    Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Publishing Authors By Initials

    ba garciaBA Garcia,md plattMD Platt,tl bornTL Born,j shabanowitzJ Shabanowitz,na marcusNA Marcus,df huntDF Hunt,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Rapid communications in mass spectrometry : RCM

    VOLUME: 20

    Page Numbers: 2999-3006

    Journal Abbreviation: Rapid Commun. Mass Spectrom.

    ISSN: 0951-4198

    DAY: 3

    MONTH: 12

    YEAR: 2006

    Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 8802365

    Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Keywords Mesh Terms:

    KEYWORDS: Spectrometry, Mass, Electrospray Ionizat

    MESH TERMS: methods

    Chemical & Substance for Abstract: Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry. Information

    Substance Name: Proteome

    Registry Number: 0

    Grant and Affiliation Information for Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry.

    AFFILIATION: Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NIGMS

    GRANT: GM37537

    ACRONYM: GM

    MEDLINETA: Rapid Commun Mass Spectrom

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Protein profile of osteoarthritic human articular cartilage using tandem mass spectrometry Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News