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Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research.

Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Research Abstract Details 

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  • Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Abstract Text:

    s toegelS Toegel,n harrerN Harrer,v e plattnerV E Plattner,f m ungerF M Unger,h viernsteinH Viernstein,m b goldringM B Goldring,f gaborF Gabor,m wirthM Wirth,

    The present study was performed to evaluate the applicability of plant lectins as mediators of bioadhesion in cartilage research using human chondrocyte cell lines C-28/I2 and T/C-28a2. The bioadhesive properties of fluorescein-labelled lectins with different carbohydrate specificities were investigated by flow cytometry. Specificity of the lectin-cell interactions was ascertained by competitive inhibition using complementary carbohydrates. As compared to that of other lectins, the interaction between wheat germ agglutinin (WGA) and chondrocytic cells was characterised by remarkable cytoadhesion, adequate binding strength and a high degree of specificity for N-acetyl-glucosamine as contained in hyaluronan chains. We therefore suggest WGA to be a promising candidate for mediating bioadhesion to low-adhesive scaffolds in cartilage tissue engineering. Moreover, the WGA-association rate of C-28/I2 and T/C-28a2 cells was dependent on temperature indicating cellular uptake of membrane-bound WGA. Intracellular enrichment was confirmed by confocal microscopy. Equilibration of intracellular pH gradients with monensin resulted in the reversal of quenching effects indicating accumulation of WGA within acid compartments of chondrocytic cells. Thus, WGA might be internalised into chondrocytes together with hyaluronan via the CD44 receptor-mediated endocytosis pathway and accumulated within lysosomes. This physiological process could represent a feasible pathway to target WGA-functionalised drug delivery devices into chondrocytes.

    Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Publishing Authors By Initials

    s toegelS Toegel,n harrerN Harrer,ve plattnerVE Plattner,fm ungerFM Unger,h viernsteinH Viernstein,mb goldringMB Goldring,f gaborF Gabor,m wirthM Wirth,

    For similar proteins: lectins: plant lectins: wheat germ agglutinins research abstracts see: proteins: lectins: plant lectins: wheat germ agglutinins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Journal Published:

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

    Journal: Journal of controlled release : official journal o

    VOLUME: 117

    Page Numbers: 121-9

    Journal Abbreviation:

    ISSN: 0168-3659

    DAY: 6

    MONTH: 10

    YEAR: 2006

    Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 8607908

    Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Keywords Mesh Terms:

    KEYWORDS: Wheat Germ Agglutinins

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research. Information

    Substance Name: Hyaluronic Acid

    Registry Number: 9004-61-9

    Grant and Affiliation Information for Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research.

    AFFILIATION: Department of Pharmaceutical Technology and Biopharmaceutics, University of Vienna, Althanstrasse 14, A-1090 Vienna, Austria.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

    AGENCY: United States NIA

    GRANT: AG-22021

    ACRONYM: AG

    MEDLINETA: J Control Release

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Lectin binding studies on C-28/I2 and T/C-28a2 chondrocytes provide a basis for new tissue engineering and drug delivery perspectives in cartilage research Related Publications

     

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