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Fibronectin on activated T lymphocytes is bound to gangliosides and is present in detergent insoluble microdomains
Author(s) -
Blum Stefan,
Hug Friederike,
Hänsch Gertrud M,
Wagner Christof
Publication year - 2005
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1111/j.1440-1711.2005.01318.x
Subject(s) - fibronectin , lipid microdomain , microbiology and biotechnology , gene isoform , lipid raft , extracellular matrix , ganglioside , glycoprotein , t cell , chemistry , cell , biochemistry , biology , membrane , immune system , immunology , gene
Fibronectin (FN) is a multifunctional extracellular matrix glycoprotein, which participates in cell migration and signalling to adhering cells. Due to alternative splicing and post‐translational modifications, different isoforms of FN are generated by a wide variety of cells. T lymphocytes synthesize a surface‐associated isoform of FN, containing the two ‘extradomains’ EDA and EDB. In the present study, we identified gangliosides within the T‐cell membrane as specific binding sites for the N‐terminal 30 kDa fragment of FN. When T cells were activated with anti‐CD3 coated beads, FN, together with the ganglioside GM1, converged at the contact zone. Moreover, endogenous FN was present in the detergent insoluble microdomain. The function of FN in T cells is still under investigation; however, its presence together with gangliosides at the activation site suggests participation in T‐cell signalling.