Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments.
A structural and functional model of tenascin was elaborated using recombinant parts of three alternatively spliced tenascin variants and anti-tenascin monoclonal antibodies. The fusion proteins were compared with intact tenascin for their functions and by electron microscopy. A strong cell binding site was localized within 104 amino acids. This fragment also contains the epitope of the monoclonal antibody anti-Tn68, which inhibits cell attachment to tenascin and binds near the tips of the six arms of tenascin. In contrast, constructs containing the 13 1/2 EGF-like repeats of tenascin showed an antiadhesive effect. The coexistence of the two contrary signals on the same molecule might be responsible for the versatile features of tenascin.
Spring
J
J
Friedrich Miescher-Institut, Basel, Switzerland.
Beck
K
K
Chiquet-Ehrismann
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002448:Cell Adhesion; D015816:Cell Adhesion Molecules, Neuronal / Q000235:genetics / Q000502:physiology*; D002642:Chick Embryo; D004247:DNA / Q000235:genetics*; D015723:Gene Library; D007256:Information Systems; D007739:L Cells / Q000166:cytology; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000502:physiology*; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000648:ultrastructure; D012689:Sequence Homology, Nucleic Acid; D012867:Skin / Q000378:metabolism; D019063:Tenascin
D015816:Cell Adhesion Molecules, Neuronal; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D019063:Tenascin; D004247:DNA