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Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments

Spring, J., Beck, Konrad and Chiquet-Ehrismann, R. 1989. Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell 59 (2) , pp. 325-334. 10.1016/0092-8674(89)90294-8

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Abstract

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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: Q Science > QD Chemistry
Publisher: Elsevier
ISSN: 0092-8674
Last Modified: 04 Jun 2017 03:04
URI: http://orca.cf.ac.uk/id/eprint/16300

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