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PubMed · 8645316

Fibronectin harbors anticell adhesive activity.

F Fukai·H Takahashi·Y Habu·N Kubushiro·T Katayama
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Abstract

Effect of fibronectin (FN) fragment derived from the carboxyl-terminal heparin-binding (Hep 2) domain on cell adhesion was studied. A 30-kDa Hep 2 fragment showed no significant effect on adhesion of Mardin Darbyn caine kidney (MDCK) cells to FN substrate, whereas after exposure to urea, the Hep 2 fragment suppressed the MDCK cell adhesion to FN in an incompetitive fashion. This anti-cell adhesive Hep 2 fragment preferentially inhibited the RGD (Arg-Gly-Asp)-dependent cell adhesion to FN. No significant binding of the Hep 2 fragment with FN was detected. Additionally, data of flow cytometry showed the presence of specific binding site for the Hep 2 fragment on MDCK cell surface. These results indicate that the Hep 2 domain of FN has a cryptic molecular region having the anti-cell adhesive activity that is probably transduced by a putative cell surface receptor.

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Amino Acid SequenceAnimalsBinding SitesCell AdhesionCell LineDogsFibronectinsFlow CytometryFluorescein-5-isothiocyanateFluorescent DyesHeparinKidneyMolecular Sequence DataOligopeptidesPeptide FragmentsUreaJournal Article

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F Fukai, H Takahashi, Y Habu, N Kubushiro, T Katayama. 1996-03-18. Fibronectin harbors anticell adhesive activity.. https://doi.org/10.1006/bbrc.1996.0416

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