A Mr 72K cell surface concanavalin A binding glycoprotein is specifically involved in the spreading of chick embryo fibroblasts onto laminin substrate

Moutsita, Richard; Auger, Michèle; Codogno, Patrice

doi:10.1016/0014-4827(91)90181-s

Cited by 6 publications

(1 citation statement)

References 46 publications

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“…These changes can be induced either by direct interaction or indirectly as a result of the laminin interaction with other cellular receptors. Recently, it has been reported that cell spreading on laminin substrate involves concanavalin A-binding proteins, among them the ecto-5'nucleotidase [20,41,42]. These pieces of evidence and our own results strongly support the hypothesis of a direct interaction between laminin and 5'-nucleotidase which could take place between the El-4 and E8 fragments and 5'-nucleotidase, inducing the activity enhancement reported here.…”

Section: Discussionsupporting

confidence: 90%

Modulation of 5′-nucleotidase activity in plasma membranes and intact cells by the extracellular matrix proteins laminin and fibronectin

Olmo

Turnay

Risse

et al. 1992

Biochemical Journal

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Modulation of 5'-nucleotidase activity by the extracellular matrix proteins fibronectin, laminin and their fragments has been studied in plasma membrane preparations as well as in intact BCS-TC2 and Rugli cells. The ectoenzyme on plasma membranes is activated by laminin; fibronectin inhibits the AMPase activity on BCS-TC2 plasma membranes but no inhibitory effect is found in plasma membrane preparations from Rugli cells. These effects are dependent on the preincubation time and protein concentration. When the effect of the extracellular matrix proteins is studied on intact cells, both BCS-TC2 and Rugli cells show similar behaviour. A decrease in the enzyme activity is observed in the presence of fibronectin. The AMPase inhibitory activity is located on its 40 kDa fragment. No inhibitory activity is found in other fibronectin fragments, including the 140 kDa fragment which contains the RGDS cell-adhesion sequence. Laminin and its E1-4 and E8 fragments are able to activate the ecto-5'-nucleotidase activity of both BCS-TC2 and Rugli cells. The effect of the E1-4 fragment on intact cells is greater than that observed for the E8 fragment and uncleaved laminin. Our results suggest a bifunctional role for 5'-nucleotidase as ectoenzyme and cell receptor for extracellular matrix proteins.

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Section: Discussionsupporting

confidence: 90%