Cell spreading on laminin substrate involves Con A-binding proteins

Moutsita, Richard; Botti, Joëlle; Doyennette-Moyne, MA; Auger, Michèle; Codogno, Patrice

doi:10.1051/rnd:19900312

Cited by 2 publications

(2 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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

View full text Add to dashboard Cite

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.

show abstract

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

View full text Add to dashboard Cite

show abstract

“…Con A binds specifically to terminal mannose residues on cell surface glycoproteins and glycolipids and it has been widely used in studies of cell attachment, cell shape, cytoskeletal integrity, and cell proliferation. The presence of Con A in solution prevents attachment (Prinz and VonFigura, 1978) and flattening (Grinnell, 1978; 0 1995 WILEY-LISS, INC Codogno et al, 1988;Moutsita et al, 1990) of several cell types on substrates that are normally permissive for these processes, although cells will attach and flatten on substrates coated with Con A. The presence of Con A has been correlated with decreases in the amount of tubulin assembled into microtubules (Ostlund et al, 1980;Bod0 et al, 1990a,b) and a reduction of actin in stress fibers (Badley et al, 1981); binding of Con A to the cell surface has also been shown to be affected by the integrity of actin-containing filaments (Thom et al, 1979;Bourguignon, 1980).…”

mentioning

confidence: 99%

EGF receptor‐mediated signals are differentially modulated by concanavalin A

Hazan¹,

Krushel²,

Crossin³

1995

Journal Cellular Physiology

View full text Add to dashboard Cite

NIH 3T3 cells expressing high levels of the human epidermal growth factor (EGF) receptor were used to examine the effects of the lectin concanavalin A (Con A) on EGF-mediated signaling events. Proliferation of NIH 3T3 cells expressing high levels of the human EGF receptor was inhibited in a dose-dependent manner by Con A. At the same time, Con A also inhibited both dimerization and tyrosine phosphorylation of the EGF receptor. Tyrosine phosphorylation of the enzyme phospholipase C-gamma, a substrate of the phosphorylated EGF receptor kinase, was also inhibited. In contrast, EGF-stimulated changes in pH, calcium, and levels of inositol phosphates were unaffected by the presence of Con A. These results indicate that certain signals (changes in the levels of intracellular calcium, pH, and inositol phosphates) mediated by EGF binding to its receptor still occur when receptor dimerization and phosphorylation are dramatically decreased, suggesting that multiple independent signals are transmitted by the binding of EGF to its receptor.

show abstract

Cell spreading on laminin substrate involves Con A-binding proteins

Cited by 2 publications

References 8 publications

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

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

EGF receptor‐mediated signals are differentially modulated by concanavalin A

Contact Info

Product

Resources

About