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

Olmo, Nieves; Turnay, Javier; Risse, G; Deutzmann, Rainer; Mark, Klaus von der; Lizarbe, M.A.

doi:10.1042/bj2820181

Cited by 44 publications

(27 citation statements)

References 43 publications

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“…Moreover, laminin and fragments of fibronectin were found to activate eN on BCS-TC2 human colon adenocarcinoma cells. Thus, a role of eN as a cell receptor for extracellular matrix proteins was proposed [275]. In support of this, a monoclonal antibody against eN from a human pancreatic tumor cell line (PaTu 8902) reduced the attachment of these cells to a fibronectin substratum.…”

Section: Soluble Formsmentioning

confidence: 91%

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Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

891

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: Soluble Formsmentioning

confidence: 91%

“…Antibodies directed against eN or laminin specifically perturbed the association of the two proteins. Laminin stimulated and fibronectin inhibited catalytic activity [275,276]. Moreover, laminin and fragments of fibronectin were found to activate eN on BCS-TC2 human colon adenocarcinoma cells.…”

Section: Soluble Formsmentioning

confidence: 93%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

891

922

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“…More recently, these effects of these two extracellular matrix glycoproteins on AMPase activity were also demonstrated on BCS-TC2 and Rugli cells (tested as intact cells and isolated plasma membranes) [6]. By its enzymatic activity, 5'-nucleotidase is considered to be the main producer of adenosine.…”

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confidence: 93%

Dual mechanism of laminin modulation of ecto‐5′‐nucleotidase activity

Méhul

Auger

Mannherz

et al. 1993

J of Cellular Biochemistry

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The myoblast cell surface activity of ecto-5'-nucleotidase was stimulated by a laminin substrate, whereas fibronectin and gelatin did not increase the AMPase activity of ecto-5'-nucleotidase. This increase was related to a higher expression of ecto-5'-nucleotidase on the surface of cells seeded on a laminin substrate, but without the mobilization of an intracellular pool of enzyme. Furthermore, laminin and its fragments E'1 and E8 modified the AMPase activity of the ecto-5'-nucleotidase purified from chicken striated muscle and reconstituted in liposomes. Over the range of concentrations used, intact laminin and its fragment E8, consisting of the distal half of the long arm, stimulated the AMPase activity of ecto-5'-nucleotidase. By contrast, the large fragment derived from the short arms, designated E'1, inhibited the AMPase activity. Furthermore, the monoclonal anti-ecto-5'-nucleotidase antibody, CG37, abolished the stimulatory effect of fragment E8 on the AMPase activity of ecto-5'-nucleotidase but did not reverse the inhibitory effect of fragment E'1. In conclusion, laminin stimulates the AMPase activity of ecto-5'-nucleotidase by two mechanisms: inducing the expression of ecto-5'-nucleotidase to the cell surface and direct modulation of the enzymatic activity.

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“…This could be explained by two facts: first, that in the palatine tonsil extracellular fibronectin was observed in interfollicular areas but not in germinal centres [11,12], and second, that in vitro extracellular fibronectin inhibits the 5)-NT activity [13]. Thus, it is possible that in tonsillar tissue the lack of 5)-NT in interfollicular areas coincides with inhibition of this enzyme by extracellular fibronectin.…”

Section: Discussionmentioning

confidence: 97%

Localisation of Ecto-5{LC2}’- Nucleotidase and Divalent Cation-Activated Ecto-ATPase in Chronic Tonsillitis

Avramović¹,

Vlahović²,

Savić³

et al. 1998

ORL

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The histochemical localisation of two ecto-enzymes, 5′-nucleotidase (5′-NT) and Mg²⁺-ATPase, was investigated in hyperplastic and recurrent tonsillitis. Detection of enzymes was performed on frozen sections using the classical lead nitrate method. Activity of 5′-NT was demonstrated particularly in the cells of lymphoid follicles and in the basal layer of the surface tonsillar epithelium. There was no difference in localisation of 5′-NT between hyperplastic and recurrent tonsillitis, whereas a stronger reaction in follicular mantle zones was observed in recurrent tonsillitis compared to hyperplastic tonsillitis. Mg²⁺-ATPase activity was mainly associated with the cells lining the tonsillar crypt, with the interfollicular areas and blood vessels. In recurrent tonsillitis only half of the studied follicular germinal centres expressed Mg²⁺-ATPase activity, compared to hyperplastic tonsillitis. The similar localisation of 5′-NT and ecto-ATPase in both types of chronic tonsillitis suggests that in inflamed tonsils expression of investigated enzymes probably does not depend on the type of chronic tonsillitis.

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

Cited by 44 publications

References 43 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Dual mechanism of laminin modulation of ecto‐5′‐nucleotidase activity

Localisation of Ecto-5{LC2}’- Nucleotidase and Divalent Cation-Activated Ecto-ATPase in Chronic Tonsillitis

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