Polyclonal and monoclonal antibodies against chicken gizzard 5′-nucleotidase inhibit the spreading process of chicken embryonic fibroblasts on laminin substratum

Codogno, Patrice; Doyennette-Moyne, Marie-Agnès; Auger, Michèle; Dieckhoff, J; Lietzke, Rolf; Mannherz, Hans Georg

doi:10.1016/0014-4827(88)90305-9

Cited by 40 publications

(19 citation statements)

References 22 publications

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“…Several studies suggest that eN can interact with components of the extracellular matrix. Antibodies against chicken eN inhibited spreading of chicken fibroblasts and myoblasts after their attachment to a laminin substrate [271,272]. Furthermore, eN was found to directly bind to laminin/ nidogen and fibronectin, interactions that did not involve the active site of the enzyme or the carbohydrate moieties [273,274].…”

Section: Soluble Formsmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

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: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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“…Although, Dean et al (1988) (Lesot et al, 1983) and to the extracellular matrix receptor belonging to the integrin family (Ruoslahti, 1988). Nevertheless, we cannot exclude the presence of 5 nucleotidase among the Con A binding proteins isolated which interact with LM (Dieckhoff et al, 1986) and was shown to inhibit CEF spreading on LM (Codogno et al, 1988b (Bernard ef al, 1982).…”

mentioning

confidence: 99%

Cell spreading on laminin substrate involves Con A-binding proteins

Moutsita

Botti²,

Doyennette-Moyne³

et al. 1990

Reprod. Nutr. Dévelop.

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“…The use of monoclonal antibodies has proven to be a powerful tool for examining developmentally regulated antigens in both prokaryotic and eukaryotic systems (5,10). Investigations of the cell surface's architecture and antigenic mosaic of methanosarcinae have revealed antigens whose expression is associated with morphology (22,23), and thus these antigens can be useful as markers in the study of temporal gene expression during morphologic changes.…”

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confidence: 99%

Lamina, a novel multicellular form of Methanosarcina mazei S-6

Mayerhofer

Macario

1992

J Bacteriol

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A novel multicellular form of Methanosarcina mazei S-6 is described. It was termed lamina, and it formed during the exponential growth phase when packets or single cells were grown in 40 mM trimethylamine and a total concentration of 8.3 to 15.6 mM Ca2`and/or Mg2+, in cultures that were not shaken. A distinct molecular event represented by the increment in expression and a spatial redistribution of an antigen during lamina formation is documented.Methanosarcinae are the only members of the archaebacterial domain, Archaea (33, 34), for which uni-and multicellular forms have been observed (20,26,29,31), suggesting an underlying complexity in gene regulation not hitherto observed in other archaebacteria. There are other features of methanosarcinae that remind one of higher organisms, such as the cell wall polymer methanochondroitin, which closely resembles eukaryotic chondroitin (14, 15). Also, Methanosarcina gene organization, although typically prokaryotic, shows conserved molecules involved in replication, transcription, and translation with a higher degree of homology to those of eukaryotes than to those of eubacteria (4,33,37).Among methanosarcinae, Methanosarcina mazei S-6 (20, 21) is one of the better-studied species in pure culture concerning different morphologies-i.e., single cells and small and large packets (1,12,26,27,35). These morphologies have also been observed in complex ecosystems like anaerobic bioreactors (18). Different morphologies allow analysis from various perspectives. Packets of M. mazei S-6 can easily be monitored in different types of anaerobic bioreactors (18,19), whereas single cells facilitate molecular biologic studies (12). In addition, the multicellular structures in M. mazei S-6 afford the opportunity to examine cell-cell interaction in archaebacteria.The use of monoclonal antibodies has proven to be a powerful tool for examining developmentally regulated antigens in both prokaryotic and eukaryotic systems (5, 10). Investigations of the cell surface's architecture and antigenic mosaic of methanosarcinae have revealed antigens whose expression is associated with morphology (22, 23), and thus these antigens can be useful as markers in the study of temporal gene expression during morphologic changes. A multicellular form of M. mazei S-6, which we have termed lamina, and the temporal variations of a cell surface antigen (AgIc) paralleling the morphological rearrangements involved in lamina formation are described here. The word lamina best illustrates the structure's distinctive morphologic feature, i.e., its flat shape observed macro-and microscopically, its thickness being minimal in comparison with its length and width. Monoclonal antibody IC (MAbIC) generated and characterized as described previously (9, 17) was used for immunologic assays. The presence of antigen (AgIc) in sections of M. mazei S-6 was detected with MAbIC by immunohistochemistry and indirect immunofluorescence (6,7,13 (Fig. la). These packets were inoculated into medium containing 40

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Polyclonal and monoclonal antibodies against chicken gizzard 5′-nucleotidase inhibit the spreading process of chicken embryonic fibroblasts on laminin substratum

Cited by 40 publications

References 22 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Cell spreading on laminin substrate involves Con A-binding proteins

Lamina, a novel multicellular form of Methanosarcina mazei S-6

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