Vigny M

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Full name : Vigny Marc

First name : Marc

Mail : UMR_S839 INSERM\/UPMC, Institut du Fer a Moulin (IFM), UPMC, Paris

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Country : France

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References (34)

Title : In vivo proliferative pattern of trembler hypomyelinating Schwann cells is modified in culture: an experimental analysis - Do Thi_1993_Dev.Neurosci_15_10
Author(s) : Do Thi NA , Koenig HL , Vigny M , Fournier M , Ressouches A
Ref : Developmental Neuroscience , 15 :10 , 1993
Abstract : Trembler mouse, a Schwann cell mutation, is characterized by severe hypomyelination of peripheral nerves, high Schwann cell proliferation and the presence of a multilayered basal lamina which surrounds them. In contrast with their continuous in vivo division, mutant Schwann cells prepared from 15-day sciatic nerves display a lower proliferation rate in cell culture than normal Schwann cells. However, quiescent Trembler Schwann cells are still able to respond, as normal Schwann cells, to exogenous mitogens, such as nerve extracts and myelin-enriched fractions. In addition, both normal and Trembler Schwann cells proliferate in response to Trembler serum. Fibroblast growth factor is not the mitogenic factor which stimulates mutant Schwann cell proliferation in vivo, since it is absent in Trembler serum and poorly concentrated in Trembler adult sciatic nerves. Our results suggest that, in vivo, the serum of Trembler mouse probably contains mitogenic factors, not yet characterized, which may trigger the permanent division of mutant Schwann cells, in contrast to the quiescent state of these cells in the nerves of normal mice.
ESTHER : Do Thi_1993_Dev.Neurosci_15_10
PubMedSearch : Do Thi_1993_Dev.Neurosci_15_10
PubMedID: 8269863

Title : Molecular forms of acetylcholinesterase in dystrophic (mdx) mouse tissues - Oliver_1992_Neuromuscul.Disord_2_87
Author(s) : Oliver LJ , Chatel JM , Massoulie J , Vigny M , Vallette FM
Ref : Neuromuscular Disorders , 2 :87 , 1992
Abstract : We analyzed the activity of acetylcholinesterase (AChE) and its molecular forms in the tissues of normal and dystrophic (mdx) mice, at different developmental stages. We studied the brain, the heart and the serum, in addition to four predominantly fast-twitch muscles (tibialis, plantaris, gastrocnemius and extensor digitorum longus (EDL)) and the slow-twitch, soleus muscle. We found no difference between mdx and control mice in the AChE activity of the brain and the heart. The skeletal muscles affected by the disease undergo active degeneration counterbalanced by regeneration between 3 and 14 weeks after birth. The distribution of AChE patches associated with neuromuscular junctions was abnormally scattered in mdx muscles, and in some cases (tibialis and soleus), the number of endplates was more than twice that of normal muscles. There were only minor differences in the concentration and pattern of AChE molecular forms during the acute phase of muscle degeneration and regeneration. After this period, however, we observed a marked deficit in the membrane-bound G4 molecular form of AChE in adult mdx tibialis, gastrocnemius and EDL but not in the plantaris or in the soleus, as compared with their normal counterparts. Whereas the amount of AChE markedly decreased in the serum of normal mice during the first weeks of life, it remained essentially unchanged in the serum of mdx mice. It is likely that this excess of AChE activity in serum originates from the muscles. A deficit in muscle G4 was also reported in other forms of muscular dystrophy in the mouse and chicken. Since it is not correlated to the acute phase of the disease in mdx and also occurs in genetically different dystrophies, it probably represents a secondary effect of the dystrophy.
ESTHER : Oliver_1992_Neuromuscul.Disord_2_87
PubMedSearch : Oliver_1992_Neuromuscul.Disord_2_87
PubMedID: 1422203

Title : Acetylcholinesterase in cocultures of rat myotubes and spinal cord neurons: effects of collagenase and cis-hydroxyproline on molecular forms, intra- and extracellular distribution, and formation of patches at neuromuscular contacts - Vallette_1990_J.Neurochem_54_915
Author(s) : Vallette FM , De La Porte S , Koenig J , Massoulie J , Vigny M
Ref : Journal of Neurochemistry , 54 :915 , 1990
Abstract : Cultures of rat myotubes from 18-day-old embryos produce both globular (G) and asymmetric (A) forms of acetylcholinesterase (AChE; EC 3.1.1.7), mostly G1, G4, and A12 and a small proportion of A8. We show that all forms are partly intracellular and partly exposed to the extracellular medium; the A forms and their intra- and extracellular distribution are not modified when myotubes are grown in the presence of spinal cord neurons. In these cocultures, however, AChE patches may be detected immunohistochemically at sites of neuromuscular contacts. These patches represent a very minor proportion of AChE activity. We found that collagenase removes AChE patches but not the acetylcholine receptor clusters with which they coincide. This digestion specifically decreases the level of the A12 form. cis-Hydroxyproline, an inhibitor of collagen synthesis, reduces the level of G1 and blocks the synthesis of A forms.
ESTHER : Vallette_1990_J.Neurochem_54_915
PubMedSearch : Vallette_1990_J.Neurochem_54_915
PubMedID: 2154553

Title : Monoclonal antibodies against acetylcholinesterase from electric organs of Electrophorus and Torpedo - Musset_1987_Biochimie_69_147
Author(s) : Musset F , Frobert Y , Grassi J , Vigny M , Boulla G , Bon S , Massoulie J
Ref : Biochimie , 69 :147 , 1987
Abstract : We studied the reactivity of monoclonal antibodies (mAbs) raised against acetylcholinesterase (AChE) purified from Electrophorus and Torpedo electric organs. We obtained IgG antibodies (Elec-21, Elec-106, Tor-3E5, Tor-ME8, Tor-1A5), all of them directed against the catalytic subunit of the corresponding species, with no significant cross-reactivity. These antibodies do not inhibit the enzyme and recognize all molecular forms, globular (G) and asymmetric (A). Tor-ME8 reacts specifically with the denatured A and G subunits of Torpedo AChE, in immunoblots. Several hybridomas raised against Electrophorus AChE produced IgM antibodies (Elec-39, Elec-118, Elec-121). These antibodies react with the A forms of Electrophorus electric organs and also with a subset of dimers (G2) from Torpedo electric organ. In addition, they react with a number of non-AChE components, in immunoblots. In contrast, they do not recognize AChE from other Electrophorus tissues or A forms from Torpedo electric organs.
ESTHER : Musset_1987_Biochimie_69_147
PubMedSearch : Musset_1987_Biochimie_69_147
PubMedID: 3105603

Title : Presynaptic or postsynaptic origin of acetylcholinesterase at neuromuscular junctions? An immunological study in heterologous nerve- muscle cultures - De La Porte_1986_Dev.Biol_116_69
Author(s) : De La Porte S , Vallette FM , Grassi J , Vigny M , Koenig J
Ref : Developmental Biology , 116 :69 , 1986
Abstract : Numerous studies have shown that the acetylcholine receptor (AChR) is inserted in the plasma membrane of the muscle fiber, and that it is focalized at the site of neuromuscular junctions, as an effect of neural influence. In contrast, acetylcholinesterase (AChE) may be presynaptic or anchored in the basal lamina, as well as postsynaptic at neuromuscular junctions. We investigated the origin of the junctional enzyme, particularly the collagen-tailed asymmetric A12 forms, by studying the AChE contents of heterologous rat and chicken neuromuscular cocultures by immunohistochemical and biochemical methods. We found that the overall content of AChE, in the neuromuscular cocultures, including the A12 form, was essentially identical to the sum of the contents of separate myotube and motoneuron cultures. The sedimentation coefficients of the rat and chicken asymmetric forms are sufficiently different to clearly differentiate these enzymes in sucrose gradients: 16 S for rat, 20 S for chicken A12 AChE. Sedimentation analyses of AChE in cocultures thus showed that the A12 form was of muscular origin. In the case of aneural cultures of myotubes, histochemical staining of AChE activity or immunohistochemical staining with specific antibodies showed only very scarce, faint concentrations of enzyme. Some patches of acetylcholine receptor (AChR) were, however, visible in these cultures. Neuromuscular contacts are readily established in cocultures of myotubes with embryonic motoneurons from spinal cords. In the presence of motoneurons, the myotubes presented a larger number of AChR patches. The most remarkable feature of neuromuscular cocultures was the presence of numerous intense AChE patches which always coincided with AChR clusters. By specifically staining nerve terminals with tetanus toxin, we could show an excellent correlation between neuromuscular contacts and the presence of AChE-AChR patches. We found that the AChE patches in heterologous cocultures could be stained exclusively by the anti-myotube AChE antiserum. The focalized enzyme is therefore exclusively, or very predominantly, provided by the myotube.
ESTHER : De La Porte_1986_Dev.Biol_116_69
PubMedSearch : De La Porte_1986_Dev.Biol_116_69
PubMedID: 3525279

Title : Stimulation of denervated rat soleus muscle with fast and slow activity patterns induces different expression of acetylcholinesterase molecular forms - Lomo_1985_J.Neurosci_5_1180
Author(s) : Lomo T , Massoulie J , Vigny M
Ref : Journal of Neuroscience , 5 :1180 , 1985
Abstract : The relative amount and distribution of acetylcholinesterase (AChE) molecular forms were studied in slow soleus and (less extensively) in fast extensor digitorum longus (EDL) muscles of the rat before and after denervation and direct stimulation. Normal EDL muscles showed higher total and specific AChE activity than normal soleus muscles and contained essentially three different molecular AChE forms (G1, G4, and A12) as opposed to six forms (G1, G2, G4, A4, A8, and A12) in the soleus. Denervation reduced AChE activity in both muscles. In the soleus direct stimulation starting 2 to 3 weeks after denervation increased the specific AChE activity markedly. The increase started 12 to 24 hr after the onset of stimulation, reached 3 to 5 times normal values after 2 to 7 days, and then declined gradually toward normal values over the next 2 weeks. Furthermore, the effect on the different molecular forms depended strongly on the stimulus pattern. Thus, intermittent 100 Hz stimulation (fast pattern) induced essentially the three forms typical of the normal EDL, whereas continuous 10 Hz stimulation induced the six forms characteristic of normal soleus muscles but with some differences in their relative proportions. In the EDL, 2 days of continuous 10 Hz stimulation (the only duration and pattern examined) failed to induce a similar increase in AChE activity.
ESTHER : Lomo_1985_J.Neurosci_5_1180
PubMedSearch : Lomo_1985_J.Neurosci_5_1180
PubMedID: 3998815

Title : The polymorphism of cholinesterases: classification of molecular forms\; Interactions and solubilization characteristics metabolic relationships and regulations -
Author(s) : Massoulie J , Bon S , Lazar M , Grassi J , Marsh D , Meflah K , Toutant JP , Vallette FM , Vigny M
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter :73 , 1984
PubMedID:

Title : Action of veratridine on acetylcholinesterase in cultures of rat muscle cells - De La Porte_1984_Dev.Biol_106_450
Author(s) : De La Porte S , Vigny M , Massoulie J , Koenig J
Ref : Developmental Biology , 106 :450 , 1984
Abstract : Studies on cultures of embryonic rat muscle cells have suggested that the presence of collagen-tailed forms may be correlated with spontaneous contractile activity: these forms disappear in the presence of tetrodotoxin which blocks the sodium channels involved in the propagation of action potentials. The effect of veratridine, a drug which maintains the sodium channels in the open state, was studied. It is shown here that in young cultures veratridine provoked a dramatic increase in total acetylcholinesterase activity and changed the distribution of the molecular forms of the enzyme, increasing the proportion and absolute amount of the A12 form. In order to elucidate the mechanism of action of this drug, the effects of various ions, ionophores, or other agents that modify the ionic permeabilities of membranes were also investigated.
ESTHER : De La Porte_1984_Dev.Biol_106_450
PubMedSearch : De La Porte_1984_Dev.Biol_106_450
PubMedID: 6437894

Title : Poster 15. An Immunological study of mammalian acetylcholinesterase using anti-rat serum -
Author(s) : Grassi J , Marsh D , Vigny M , Massoulie J
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
PubMedID:

Title : Heavy isotope-labeling study of the metabolism of monomeric and tetrameric acetylcholinesterase forms in the murine neuronal-like T 28 hybrid cell line - Lazar_1984_J.Biol.Chem_259_3703
Author(s) : Lazar M , Salmeron E , Vigny M , Massoulie J
Ref : Journal of Biological Chemistry , 259 :3703 , 1984
Abstract : We have used the method of heavy isotope labeling to study the metabolic turnover of acetylcholinesterase forms in the neuroblastoma-derived T 28 hybrid cells in their differentiated state. These cells contain mostly G1 and G4 forms, together with a small proportion of G2, and secrete all these forms into the culture medium. The cells maintained constant and equal levels of acetylcholinesterase, with the same proportions of molecular forms, in a medium containing heavy isotope-labeled amino acids and in a control light medium of similar composition. In addition, they secreted acetylcholinesterase at the same rate in both media. After transfer of the cells into the heavy medium, heavy isotope-labeled acetylcholinesterase molecules progressively replace preexisting light molecules. We analyzed heavy and light components of acetylcholinesterase for each of the two major G1 and G4 forms, by reconstructing the pattern obtained in sucrose gradient differential sedimentation, using combinations of weighted elementary distributions. Heavy molecules were detected in cellular extracts after about 30 min for G1 and 3 h for G4. Both heavy forms also appeared in the medium after a lag of about 3 h. The cellular complement of G1 was renewed much faster than that of G4, the levels of the light forms being reduced to 50% of the original level after 3.5 and 40 h, respectively. Each of these forms appeared to consist of several metabolic pools, and we present simplified models which describe their possible relationships.
ESTHER : Lazar_1984_J.Biol.Chem_259_3703
PubMedSearch : Lazar_1984_J.Biol.Chem_259_3703
PubMedID: 6706975

Title : Poster 39 . Ultrastructural localisation of acetylcholinesterase at the neuro-muscular junction. Immunocytochemical and biochemical study using monoclonal antibodies -
Author(s) : Mailly P , Vigny M , Koenig HL
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
PubMedID:

Title : Poster 41. Acetylcholinesterase focalized at neuromuscular contacts: Neuronal or muscular origin? -
Author(s) : De La Porte S , Marsh D , Grassi J , Vallette FM , Vigny M , Koenig J
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
PubMedID:

Title : An immunological study of rat acetylcholinesterase: comparison with acetylcholinesterases from other vertebrates - Marsh_1984_J.Neurochem_43_204
Author(s) : Marsh D , Grassi J , Vigny M , Massoulie J
Ref : Journal of Neurochemistry , 43 :204 , 1984
Abstract : We have examined the immunoreactivity of acetylcholinesterase from different vertebrate species with a rabbit antiserum raised against the purified rat brain hydrophobic enzyme (G4 form). We found no significant interaction with enzymes from Electrophorus, Torpedo, chicken, and rabbit. The antiserum reacted with acetylcholinesterases from the brains of the other mammalian species studied, with titers decreasing in the following order: rat = mouse greater than human greater than bovine. The serum was inhibitory with murine and human acetylcholinesterases, but not with the bovine enzyme. The inhibition was partially depressed in the presence of salt (e.g., 1 M NaCl). In those species whose acetylcholinesterase was recognized by the antiserum, both soluble and detergent-soluble fractions behaved in essentially the same manner, interacting with the same antibodies. The apparent immunoprecipitation titer was decreased in the presence of salt, and it did not make any difference whether NaCl was included in the solubilization procedure or added to the extracts. Both G1 and G4 forms of acetylcholinesterase in the soluble and detergent-soluble fractions were recognized by the antiserum, and in the case of the human enzyme, by monoclonal antibodies produced against human erythrocyte acetylcholinesterase. However, the monomer G1 showed a clear tendency to form smaller complexes and precipitate less readily than the tetramer G4. Although we cannot exclude the existence of significant differences between the various molecular forms of acetylcholinesterase, our results are consistent with the hypothesis that they all derive from the same gene or set of genes by posttranslational modifications.
ESTHER : Marsh_1984_J.Neurochem_43_204
PubMedSearch : Marsh_1984_J.Neurochem_43_204
PubMedID: 6374038

Title : Poster 46. Denervation of sternocleidomastoid muscle in trembler dysmyelinating mutant as compared to control mouse -
Author(s) : Do Thi NA , Koenig HL , Vigny M
Ref : In: Cholinesterases, fundamental and applied aspects : proceedings of the Second International Meeting on Cholinesterases , (Brzin M, Barnard EA, Sket D, Eds) De Gruyter , 1984
PubMedID:

Title : Laminin induces acetylcholine receptor aggregation on cultured myotubes and enhances the receptor aggregation activity of a neuronal factor - Vogel_1983_J.Neurosci_3_1058
Author(s) : Vogel Z , Christian CN , Vigny M , Bauer HC , Sonderegger P , Daniels MP
Ref : Journal of Neuroscience , 3 :1058 , 1983
Abstract : The effect of several basement membrane components on the aggregation of acetylcholine (ACh) receptors on cultured myotubes was studied. Cultures were incubated for 16 to 24 hr with laminin, a heparan sulfate proteoglycan, collagen types IV and V, or fibronectin, alone, or together with medium conditioned by NG108-15 neuroblastoma X glioma hybrid cells (NCM). The number of ACh receptor aggregates per myotube was assayed by fluorescence microscopy of cultures stained with tetramethylrhodamine-labeled alpha-bungarotoxin. Laminin induced ACh receptor aggregation on primary rat myotubes and on myotubes formed by G8-1 clonal rat muscle cells. Laminin enhanced the receptor-aggregating activity of NCM in a concentration-dependent manner (0.6 to 6.0 micrograms/ml) and the number of aggregates formed in the presence of laminin and NCM together was greater than the sum of the aggregates induced by NCM and laminin separately. The aggregation factor in NCM is probably not laminin, since less than 10 ng/ml of laminin-like immunoreactivity was detected in NCM, and antiserum against laminin blocked the effects of laminin but had little effect on NCM aggregation activity. Collagen type V enhanced the receptor aggregation activity of NCM, but less strongly than laminin, and had little or no effect by itself. The other basement membrane components did not induce receptor aggregation or enhance the effect of NCM. Experiments in which ACh receptors were labeled before exposure of cultures to NCM and laminin indicated that laminin enhanced the rearrangement of receptors at the cell surface. Immunofluorescence microscopy indicated that laminin binds to the myotubes within 30 min and forms patches on the cell surface over a period of hours. Laminin bound to the myotube surface enhanced receptor aggregation as well as laminin continuously present in the culture medium. The results suggest the possibility that laminin could enhance the receptor aggregation activity of a neuronal factor(s) released at the developing neuromuscular junction.
ESTHER : Vogel_1983_J.Neurosci_3_1058
PubMedSearch : Vogel_1983_J.Neurosci_3_1058
PubMedID: 6341513

Title : Interactions of asymmetric forms of acetylcholinesterase with basement membrane components - Vigny_1983_J.Biol.Chem_258_8794
Author(s) : Vigny M , Martin GR , Grotendorst GR
Ref : Journal of Biological Chemistry , 258 :8794 , 1983
Abstract : Previous studies have indicated that the asymmetric form of acetylcholinesterase is localized in the basement membrane zone of the neuromuscular junction. We find that the collagenous subunit of the enzyme is required for interactions with basement membrane components. Acetylcholinesterase (the A12 form) binds best to the basement membrane heparan sulfate proteoglycan and type V collagen, to a lesser extent to laminin, fibronectin, and type I collagen, but not to type IV collagen. In addition, the purified A12 enzyme as prepared from electric eel is associated with a heparan sulfate-like component which appears to be responsible for the aggregation of the enzyme at low ionic strength. We observed that the purified form of the enzyme reacted with antibodies to type V collagen, and to a lesser extent with anti-type I collagen antibody, but not with anti-type IV collagen antibody. These data suggest that the collagenous subunit of the enzyme may have some similarity to type V collagen and that the interaction of the collagenous subunit with a heparan sulfate proteoglycan may be involved in its binding to basement membrane in the neuromuscular junction.
ESTHER : Vigny_1983_J.Biol.Chem_258_8794
PubMedSearch : Vigny_1983_J.Biol.Chem_258_8794
PubMedID: 6863310

Title : Molecular forms of acetylcholinesterase in bovine caudate nucleus and superior cervical ganglion: solubility properties and hydrophobic character -
Author(s) : Grassi J , Vigny M , Massoulie J
Ref : Journal of Neurochemistry , 38 :457 , 1982
PubMedID: 7108551

Title : [Motor innervation of the Trembler mouse] - Lefaix_1982_Reprod.Nutr.Dev_22_275
Author(s) : Lefaix JL , Koenig HL , Vigny M , Bourre JM
Ref : Reprod Nutr Dev , 22 :275 , 1982
Abstract : The effects on muscle fibres and particularly on their motor end-plates, by axons whose Schwann cells fail to form and maintain a normal myelin sheath, were examined by morphological and biochemical techniques. In the soleus (slow type), the innervation area was more extensive along the muscle fibre; the most frequent modifications were: abnormal axonal branching pattern, swellings of the terminal branches and terminal and preterminal sprouting. Additional clusters of ACh receptors were frequent and AChE activity was unaffected. In the fast part of the gastrocnemius, neuromuscular junctions were slightly affected: sprouting was slight and all the muscle fibres had a single cluster of AChE receptors; AChE activity was modified. In trembler mouse, the alteration of axon-Schwann cell relationships interacted with the regulatory processes ensuring the maintenance and stability of muscle fibre innervation.
ESTHER : Lefaix_1982_Reprod.Nutr.Dev_22_275
PubMedSearch : Lefaix_1982_Reprod.Nutr.Dev_22_275
PubMedID: 7156482

Title : The quaternary structure of chicken acetylcholinesterase and butyrylcholinesterase\; effect of collagenase and trypsin - Allemand_1981_J.Neurochem_36_860
Author(s) : Allemand P , Bon S , Massoulie J , Vigny M
Ref : Journal of Neurochemistry , 36 :860 , 1981
Abstract : Acetylcholinesterase (EC 3.1.1.7.; AChE) and butyrylcholinesterase (EC 3.1.1.8.; BCHE) from chicken muscle exist as sets of structurally homologous forms with very similar properties. The collagenase sensitivity and aggregation properties of the 'heavy' forms of both enzymes indicate that they possess a collagen-like tail, and their stepwise dissociation by trypsin confirms that they correspond to triple (A12) and double (A8) collagen-tailed tetramers. In addition to this dissociating effect, trypsin digests an important fraction of the catalytic units of AChE, in a progressive manner, removing as much as 30% of the enzyme's mass, without inactivation of the tetramers and of the tailed molecules. The trypsin-modified AChE forms closely resemble the corresponding mammalian AChE forms in their hydrodynamic properties. It is not known whether the trypsin-digestible peptides, which do not appear to be involved in the ionic or hydrophobic interactions of the enzymes, are a fragment of the catalytic subunit or whether they constitute distinct polypeptides.
ESTHER : Allemand_1981_J.Neurochem_36_860
PubMedSearch : Allemand_1981_J.Neurochem_36_860
PubMedID: 6259292

Title : Spontaneous contractile activity and the presence of the 16 S form of acetylcholinesterase in rat muscle cells in culture: reversible suppressive action of tetrodotoxin -
Author(s) : Rieger F , Koenig J , Vigny M
Ref : Developmental Biology , 76 :358 , 1980
PubMedID: 7390008

Title : Modulation of the distribution of acetylcholinesterase molecular forms in a murine neuroblastoma x sympathetic ganglion cell hybrid cell line - Lazar_1980_J.Neurochem_35_1067
Author(s) : Lazar M , Vigny M
Ref : Journal of Neurochemistry , 35 :1067 , 1980
Abstract : Studies were carried out on the polymorphism of acetylcholinesterase (AChE, EC 3.1.1.7) in a neuroblastoma x sympathetic ganglion cell hybrid cell line (T28) and its parental clone (N18TG2). These cells contain the tetrameric (G4, 10S), dimeric (G2, 6.5S) and monomeric (G1, 4S) forms of AchE, but not the collagen-tailed A12(16S) form of the sympathetic ganglion. Three variants of these forms could be distinguished on the basis of their solubility properties: (i) secreted forms which do not interact with the detergent Triton X-100; (ii) cellular forms which may be solubilized in detergent-free buffer and which interact reversibly with Triton X-100; (iii) cellular forms which require detergent for solubility, and aggregate in its absence. By using a nonpenetrating inhibitor, we demonstrated that, in T28 stationary cells, the cellular G4 form is associated with the plasma membrane, whereas the G1 form is intracellular. During induction of AChE activity in T28 cells, the relative proportion of the G4 form increases, suggesting, in agreement with previous observations, that G1 is a metabolic precursor of G4. The evolution of AChE molecular forms released into the culture medium closely resembles that of the cellular forms. The preferential accumulation of the G4 molecules does not simply depend on the cellular level of G1. It is favoured by culture conditions which promote morphological differentiation, but does not require the actual extension of neurites. T28 cells as well as other neuroblastoma-derived cells appear to be useful experimental materials to investigate the regulatory mechanisms underlying the maturation of AChE globular forms.
ESTHER : Lazar_1980_J.Neurochem_35_1067
PubMedSearch : Lazar_1980_J.Neurochem_35_1067
PubMedID: 7452305

Title : Asymmetric and globular forms of acetylcholinesterase in mammals and birds - Bon_1979_Proc.Natl.Acad.Sci.U.S.A_76_2546
Author(s) : Bon S , Vigny M , Massoulie J
Ref : Proceedings of the National Academy of Sciences of the United States of America , 76 :2546 , 1979
Abstract : We have identified six molecular forms of acetylcholinesterase (AcChoE: acetylcholine hydrolase, EC 3.1.1.7) in extracts from bovine superior cervical ganglia. We show that three of them resemble the collagen-tailed forms of Electrophorus AcChoE in their hydrodynamic parameters, low-salt aggregation properties, and collagenase sensitivity. The six molecular forms of bovine AcChoE appear structurally homologous to the six forms of electric fish AcChoE that have previously been characterized. They include globular molecules (monomers, dimers, and tetramers) and asymmetric aggregating molecules that possess a collagen-like tail associated with one, two, and three tetramers. We propose to call the globular forms G1, G2, and G4 and the asymmetric forms A4, A8, and A12, the subscripts indicating the number of catalytic subunits. In spite of quantitative differences in their molecular parameters, the AcChoE forms from rat and chicken are clearly homologous to those of bovine AcChoE. Thus the nomenclature we introduce is very probably valid for the main AcChoE molecular forms, at least in vertebrates, and should help to clarify structural relationships and homologies among them. This model, however, does not claim to represent entirely the complex polymorphism of AcChoE, because more or less hydrophobic variants of the G forms have been observed, and because other molecular associations cannot be excluded. We discuss the significance of the globular and collagen-tailed structure for the molecular localization of AcChoE.
ESTHER : Bon_1979_Proc.Natl.Acad.Sci.U.S.A_76_2546
PubMedSearch : Bon_1979_Proc.Natl.Acad.Sci.U.S.A_76_2546
PubMedID: 288044

Title : The subunit structure of mammalian acetylcholinesterase: catalytic subunits, dissociating effect of proteolysis and disulphide reduction on the polymeric forms -
Author(s) : Vigny M , Bon S , Massoulie J , Gisiger V
Ref : Journal of Neurochemistry , 33 :559 , 1979
PubMedID: 469545

Title : Distribution of acetylcholinesterase molecular forms in neural and non- neural sections of human muscle -
Author(s) : Carson S , Bon S , Vigny M , Massoulie J , Fardeau M
Ref : FEBS Letters , 97 :348 , 1979
PubMedID: 761642

Title : Active-site catalytic efficiency of acetylcholinesterase molecular forms in Electrophorus, torpedo, rat and chicken - Vigny_1978_Eur.J.Biochem_85_317
Author(s) : Vigny M , Bon S , Massoulie J , Leterrier F
Ref : European Journal of Biochemistry , 85 :317 , 1978
Abstract : The active sites of acetylcholinesterase multiple forms from four widely different zoological species (Electrophorus, Torpedo, rat and chicken) were titrated using a stable, irreversible phosphorylating inhibitor (O-ethyl-S2-diisopropylaminoethyl methyl-phosphonothionate). In all cases, we found that within a given species, the molecular forms we examined were equivalent in their catalytic activity per active site. As pure preparations of the molecular forms of Electrophorus acetylcholinesterase were available, we were able to establish that one inhibitor molecule binds per monomer unit for each of them. This had already been shown by several authors for the tetrameric globular form, but not for the tailed molecules. Analysis of the phosphorylation reaction showed that they are equally reactive. Under our experimental conditions, their turnover number per site was 4.4 x 10(7) mol of acetylthiocholine hydrolysed . h-1 at 28 degrees C, pH 7.0. The corresponding value was less than half for Torpedo (1.64 x 10(7) mol . h-1), and again lower for rat (1.32 x 10(7) mol . h-1) and chicken (1.05 x 10(7) mol . h-1). In the case of rat acetylcholinesterase, the activity per active site of solubilized (with or without Triton X-100) and membrane-bound enzyme were identical. We discuss the implications of these findings with respect to the quaternary structure of acetylcholinesterase, and to the physico-chemical state and physiological properties of its molecular forms.
ESTHER : Vigny_1978_Eur.J.Biochem_85_317
PubMedSearch : Vigny_1978_Eur.J.Biochem_85_317
PubMedID: 648523

Title : Neural induction of the 16S acetylcholinesterase in muscle cell cultures -
Author(s) : Koenig J , Vigny M
Ref : Nature , 271 :75 , 1978
PubMedID: 564456

Title : [Molecular forms of acetylcholinesterase in the slow muscle and the fast muscle of the chicken] - Koenig_1978_C.R.Seances.Soc.Biol.Fil_172_1069
Author(s) : Koenig J , Vigny M
Ref : Comptes Rendus des Seances de la Societe de Biologie et de Ses Filiales , 172 :1069 , 1978
Abstract : Five molecular forms of AChE are present in the slow (ALD) and twitch (PLD) muscles of the chick. These forms have 4 S, 7 S, 11 S, 15 S and 20 S sedimentation coefficient in sucrose gradient. The heaviest forms, the 20 S and 15 S of AChE are absent in uninnervated muscles and present in innervated muscles. In innervated muscles, the 20 S and 15 S AChE are present in both nerve-free segments and end-plates zones. The 20 S and 15 S which are not specifically associated with the end-plate zones in the chick could be considered as a biochemical "marker" of neuromuscular interactions.
ESTHER : Koenig_1978_C.R.Seances.Soc.Biol.Fil_172_1069
PubMedSearch : Koenig_1978_C.R.Seances.Soc.Biol.Fil_172_1069
PubMedID: 159094

Title : Nonspecific cholinesterase and acetylcholinesterase in rat tissues: molecular forms, structural and catalytic properties, and significance of the two enzyme systems - Vigny_1978_Proc.Natl.Acad.Sci.U.S.A_75_2588
Author(s) : Vigny M , Gisiger V , Massoulie J
Ref : Proceedings of the National Academy of Sciences of the United States of America , 75 :2588 , 1978
Abstract : "Nonspecific" cholinesterase (acylcholine acylhydrolase; EC 3.1.1.8) from various rat tissues has been found to exist in several stable molecular forms that appear as exact counterparts of molecular forms of acetylcholinesterase (acetylcholine hydrolase; EC 3.1.1.7). The sedimentation pattern of cholinesterase was similar to that of acetylcholinesterase with a small but significant shift between the sedimentation coefficients of the corresponding forms. Extraction yields in different media also demonstrated a close parallelism between the two enzyme systems. Other properties, such as thermal stability and catalytic characteristics, indicated both differences and similarities. In spite of the structural resemblance implied by their physicochemical properties, cholinesterase did not crossreact with antibodies against acetylcholinesterase. The nature of the relationships revealed by these studies and their bearing on the physiological significance of cholinesterases are discussed.
ESTHER : Vigny_1978_Proc.Natl.Acad.Sci.U.S.A_75_2588
PubMedSearch : Vigny_1978_Proc.Natl.Acad.Sci.U.S.A_75_2588
PubMedID: 78492

Title : Acetylcholinesterase of rat sympathetic ganglion: molecular forms, localization and effects of denervation -
Author(s) : Gisiger V , Vigny M , Gautron J , Rieger F
Ref : Journal of Neurochemistry , 30 :501 , 1978
PubMedID: 681929

Title : Solubilization and physicochemical characterization of rat brain acetylcholinesterase: development and maturation of its molecular forms -
Author(s) : Rieger F , Vigny M
Ref : Journal of Neurochemistry , 27 :121 , 1976
PubMedID: 956821

Title : Molecular forms of chicken acetylcholinesterase: effect of denervation -
Author(s) : Vigny M , Di Giamberardino L , Couraud JY , Rieger F , Koenig J
Ref : FEBS Letters , 69 :277 , 1976
PubMedID: 992039

Title : The motor end-plate specific form of acetylcholinesterase: appearance during embryogenesis and re-innervation of rat muscle -
Author(s) : Vigny M , Koenig J , Rieger F
Ref : Journal of Neurochemistry , 27 :1347 , 1976
PubMedID: 1003208

Title : Molecular forms of acetylcholinesterase: their de novo synthesis in mouse neuroblastoma cells - Rieger_1976_J.Neurochem_27_1059
Author(s) : Rieger F , Faivre-Bauman A , Benda P , Vigny M
Ref : Journal of Neurochemistry , 27 :1059 , 1976
Abstract : Rat mouse AChE molecular forms are indistinguishable with respect to their sedimentation coefficients and their evolutive proportions during brain maturation. Among rat or mouse erythrocytes, rat C6 glial cells, and mouse 2A and NS 20 neuroblastoma cells, only neuroblastoma cells showed both the ES and HS molecular forms with a 1:1 proportion for NS 20 cells. All these cells lack a third molecular form (16S), which is present in rat and mouse superior cervical ganglia. After irreversible inhibition of pre-existing NS 20 neuroblastoma AchE, the ES form is first synthesized (de novo synthesis). The HS form begins to appear after a lag time of several hours and represents, 24 h after inhibition, only 15% of the total recovered activity, which is near the initial level. The initial relative proportions return by 2 to 3 days after inhibition. The recovery of the HS form is, for the most part, blocked by actinomycin D, which does not block the recovery of activity itself, which remains as an ES form. It seems that integration of the ES form into the HS form more probably depends on the synthesis of a new messenger RNA, which is required for the synthesis of either new AChE polypeptide chain, polymerization initiating protein or activating enzyme.
ESTHER : Rieger_1976_J.Neurochem_27_1059
PubMedSearch : Rieger_1976_J.Neurochem_27_1059
PubMedID: 12170588

Title : Molecular forms of acetylcholinesterase -
Author(s) : Massoulie J , Bon S , Rieger F , Vigny M
Ref : Croatica Chemica Acta , 47 :163\ , 1975
PubMedID: