On the specificity of the acetylcholinesterase defect in dystrophic mice

Skau, Kenneth A.

doi:10.1002/mus.880130407

Cited by 8 publications

(16 citation statements)

References 17 publications

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“…Consequently, the deficiency of AChE tetramers, which has been described previously at the whole-muscle level (Gisiger and Stephens, 1988;Skau, 1990;Cabezas-Herrera et al, 1994a,b), seemed to affect internal membranes. However, it could be argued that some of the tetramers came from the SM.…”

Section: Solubilization and Distribution Of Ache Forms In Muscle Micrmentioning

confidence: 60%

“…3), which in agreement with previous results (Cabezas-Herrera et al, 1994a;Moral-Naranjo et al, 1996) corresponded to G~(amphiphilic monomers), G~(amphiphilic dimers), G( amphiphilic, detergent-interacting tetramers), G( hydrophilic, detergent-noninteracting tetramers), and asymmetric A12 forms. Sedimentation analyses in Brij 96-containing gradients allowed us to distinguish Gf rom G' forms, improving the resolution of the AChE forms with respect to previous studies in muscle extracts (Gisiger and Stephens, 1988;Skau, 1990). Considering the enzyme activity recovered in SI + S2 + S3 as the 100% value, the percentages of AChE compo- …”

Section: Characterization Of Microsomal Membranes From Normal and Dysmentioning

confidence: 99%

“…1) and in whole dystrophic muscle (Cabezas-Herrera et al, 1994a). As the content of AChE monomers is developmentally regulated (Arendt et al, 1992;Inestrosa et al, 1994), it may be thought that the increased level of light AChE species in dystrophic muscle is related to a maturational defect (Skau, 1990), the synthesis of the light AChE forms being boosted and/or their assembly for building tetramers being restricted by dystrophy. In contrast, the G2/G1 ratio consistently increased in DMV, because G1 predominated in NMV and G2 in dystrophic muscle membranes (Fig.…”

Section: Solubilization and Distribution Of Ache Forms In Muscle Micrmentioning

confidence: 99%

“…Little is known about the distribution of AChE forms in internal membranes of mammalian muscle (Campoy et al, 1992). Skeletal muscles of the Lama2"~mice show a specific deficit of G4 AChE forms (Gisiger and Stephens, 1988;Skau, 1990), changes in the content of amphiphilic AChE forms, and abnormal glycosylation of G4 AChE and butyrylcholinesterase (BuChE) species (Cabezas-Herrera et al, 1994a,b). These differences are probably musclespecific, because they have not been found in dystrophic mouse serum (Cabezas-Herrera et al, 1994b) or brain (Moral-Naranjo et al, 1996.…”

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Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

Cabezas-Herrera

Moral‐Naranjo

Campoy

et al. 1997

Journal of Neurochemistry

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Abstract:The distribution and glycosylation of acetyicholinesterase (AChE) forms in vesicles derived from sarcoplasmic reticulum of normal muscle (NMV) were investigated and compared with those from dystrophic muscle vesicles (DMV). AChE activity was similar in NMV and DMV. Most of the AChE in NMV and half in DMV were released with Triton X-1 00. Asymmetric (A 12) and globular hydrophilic and amphiphilic (G~, G~, G~, and G~) AChE species occurred in NMV and DMV, the lighter forms being predominant. The percentage of G~and G~de-creased in DMV. A fraction of the AChE that could not be extracted with detergent was detached with collagenase. Most of the detergent-released A12 AChE from NMV and nearly half in DMV failed to bind to Ricinus communis agglutinin (RCA-I). Conversely, the collagenase-detached isoforms bound to RCA, revealing that asymmetric AChE associated with internal membranes or basal lamina differed in glycosylation. Moreover, nearly half of GÃChE in DMV and a few in NMV bound to RCA. Most of the RCA-unreactive Gforms in NMV come from sarcolemma. The results indicate that dystrophy induces minor changes in the distribution and glycosylation of AChE forms in internal membranes of muscle.

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Section: Solubilization and Distribution Of Ache Forms In Muscle Micrmentioning

confidence: 60%

Section: Characterization Of Microsomal Membranes From Normal and Dysmentioning

confidence: 99%

Section: Solubilization and Distribution Of Ache Forms In Muscle Micrmentioning

confidence: 99%

mentioning

confidence: 99%

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Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

Cabezas-Herrera

Moral‐Naranjo

Campoy

et al. 1997

Journal of Neurochemistry

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“…The skeletal muscle of the Lama2 dy mouse shows a specific deficit of G 4 AChE forms (Gisiger and Stephens, 1988;Skau, 1990), an increase of amphiphilic AChE components (Cabezas-Herrera et al, 1994a), and a differential interaction of AChE and BuChE tetramers with RCA (Cabezas-Herrera et al, 1994b), these anomalies probably being related to the abnormal response of acetylcholine receptors in muscle cells of dystrophic mice Lansman, 1994, 1995). Neither the composition nor the glycosylation of ChE forms are altered in serum (Cabezas-Herrera et al, 1994b) or brain (Moral-Naranjo et al, 1996 of Lama2 dy mice.…”

Section: Introductionmentioning

confidence: 99%

Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart

1999

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In searching for possible differences in acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) forms of dystrophic heart, the properties of ChE species in normal (NH) and dystrophic Lama2dy mouse heart (DH) were investigated. BuChE predominated over AChE. Loosely- and tightly-bound ChEs were released with saline (extract S1) and saline-Triton X-100 buffers (S2). About 50% of AChE, and 25% of BuChE, in NH or DH was measured in S1, and the rest in S2. Asymmetric AChE forms A12 (15%) and A8 (11%), globular hydrophilic G(H)4 (8%), amphiphilic G(A)4 (15%), and G(A)2+G(A)1 (51%) AChE species, and BuChE forms G(H)4 (13%), G(A)4 (3%), and G(A)2+G(A)1 (84%) were identified in NH and DH. Most of the asymmetric and G(A)4 AChE species were bound to Triticum vulgaris (WGA) or Ricinus communis (RCA) agglutinins. About half of G(H)4 and G(A)2+G(A)1 AChE were bound to WGA, and less (10%) to RCA. Variable amounts of G(H)4+G(A)4 (60%), and G(A)2+G(A)1 (75%) BuChE bound to WGA, and 50 and 10% to RCA. The lack of structural differences between ChE species in NH and DH indicates that, in contrast to the ChE forms in mouse skeletal muscle, the biosynthesis of ChE components in heart is not disturbed by dystrophy.

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Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain

Moral‐Naranjo¹,

Cabezas‐Herrera²,

Vidal³

1996

J. Neurosci. Res.

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In searching for possible differences in the composition of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) forms in dystrophic brain, the distribution of various enzyme molecules in normal (NB) and dystrophic (DB) 129B6F1/J mouse brain has been investigated. The tissue was sequentially extracted with saline (S1) and with saline‐Triton X‐100 buffers (S2) to release soluble and membrane‐bound cholinesterases. About 15% of the AChE and 35% of the BuChE activities in NB were recovered in S1, and the rest in S2, G4, G2, and G1 AChE and BuChE forms were identified in the soluble fractions obtained from NB and DB. The shift in sedimentation values of the separated AChE and BuChE species in sucrose gradients made with and without detergents revealed the occurrence of hydrophilic (H) and amphiphilic (A) variants of cholinesterases in the extracts. The amphiphilic properties of the several AChE and BuChE molecules were analyzed by Triton X‐114 phase‐partitioning and by phenyl‐agarose chromatography. A12 (1%), G4A (72%), G4H (8%), and G2A + G1A (19%) AChE molecules, and G4A (34%), G4H (19%), and G2A + G1A (47%) BuChE forms, were identified in NB. The G4A AChE and BuChE isoforms differed in their interaction with Triton X‐114 and with a hydrophobic matrix. Neither the extent of cholinesterase solubilization, nor the distribution of individual enzyme forms, was significantly altered in DB. The lack of specific differences in the distribution of AChE and BuChE forms between NB and DB suggests that the biosynthetic pathway leading to the various enzyme forms is altered in muscle but not in dystrophic mouse brain. © 1996 Wiley‐Liss, Inc.

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On the specificity of the acetylcholinesterase defect in dystrophic mice

Cited by 8 publications

References 17 publications

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart

Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain

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On the specificity of the acetylcholinesterase defect in dystrophic mice

Cited by 8 publications

References 17 publications

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2dy Mouse Muscle

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2dy Mouse Muscle

Characterization of acetylcholinesterase and butyrylcholinesterase forms in normal and dystrophic Lama2dy mouse heart

Molecular forms of acetyl- and butyrylcholinesterase in normal and dystrophic mouse brain

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Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle

Glycosylation of Acetylcholinesterase Forms in Microsomal Membranes from Normal and Dystrophic Lama2^dy Mouse Muscle