The Collagen-Like Subunits of Acetylcholinesterase From the Eel Electrophorus Electricus

Rosenberry, Terrone L.; Barnett, Philip; Mays, Carol

doi:10.1016/b978-0-08-026371-7.50022-4

Cited by 2 publications

(2 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast to the asymmetric and globular forms of AChE from electric fish (Rosenberry et al, 1980;Massoulie and Bon, 1982), little has been reported on the molecular structure of brain AChE (Rosenberry, 1982). Sorensen et al (1982) have proved with human NC AChE that there exists a sizable hydrophobic segment which may be responsible for activity modulation on detergent binding and for ag-gregation and membrane anchoring as well.…”

mentioning

confidence: 99%

Bovine Nucleus Caudatus Acetylcholinesterase: Active Site Determination and Investigation of a Dimeric Form Obtained by Selective Proteolysis

Landauer¹,

Ruess²,

Liefländer³

1984

Journal of Neurochemistry

View full text Add to dashboard Cite

The number of catalytic subunits of purified bovine nucleus caudatus acetylcholinesterase (E.C. 3.1.1.7) has been determined by active site labelling with [3H]diisopropyl fluorophosphate ([3H]DFP). The 10.5 S, 16 S, and 20 S forms were estimated to contain two, four, and six active sites, respectively, per molecule. A 4.8 S form, which showed a weak amphiphile-dependent activity behavior, was obtained by selective proteolytic digestion with pronase. The inability of the purified 4.8 S form to aggregate after detergent removal, and the molecular mass in the range of 130-165 kD under nondenaturating conditions, indicate that this form is a dimeric form, lacking those hydrophobic regions responsible for aggregation.

show abstract

mentioning

confidence: 99%

Bovine Nucleus Caudatus Acetylcholinesterase: Active Site Determination and Investigation of a Dimeric Form Obtained by Selective Proteolysis

Landauer¹,

Ruess²,

Liefländer³

1984

Journal of Neurochemistry

View full text Add to dashboard Cite

show abstract

“…The collagen-containing tail unit presumably exists as a triple helix. The multiplicity of collagen containing bands seen with the purified species in Torpedo and Electrophorus suggests that the tail may be composed of nonidentical subunits (10,30,31). Accordingly, as with many of the collagens, we should expect each subunit to be encoded by a separate gene.…”

Section: Discussionmentioning

confidence: 99%

Patients with congenital myasthenia associated with end-plate acetylcholinesterase deficiency show normal sequence, mRNA splicing, and assembly of catalytic subunits.

et al. 1995

View full text Add to dashboard Cite

A congenital myasthenic condition has been described in several patients characterized by a deficiency in end-plate acetylcholinesterase (AChE). The characteristic form of AChE in the end-plate basal lamina has the catalytic subunits disulfide linked to a collagen-like tail unit. Southern analysis of the gene encoding the catalytic subunits revealed no differences between patient and control DNA. Genomic DNA clones covering exon 4 and the alternatively spliced exons 5 and 6 were analyzed by nuclease protection and sequencing. Although allelic differences were detected between controls, we found no differences in exonic and intronic areas that might yield distinctive splicing patterns in patients and controls. The ACHE gene was cloned from genomic libraries from a patient and a control. Transfection of the cloned genes revealed identical species of mRNA and expressed AChE. Cotransfection of the genes expressing the catalytic subunits with a cDNA from Torpedo encoding the tail unit yielded asymmetric species that require assembly of catalytic subunits and tail unit. Thus the catalytic subunits of AChE expressed in the congenital myasthenic syndrome appear identical in sequence, arise from similar splicing patterns, and assemble normally with a tail unit to form a heteromeric species. (J. Clin. Invest. 1995. 95:333-340.)

show abstract

The Collagen-Like Subunits of Acetylcholinesterase From the Eel Electrophorus Electricus

Cited by 2 publications

References 14 publications

Bovine Nucleus Caudatus Acetylcholinesterase: Active Site Determination and Investigation of a Dimeric Form Obtained by Selective Proteolysis

Bovine Nucleus Caudatus Acetylcholinesterase: Active Site Determination and Investigation of a Dimeric Form Obtained by Selective Proteolysis

Patients with congenital myasthenia associated with end-plate acetylcholinesterase deficiency show normal sequence, mRNA splicing, and assembly of catalytic subunits.

Contact Info

Product

Resources

About