Cholinesterases

Brzin, Miro; Sketelj, Janez; Klinar, Biba

doi:10.1007/978-1-4899-1881-9_11

Cited by 18 publications

(6 citation statements)

References 414 publications

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“…The AChE cytochemical reaction was present at the level of the Nissl bodies, the entire Golgi apparatus, and in the extracellular space surrounding the ganglionic cells. These results were identical to those published previously (Gautron 1974;Gautron and Gisiger 1976;Gisiger et al 1978;Brzin et al 1982). In the immunocytochemical demonstration of AChE in ganglionic cells, the gold particles revealed the pres- ence of antigenic sites within the cisternae of the RER forming the Nissl bodies (results not shown).…”

Section: Resultssupporting

confidence: 92%

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Demonstration of Acetylcholinesterase Molecular Forms in a Continuous Tubular Lysosomal System of Rat Pancreatic Acinar Cells

Bendayan

Gisiger

2001

J Histochem Cytochem.

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S U M M A R Y By applying the highly sensitive cytochemical Gautron's technique, we were able to reveal AChE activity in rat pancreatic acinar cells, particularly at the level of a complex membrane-bound network formed by tubules with varicosities located around the nuclei and close to the basolateral membrane. The Golgi apparatus was devoid of cytochemical reaction beside the trans -Golgi network cisternae, which showed a positive reaction. The RER of some acinar cells also presented a signal, demonstrating their capability of synthesizing AChE. Immunogold using a specific anti-AChE antibody yielded similar results. Double-labeling experiments corroborated the presence of enzyme cytochemical and immunocytochemical signals in the same lysosomal tubular network. Biochemical sedimentation assays confirmed the presence of AChE in acinar cells, which exists as two globular molecular forms, G 1 and G 4 . These results were obtained with pancreatic tissue in situ as well as with isolated acinar cells maintained in culture and devoid of neural elements. The existence of a continuous tubular lysosomal network containing AChE is in agreement with previous reports on acinar and other cell types, and supports a more general hypothesis on dynamic continuities among cell structures. Whether AChE is being secreted by the acinar cells or internalized through this endo-lysosomal system was not defined. However, the capability of the acinar cells to synthesize AChE and to channel it through a tubular system is a good indication that the cells can modulate their cholinergic stimulation for optimal secretion of digestive enzymes. (J Histochem Cytochem 49: 29 -39, 2001)

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Section: Resultssupporting

confidence: 92%

“…Neurons of these ganglia are known to contain large amounts of AChE, particularly in their Nissl bodies (Gautron 1974;Gautron and Gisiger 1976;Gisiger et al 1978;Brzin et al 1982). Both the cytochemical and immunocytochemical protocols were applied on the ganglionic tissue as described above for the pancreas.…”

Section: Ganglionic Tissuementioning

confidence: 99%

Demonstration of Acetylcholinesterase Molecular Forms in a Continuous Tubular Lysosomal System of Rat Pancreatic Acinar Cells

Bendayan

Gisiger

2001

J Histochem Cytochem.

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“…Analysis of VUC1 amino acid sequence revealed the presence two cystatin-like domains (referenced as domains 1 and 2), whereas plant cystatins typically are smaller proteins (12-16 kDa) with single cystatin-like domains [4]. In plants, protein or nucleotide sequences corresponding to single-domain cystatins have previously been identified from leaves [30,18], flowers [31] and seeds [32][33][34][35]. In cowpea, a single-domain cystatin has been identified and characterized in the seeds [36].…”

Section: Discussionmentioning

confidence: 99%

A multicystatin is induced by drought‐stress in cowpea (Vigna unguiculata (L.) Walp.) leaves

et al. 2004

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Cystatins are protein inhibitors of cystein proteinases belonging to the papain family. In cowpea, cystatin-like polypeptides and a cDNA have been identified from seeds and metabolic functions have been attributed to them. This paper describes VuC1, a new cystatin cDNA isolated from cowpea leaves (Vigna unguiculata (L.) Walp.). Sequence analysis revealed a multicystatin structure with two cystatin-like domains. The recombinant VUC1 protein (rVUC1) was expressed in an heterologous expression system and purified to apparent homogeneity. It appeared to be an efficient inhibitor of papain activity on a chromogenic substrate. Polyclonal antibodies against rVUC1 were obtained. Involvement of the VuC1 cDNA in the cellular response to various abiotic stresses (progressive drought-stress, dessication and application of exogenous abscissic acid) was studied, using Northern blot and Western blot analysis, in the leaf tissues of cowpea plants corresponding to two cultivars with different capacity to tolerate drought-stress. Surprisingly, these abiotic stresses induced accumulation of two VuC1-like messages both translated into VUC1-like polypeptides. Difference in the transcript accumulation patterns was observed between the two cultivars and related to their respective tolerance level. Presence of multiple cystatin-like polypeptides and their possible involvement in the control of leaf protein degradation by cysteine proteinases is discussed.

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“…Several recent reviews have reviewed the structural polymorphism of the cholinesterases in a broader context or have emphasized more specific issues concerning their biology and biochemistry (see, for example, [14, 15,[18][19][20][21]). …”

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confidence: 99%

Modes of attachment of acetylcholinesterase to the surface membrane

Silman

Futerman

1987

European Journal of Biochemistry

173

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Acetylcholinesterase (AChE) occurs in multiple molecular forms differing in their quaternary structure and mode of anchoring to the surface membrane. Attachment is achieved by post‐translational modification of the catalytic subunits. Two such mechanisms are described. One involves attachment to catalytic subunit tetramers, via disulfide bridges, of a collagen‐like fibrous tail. This, in turn, interacts, primarily via ionic forces, with a heparin‐like proteoglycan in the extracellular matrix. A second such modification involve the covalent attachment of a single phosphatidylinositol molecule at the carboxyl‐terminus of each catalytic subunit polypeptide; the diacylglycerol moiety of the phospholipid serves to anchor the modified enzyme hydrophobically to the lipid bilayer of the plasma membrane. The detailed molecular structure of these two classes of acetylcholinesterase are discussed, as well as their biosynthesis and mode of anchoring.

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Cholinesterases

Cited by 18 publications

References 414 publications

Demonstration of Acetylcholinesterase Molecular Forms in a Continuous Tubular Lysosomal System of Rat Pancreatic Acinar Cells

Demonstration of Acetylcholinesterase Molecular Forms in a Continuous Tubular Lysosomal System of Rat Pancreatic Acinar Cells

A multicystatin is induced by drought‐stress in cowpea (Vigna unguiculata (L.) Walp.) leaves

Modes of attachment of acetylcholinesterase to the surface membrane

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