Acetylcholine (ACh)-mediated vagal transmission as well as nonneuronal ACh release are considered cardioprotective in pathological situations with increased sympathetic drive such as ischemia-reperfusion and cardiac remodeling. ACh action is terminated by hydrolysis by the cholinesterases (ChEs), acetylcholinesterase, and butyrylcholinesterase. Both ChEs exist in multiple molecular variants either soluble or anchored by specific anchoring proteins like collagen Q (ColQ) anchoring protein and proline-rich membrane anchoring protein (PRiMA). Here we assessed the expression of specific ChE molecular forms in different heart compartments using RT-qPCR. We show that both ChEs are expressed in all heart compartments but display different expression patterns. The acetylcholinesterase-T variant together with PRiMA and ColQ is predominantly expressed in rat atria. Butylcholinesterase is found in all heart compartments and is accompanied by both PRiMA and ColQ anchors. Its expression in the ventricular system suggests involvement in the nonneuronal cholinergic system. Additionally, two PRiMA variants are detected throughout the rat heart.

• Klíčová slova
• acetylcholine, acetylcholinesterase, acétylcholine, acétylcholinestérase, butyrylcholinesterase, butyrylcholinestérase, collagen Q anchoring protein, proline-rich membrane anchoring protein, « collagen Q anchoring protein », « proline-rich membrane anchoring protein »,
• MeSH
• acetylcholin metabolismus   MeSH
• acetylcholinesterasa analýza   metabolismus   MeSH
• butyrylcholinesterasa analýza   metabolismus   MeSH
• GPI-vázané proteiny analýza   metabolismus   MeSH
• izoenzymy analýza   metabolismus   MeSH
• kolagen analýza   metabolismus   MeSH
• krysa rodu Rattus MeSH
• kvantitativní polymerázová řetězová reakce MeSH
• membránové proteiny analýza   metabolismus   MeSH
• myokard enzymologie   MeSH
• potkani Wistar MeSH
• proteiny nervové tkáně analýza   metabolismus   MeSH
• stanovení celkové genové exprese MeSH
• zvířata MeSH
• Check Tag
• krysa rodu Rattus MeSH
• mužské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• acetylcholin MeSH
• acetylcholinesterasa MeSH
• Ache protein, rat MeSH Prohlížeč
• butyrylcholinesterasa MeSH
• ColQ protein, rat MeSH Prohlížeč
• GPI-vázané proteiny MeSH
• izoenzymy MeSH
• kolagen MeSH
• membránové proteiny MeSH
• PRiMA1 protein, rat MeSH Prohlížeč
• proteiny nervové tkáně MeSH

INTRODUCTION: Determination of acetylcholinesterase and butyrylcholinesterase activity has become an important tool in drug design and discovery as well as in medicine and toxicology. There are a large number of compounds that are able to modulate cholinesterase activity. These compounds can be used for pharmacological management of various disorders (e.g., Alzheimer's disease, myasthenia Gravis). Moreover, organophosphate poisoning is frequently diagnosed via a cholinesterase activity assay. This broad variety of methods has been developed over the past decades for cholinesterase activity quantification. AREAS COVERED: This review provides a summary of the methods that are based on specific properties of cholinesterases and their interactions with native or artificial substrates. The authors also aim to provide an overview of different techniques used for the determination of quantitative cholinesterase activity. Specifically, the authors describe and discuss the manometric, potentiometric, titrimetric, photometric, fluorometric, and radioisotopic methods. EXPERT OPINION: Existing methods are able to cover most of the problems that arise during cholinesterase activity determination. Colorimetry according to Ellman has proved to be the most useful and versatile approach. It may be used in various protocols for the determination of pesticide or nerve agent exposure or for the development of new drugs. Its possible improvement lies in optimization of hemoglobin-rich samples. The progress of the most common methods (including Ellman) depends on miniaturization and modern physical platforms (e.g., optical fibers, chip methods, or nanotechnologies).

• MeSH
• Alzheimerova nemoc farmakoterapie   metabolismus   MeSH
• butyrylcholinesterasa analýza   metabolismus   MeSH
• chemické bojové látky farmakologie   MeSH
• chemické techniky analytické metody   MeSH
• cholinesterasové inhibitory farmakologie   MeSH
• cholinesterasy analýza   metabolismus   MeSH
• lidé MeSH
• myasthenia gravis farmakoterapie   metabolismus   MeSH
• racionální návrh léčiv MeSH
• referenční hodnoty MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• butyrylcholinesterasa MeSH
• chemické bojové látky MeSH
• cholinesterasové inhibitory MeSH
• cholinesterasy MeSH

Innervation of the spleen in rats was studied. Butyrylcholinesterase-(BuChE)-positive nerve components of the organ were visualized by the direct thiocholine method. BuChE-positive nerve components enter the spleen in a common bundle with arteries. In the organ they form characteristic periarterial and periarteriolar plexiform arrangements, which are especially conspicuous around the aa. centrales running through the white pulp. Then, nerve fibres extend away from these plexuses into adjacent layers of trabeculae further into marginal layers of periarterial lymphatic sheath (PALS) as well as into the mantle zone of follicles. Several scattered periarteriolar and solitary nerve fibres can be seen in the marginal sinuses and cords of the red pulp. In the fibrous capsula BuChE-positive nerve fibres can also be seen which have an evident connection with trabecular and parenchymal nerves of the organ. Microscopic findings support the notion that BuChE-positive nerve profiles supply not only the vasculature, but also the parenchymal components of the spleen, and they may participate, to a great extent, in the regulation of the immune processes in this organ.

• MeSH
• butyrylcholinesterasa analýza   metabolismus   MeSH
• krysa rodu Rattus MeSH
• nervová vlákna enzymologie   MeSH
• potkani Wistar MeSH
• slezina inervace   MeSH
• techniky in vitro MeSH
• zvířata MeSH
• Check Tag
• krysa rodu Rattus MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• butyrylcholinesterasa MeSH

Cholinesterases belong to esterases and represent important animal enzymes with multiple biological function. Acetylcholinesterase (AChE) plays the key role in cholinergic neurotransmission, whereas the function of butyrylcholinesterase (BuChE) is still unrevealed. Both enzymes seem to act as neurogenic factors during the early embryogenesis and later on they may participate in some pathological alteration. In humans, these degenerative changes are related to the deposition of pathologic proteins in the brain and with the progress of the Alzheimer's dementia (AD). Both AChE) and BuChE become recently the target for the most frequently used therapy of AD--cholinesterase inhibitors.

• MeSH
• acetylcholinesterasa analýza   fyziologie   MeSH
• Alzheimerova nemoc diagnóza   enzymologie   patofyziologie   terapie   MeSH
• butyrylcholinesterasa analýza   fyziologie   MeSH
• cholinesterasové inhibitory terapeutické užití   MeSH
• klinické enzymatické testy MeSH
• lidé MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• acetylcholinesterasa MeSH
• butyrylcholinesterasa MeSH
• cholinesterasové inhibitory MeSH

In experiments on adult albino rats the authors used the substances BW 284 C51 (1.5-bis(allyldimethylammoniumphenyl)-pentane-3-one-dibromide) as a specific inhibitor of acetylcholinesterase (AChE) and ethopropazine (10-(2-diethylaminopropyl) phenothiazine hydrochloride) as a specific inhibitor of butyrylcholinesterase (BuChE) to determine the two enzyme activities in atrial homogenates and to investigate changes after AChE or BuChE inhibition of the negative chronotropic effect of acetylcholine (ACh) on atria incubated in vitro. AChE accounted for only 12% and BuChE for 88% of the total ability of atrial homogenates to hydrolyse acetylcholine. The concentration of exogenous ACh needed to reduce the spontaneous frequency of contractions of the isolated right atrium by 30, 60, or 90/min fell by 78%, 79% and 84% respectively after BW 284 C51 inhibition of AChE and by 95%, 94% and 94% after simultaneous inhibition of AChE and BuChE. The significance of AChE in control of the negative chronotropic effect of ACh is thus evidently significantly greater than would correspond to the percentual proportion of AChE in cholinesterase activities in the atria of the rat heart. In can be assumed that AChE is functionally associated with parasympathetic innervation of the heart and that it is probably present in a high concentration in the primary pacemaker region.

• MeSH
• acetylcholinesterasa analýza   MeSH
• benzenaminium, 4,4'-(3-oxo-1,5-pentandiyl)bis(N,N-dimethyl-N-2-propenyl-), dibromid farmakologie   MeSH
• butyrylcholinesterasa analýza   MeSH
• cholinesterasy analýza   MeSH
• krysa rodu Rattus MeSH
• myokard enzymologie   MeSH
• zvířata MeSH
• Check Tag
• krysa rodu Rattus MeSH
• mužské pohlaví MeSH
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• acetylcholinesterasa MeSH
• benzenaminium, 4,4'-(3-oxo-1,5-pentandiyl)bis(N,N-dimethyl-N-2-propenyl-), dibromid MeSH
• butyrylcholinesterasa MeSH
• cholinesterasy MeSH