Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myelin, isolated from forebrain and spinal cord of young and adult rats, was distributed by zonal centrifugation on linear (0.32--1.00 M) sucrose gradients in a bell-shaped mode. The peak position of forebrain myelin shifted from the density of 0.58 M sucrose in young animals to that of 0.67 M sucrose in adult rats, while in spinal cord no such pronounced shift was noticed (approximately 0.58 M sucrose). Morphologically, the preparations appeared very similar across the density ranges. Specific activities of acetylcholinesterase were substantially below the total homogenates, while those of 2', 3'-cyclic nucleotide 3'-phosphohydrolase were higher in all fractions, except in the light myelin subfractions from adult spinal cord. Basic proteins decreased from the light to the heavier fractions; higher molecular weight proteins increased, together with proteolipid protein, which in spinal cord reached a plateau and in forebrain decreased towards the heavy side. The ratio of the small basic protein/large basic protein showed higher values in the light myelin subfractions in the regions and ages examined, pointing to a higher degree of maturation.
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PMID:Density and protein profiles of myelin from two regions of young and adult rat CNS. 20 98

Axolemma-enriched fractions were prepared from rat brain by osmotic shock of a purified preparation of myelinated axons and subsequent separation of myelin, two axolemma-enriched fractions and myelin-free axons by density gradient centrifugation. Compared with the starting whole homogenate, the fractions were enriched in specific activity of Na+K+ ATPase, acetylcholinesterase, 5'nucleotidase as well as 2',3'-cyclic nucleotide 3'phosphohydrolase. Compared with myelin, the axolemmal fractions are greatly enriched in high molecular weight proteins. The 1.0/1.2 fraction has a predominant peak of fucose-labeled glycoprotein with a molecular weight between that of the myelin associated glycoprotein and the Wolfgram protein which is absent from the myelin glycoprotein profile. Polyacrylamide gel electrophoresis showed that the protein profile of myelin isolated by this procedure was similar to that of myelin isolated by other procedures and that the myelin specific basic and proteolipid proteins were virtually absent in the axolemma-enriched fractions. Both axolemma fractions were enriched in higher MW proteins, some of which resembled proteins in the myelin protein profile. Both axolemma-enriched fractions specifically bind between 2 and 3 pmoles of [3H]tetrodotoxin per mg protein. The axolemma-enriched fractions incorporated [3H]leucine and [14C]fucose exclusively into high molecular weight proteins and glycoproteins. In contrast myelin concomitantly isolated with the axolemma-enriched fractions had a significant amount of [3H]leucine labeled protein in myelin proteolipid and basic proteins. In addition to the myelin associated g-ycoprotein the [14C]fucose labeled a glycoprotein of slightly larger apparent molecular weight than proteolipid protein was found in the myelin fraction while the comparable labeled glycoprotein was absent in the axolemma-enriched fractions. The possible extent of contamination of these fractions by myelin or myelin subfractions and relationship of these axolemma-enriched fractions to other axolemma preparations are discussed.
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PMID:Isolation and partial characterization of rat CNS axolemma enriched fractions. 20 16

A protein fatty acylesterase activity that catalyzes the removal of fatty acid from exogenous proteolipid protein (PLP) has been demonstrated in isolated rat brain myelin. Optimum enzyme activity for the deacylation of PLP was obtained in 0.5% Triton X-100, 1 mM dithiothreitol at pH 7.0 and at 37 degrees C. Other detergents (octyl beta-D-glucoside, Nonidet P-40, and Tween 20) have little or no effect, whereas deacylation was completely abolished by 0.1% sodium dodecyl sulfate or boiling the membrane fraction for 5 min prior to incubation. Under optimal conditions, the rate of deacylation was linear up to 20 min, and the apparent Km for bovine [3H]palmitoyl-PLP was 18 microM. The myelin-associated PLP fatty acylesterase has no apparent requirements for divalent cations (Ca2+, Mg2+, Mn2+), and chelators such as EDTA, [ethylenebis(oxyethylenenitrilo)] tetraacetic acid, and 1,10-phenantroline have little or no effect on enzyme activity. Sulfhydryl and histidine residues are needed for full enzyme activity, whereas the "active serine"-directed inhibitor phenylmethylsulfonyl fluoride has no effect. The myelin-associated protein fatty acylesterase was present throughout brain development and in all myelin subfractions, in agreement with the dynamic metabolism of PLP-bound fatty acids. Enzyme activity was also present in sciatic nerve, brain cortex, and heart whereas liver was devoid of activity. Several esterases, including phospholipase A2, glyoxalase II, and acetylcholinesterase, did not remove fatty acid from PLP. Myelin basic protein, palmitoyl-CoA hydrolase, and myelin-associated nonspecific esterase were also ruled out as the PLP fatty acylesterase. Thus, all data seem to indicate that this enzyme is different from esterases of the lipid metabolism. Finally, stimulation of protein phosphorylation with Ca2+, but not with cyclic-AMP, inhibited PLP deacylation, suggesting that the myelin-associated protein fatty acylesterase activity is regulated by endogenous Ca(2+)-dependent protein kinases.
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PMID:Characterization of proteolipid protein fatty acylesterase from rat brain myelin. 156 18

The light and heavy smooth-surfaced membranes (LSM and HSM), which had densities corresponding to 1.08 M and 1.28 M sucrose, respectively, were isolated from rat brain and some of their biochemical properties were investigated. Both LSM and HSM showed high Na+,K+-ATPase activity and, in particular, in HSM the activity was four times (21.55 mumol/mg protein/h) higher than that of the brain homogenate. High 2',3'-cyclic nucleotide 3'-phosphodiesterase activity (293.4 mumol/mg protein/h) was characteristic of LSM. 5'-Nucleotidase and acetylcholinesterase activities were also higher in LSM than in HSM. SDS-polyacrylamide gel electrophoresis showed that LSM and HSM had many protein component and that low molecular weight proteins such as proteolipid protein and basic protein were almost absent, in contrast with myelin and myelin-like membrane. GM1 ganglioside constituted the major class of total ganglioside in both LSM and HSM. These biochemical findings suggested that LSM is a membrane that has not previously been described, or a membrane fraction related to the oligodendroglial plasma membrane.
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PMID:Further studies on the smooth-surfaced membranes isolated from rat brain. 625 69

Immunohistochemical methods have been used to determine the distribution of macroglia and myelin in the normal rat superior colliculus (SC) and in grafts of fetal tectal tissue. The fetal tissue was derived from 15 day-old (E15) rat embryos and was transplanted onto the midbrain of newborn host rats of the same (PVG/c) strain. Antibodies to glial fibrillary acidic protein (GFAP) and carbonic anhydrase II (CAII) were used to visualize astrocytes and oligodendroglia respectively. Myelin was immunostained with antibodies to either proteolipid protein (PLP) or myelin basic protein (MBP). In the normal SC, GFAP positive astrocytes were found scattered throughout the SC, particularly in the superficial layers. They were especially prominent at the pial surface, around major blood vessels and at the midline between the two colliculi. CAII immunoreactive oligodendroglia and associated myelin were also found throughout the SC; by far the lowest density was seen in the stratum griseum superficiale (SGS). Both types of macroglia cell were found in abundance in tectal transplants, indicating that the precursors of these glial types were present in the E15 rat mesencephalon. In mature grafts, large numbers of fibrous astrocytes were found throughout the neuropil and the level of GFAP immunoreactivity was consistently greater than in host SC. Astrocytes seemed to be maintained in a reactive, perhaps immature state within the grafted tissue. Tectal transplants possessed large numbers of fully differentiated CAII-positive oligodendroglia and the grafts contained a dense network of myelinated axons. However the distribution of CAII and PLP immunoreactivity was not homogeneous; there were localized, well-defined regions that contained few oligodendroglia and relatively little myelin. These areas stained intensely for acetylcholinesterase (AChE) and were almost certainly homologous to the SGS of normal SC. The relative lack of oligodendroglia in the AChE stained patches in grafts and in SGS in situ suggests that local factors influencing the proliferation and distribution of oligodendroglia in normal SC may have been operating in a similar manner within the tectal transplant neuropil.
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PMID:The distribution of astrocytes, oligodendroglia and myelin in normal and transplanted rat superior colliculus: an immunohistochemical study. 750 97