Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies have used a sensitive histochemical technique to demonstrate acetylcholinesterase and butyrylcholinesterase within the pathological lesions of Alzheimer's disease. In this study, we used this technique to show that acetylcholinesterase localized in either frozen or fixed neocortical tissue sections is removed after treatment with various glycosaminoglycans, heparinases or proteases. Heparan sulphate, heparinase lyase type I and to a lesser degree, heparin and chondroitin sulphate were effective in solubilizing a large part of the cholinesterase activity. At physiological concentrations, the protease papain or trypsin readily removed activity but collagenase or pronase were relatively less effective. Peptide protease inhibitors and divalent metals did not exhibit any clear effect. The specificity of these observations was shown by inhibition of activity with various anticholinesterases including diisofluorophosphate. Our results suggest that acetylcholinesterase is anchored to and may be released from the heparan sulphate glycosaminoglycans shown to be contained in the lesions. We further suggest that the localization of cholinesterases is closely associated with the accumulation of the glycosaminoglycans in amyloid plaques and neurofibrillary tangles.
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PMID:Acetylcholinesterase and its association with heparan sulphate proteoglycans in cortical amyloid deposits of Alzheimer's disease. 146 81

The activity of specific acetylcholinesterase, assayed in the presence of an inhibitor of nonspecific cholinesterase, was significantly lower in the leg muscle of dystrophic mice of Bar Habor strain 129 than in that of normal mice. However, the nonspecific butyrylcholinesterase activity was much higher in dystrophic muscle than in normal muscle. Collegenase released more acetylcholinesterase activity into the soluble fraction derived from homogenized normal muscle than into that derived from dystrophic muscle. The collagenase-released activity in the normal muscle contained about 95% specific acetylcholinesterase while that from dystrophic muscle contained only 74% specific acetylcholinesterase activity. The acetylcholinesterase activity solubilized by collagenase from control muscle contained the highest activity in 10 S form with decreasing activity of 16 S and 4 S forms, but that from dystrophic muscle contained much less of the 16 S and 10 S forms with more 4 S form, compared to the controls.
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PMID:Acetylcholinesterase solubilized from normal and dystrophic muscle by collagenase treatment. 624 8

Acetylcholinesterase (EC 3.1.1.7.; AChE) and butyrylcholinesterase (EC 3.1.1.8.; BuChE) from chicken muscle exist as sets of structurally homologous forms with very similar properties. The collagenase sensitivity and aggregation properties of the 'heavy' forms of both enzymes indicate that they possess a collagen-like tail, and their stepwise dissociation by trypsin confirms that they correspond to triple (A12) and double (A8) collagen-tailed tetramers. In addition to this dissociating effect, trypsin digests an important fraction of the catalytic units of AChE, in a progressive manner, removing as much as 30% of the enzyme's mass, without inactivation of the tetramers and of the tailed molecules. The trypsin-modified AChE forms closely resemble the corresponding mammalian AChE forms in their hydrodynamic properties. It is not known whether the trypsin-digestible peptides, which do not appear to be involved in the ionic or hydrophobic interactions of the enzymes, are a fragment of the catalytic subunit or whether they constitute distinct polypeptides.
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PMID:The quaternary structure of chicken acetylcholinesterase and butyrylcholinesterase; effect of collagenase and trypsin. 625 92

The release of acetylcholinesterase activity by collagenase from the particulate fraction of mouse muscle homogenate into the soluble fraction was dependent on the time of incubation of muscle homogenate with collagenase. The collagenase-stimulated release of acetylcholinesterase was inhibited by 1,10-phenanthroline, an inhibitor of collagenase. Differential effects of inhibitors of specific acetylcholinesterase and nonspecific cholinesterase were observed in both collagenase extract and collagenase-resistant fraction derived from homogenate of muscle of normal and dystrophic mice. The collagenase extract of dystrophic muscle contained distinctly lower activity of acetylcholinesterase than that of normal muscle, while both collagenase extract and collagenase-resistant fraction of dystrophic muscle showed much higher activity of butyrylcholinesterase activity than those from normal muscle.
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PMID:Collagenase-releasable and -resistant cholinesterases in normal and dystrophic muscles. 625 46

The cholinesterase activity of Xenopus laevis oocytes was assessed using [3H]acetylcholine in a simple radiometric procedure. The cholinesterase activity of mature (stage V-Vl) oocytes was very sensitive to inhibition by the specific acetylcholinesterase inhibitor, BW284-C5l, and relatively insensitive to an inhibitor of non-specific, or butyrylcholinesterase. The Km and Vmax of the acetylcholinesterase measured in homogenates of oocytes were 312 microM and 4.6 nmol-oocyte 1-h 1, respectively. Triton X-100 increased the enzyme activity of homogenates four- to five-fold while collagenase treatment displaced into the medium none of the acetylcholinesterase activity from either homogenates or intact oocytes. Cations were found generally to diminish the acetylcholinesterase activity of oocyte homogenates, and lanthanum ions inhibited acetylcholine hydrolysis with an IC50 of 0.63 mM. Subcellular fractionation of oocytes revealed that the bulk of enzyme activity was associated with particulate fractions. Acetylcholinesterase activity was also detected on the surface, and in homogenates, of immature oocytes. Peak enzyme activity resided in stage IV oocytes. Eggs obtained from females induced to spawn were found to have acetylcholinesterase activity in homogenates but little or no hydrolytic activity was detected on the egg surface. These results provide a point of departure for further investigations of the functional significance of this enzyme in Xenopus oocytes.
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PMID:Acetylcholinesterase activity of Xenopus laevis oocytes. 666 98

Acridine ligand affinity chromatography is an effective means of acetylcholinesterase (AChE) purification. However, the synthesis of these resins is laborious and expensive. We have developed an acridine ligand affinity resin that is easy to produce, inexpensive, and selective for AChE over butyrylcholinesterase. The resin is produced in a single synthetic step by attaching the aminoacridine tacrine to epoxy-activated Sepharose. AChE from bovine serum (59% yield), Torpedo electric organ (27-60% yield), and two commercial sources of eel AChE (> 92% yield) is purified using the affinity resin. One commercial source of eel AChE contains two proteins with molecular weights of 80 and 55 kDa upon purification, while two proteins with molecular weights of 55 and 25 kDa are isolated from the other commercial source, presumably representing degraded AChE. The degradation state of the commercially available eel AChE preparations did not influence their specific activities. The isolation of AChE from bovine serum results in a single 80-kDa protein. However, butyrylcholinesterase is not purified from the serum. Using the tacrine affinity resin, and 80-kDa AChE, solubilized from Torpedo electric organ membranes by protease digestion, can also be purified. Velocity sedimentation analysis of the Torpedo AChE reveals that the molecular forms isolated are either tetrameric or asymmetric when solubilized by collagenase or trypsin, respectively. Overall, the tacrine affinity resin which is simple and inexpensive to produce allows for the selective isolation of AChE from diverse biological matrices.
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PMID:Purification of acetylcholinesterase by tacrine affinity chromatography. 852 21

The messenger RNA (mRNA) distribution of 60 proteins was examined in the 3 fractions obtained by collagenase digestion (fat cells and the nonfat cells comprising the tissue remaining after collagenase digestion [matrix] and the stromovascular cells) of omental adipose tissue obtained from morbidly obese women undergoing bariatric surgery. Fat cells were enriched by at least 3-fold as compared with nonfat cells in the mRNAs for retinol binding protein 4, angiotensinogen, adipsin, glutathione peroxidase 3, uncoupling protein 2, peroxisome proliferator-activated receptor gamma, cell death-inducing DFFA-like effector A, fat-specific protein 27, 11beta-hydroxysteroid dehydrogenase 1, glycerol channel aquaporin 7, NADPH:quinone oxidoreductase 1, cyclic adenosine monophosphate phosphodiesterase 3B, glyceraldehyde-3-phosphate dehydrogenase, insulin receptor, and amyloid A1. Fat cells were also enriched by at least 26-fold in the mRNAs for proteins involved in lipolysis such as hormone-sensitive lipase, lipoprotein lipase, adipose tissue triglyceride lipase, and FAT/CD36. The relative distribution of mRNAs in cultured preadipocytes was also compared with that of in vitro differentiated adipocytes derived from human omental adipose tissue. Cultured preadipocytes had far lower levels of the mRNAs for inflammatory proteins than the nonfat cells of omental adipose tissue. The nonfat cells were enriched by at least 5-fold in the mRNAs for proteins involved in the inflammatory response such as tumor necrosis factor alpha, interleukin lbeta, cyclooxygenase 2, interleukin 24, interleukin 6, and monocyte chemoattractant protein 1 plus the mRNAs for osteopontin, vaspin, endothelin, angiotensin II receptor 1, butyrylcholinesterase, lipocalin 2, and plasminogen activator inhibitor 1. The cells in the adipose tissue matrix were enriched at least 3-fold as compared with the isolated stromovascular cells in the mRNAs for proteins related to the inflammatory response, as well as osteopontin and endothelial nitric oxide synthase. We conclude that the mRNAs for inflammatory proteins are primarily present in the nonfat cells of human omental adipose tissue.
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PMID:Comparison of messenger RNA distribution for 60 proteins in fat cells vs the nonfat cells of human omental adipose tissue. 1855 44