Asai S

References (3)

Title : Characterization of a novel lipolytic enzyme from Aspergillus oryzae - Koseki_2013_Appl.Microbiol.Biotechnol_97_5351
Author(s) : Koseki T , Asai S , Saito N , Mori M , Sakaguchi Y , Ikeda K , Shiono Y
Ref : Applied Microbiology & Biotechnology , 97 :5351 , 2013
Abstract : In this study, we report the characterization of a protein from Aspergillus oryzae, exhibiting sequence identity with paraben esterase from the genus Aspergillus. The coding region of 1,586 bp, including a 77-bp intron, encoded a protein of 502 amino acids. The gene without the signal peptide of 19 amino acids was cloned into a vector, pPICZalphaC, and expressed successfully in Pichia pastoris as an active extracellular protein. The purified recombinant protein had pH and temperature optima of 7.0-8.0 and 30 degrees C, respectively, and was stable at the pH range of 7.0-10.0 and up to 40 degrees C. The optimal substrate for hydrolysis by the purified recombinant protein, among a panel of alpha-naphthyl esters (C2-C16), was alpha-naphthyl butyrate (C4), with activity of 0.16 units/mg protein. The considerable hydrolytic activity of the purified recombinant enzyme toward tributyrin was determined. However, no paraben esterase activity was detected toward the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. In addition, no activity was detected toward the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids that would indicate feruloyl esterase activity.
ESTHER : Koseki_2013_Appl.Microbiol.Biotechnol_97_5351
PubMedSearch : Koseki_2013_Appl.Microbiol.Biotechnol_97_5351
PubMedID: 23001008
Gene_locus related to this paper: aspor-q2uf27

Title : Muscarinic agonist potencies at three different effector systems linked to the M(2) or M(3) receptor in longitudinal smooth muscle of guinea-pig small intestine - Okamoto_2002_Br.J.Pharmacol_135_1765
Author(s) : Okamoto H , Prestwich SA , Asai S , Unno T , Bolton TB , Komori S
Ref : British Journal of Pharmacology , 135 :1765 , 2002
Abstract : 1. The abilities of muscarinic agonists (arecoline, bethanechol, carbachol, McN-A343, methacholine, pilocarpine) to inhibit isoprenaline-induced cyclic AMP production in chopped fragments (via M(2) receptors), and to evoke cationic current (I(cat)) (via M(2) receptors) or calcium store release (via M3 receptors) in enzyme-dispersed, single voltage-clamped cells from longitudinal smooth muscle of the guinea-pig small intestine were examined. 2. All muscarinic agonists (1 - 300 microM) examined inhibited isoprenaline (1 microM)-induced accumulation of cyclic AMP, the IC(50) varying from 52 to 248 microM. However, their relative potencies to evoke this M(2) effect were not significantly correlated with their ability to evoke I(cat), also a M(2) effect, whether or not calcium stores were depleted; pilocarpine and McN-A343 inhibited the I(cat) response to carbachol. 3. Muscarinic agonists (concentration 300 or 1000 microM), except pilocarpine and McN-A343 which were ineffective, evoked Ca(2+)-activated K(+) current (I(K-Ca)) resulting from Ca(2+) store release (M(3) effect). Their effectiveness was tested by estimating residual stored calcium by subsequent application of caffeine (10 mM). The relative potencies to evoke Ca(2+) store release (M(3)) and for I(cat) activation (M(2)) were closely correlated (P<0.001). 4. These data might be explained if M(2)-mediated adenylyl cyclase inhibition and I(cat) activation involve different G proteins, or involve different populations of M(2) receptors. The observed correlation of agonist potency between I(cat) activation and Ca(2+) store release supports the proposal (Zholos & Bolton, 1997) that M(3) activation can potentiate M(2)-cationic channel coupling through Ca(2+)-independent mechanisms.
ESTHER : Okamoto_2002_Br.J.Pharmacol_135_1765
PubMedSearch : Okamoto_2002_Br.J.Pharmacol_135_1765
PubMedID: 11934818

Title : Effect of 9-amino-2,3,5,6,7,8-hexahydro-1H-cyclopenta-(b)-quinoline monohydrate hydrochloride (NIK-247) on cholinergic enzyme activity in rats - Shibanoki_1991_Pharmacol.Biochem.Behav_39_499
Author(s) : Shibanoki S , Ishii Y , Kubo T , Kogure M , Asai S , Ishikawa K
Ref : Pharmacol Biochem Behav , 39 :499 , 1991
Abstract : An in vitro comparison demonstrated that the concentration of NIK-247 that inhibited cholinesterase (ChE) activities to half the normal level (ID50) was 1.3 x 10(-6) M. This value was higher than those for both physostigmine (PHY; 1.2 x 10(-7) M) and tetrahydroaminoacridine (THA; 3.6 x 10(-7) M), which are used as cholinesterase inhibitors in the treatment of cholinergic deficits. Neither NIK-247 nor THA affected the activity of choline acetyltransferase (ChAT). These inhibitions of ChE by NIK-247 and PHY lasted for 2 h, while that by THA lasted for over 4 h. In the effects of NIK-247 and PHY, the concentrations of intrastriatal acetylcholine (ACh) were changed in relation to the inhibition of the ChE activity. However, THA caused a transient increase in the ACh level lasting for only 2 h instead of inhibiting the enzyme activity for over 4 h. These findings suggest that NIK-247 is a drug with a similar profile in its effect on cholinergic neurons to PHY, the prototype drug among ChE inhibitors. The data indicate that NIK-247 may be useful as a drug for the treatment of central as well as peripheral deficits of the cholinergic mechanism.
ESTHER : Shibanoki_1991_Pharmacol.Biochem.Behav_39_499
PubMedSearch : Shibanoki_1991_Pharmacol.Biochem.Behav_39_499
PubMedID: 1946590