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  • 1
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    The L-type amino acid transporter LAT1 inhibits osteoclastogenesis and maintains bone homeostasis through the mTORC1 pathway (2019)
    The American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉L-type amino acid transporter 1 (LAT1), which is encoded by 〈i〉solute carrier transporter 7a5〈/i〉 (〈i〉Slc7a5〈/i〉), plays a crucial role in amino acid sensing and signaling in specific cell types, contributing to the pathogenesis of cancer and neurological disorders. Amino acid substrates of LAT1 have a beneficial effect on bone health directly and indirectly, suggesting a potential role for LAT1 in bone homeostasis. Here, we identified LAT1 in osteoclasts as important for bone homeostasis. 〈i〉Slc7a5〈/i〉 expression was substantially reduced in osteoclasts in a mouse model of ovariectomy-induced osteoporosis. The osteoclast-specific deletion of 〈i〉Slc7a5〈/i〉 in mice led to osteoclast activation and bone loss in vivo, and 〈i〉Slc7a5〈/i〉 deficiency increased osteoclastogenesis in vitro. Loss of 〈i〉Slc7a5〈/i〉 impaired activation of the mechanistic target of rapamycin complex 1 (mTORC1) pathway in osteoclasts, whereas genetic activation of mTORC1 corrected the enhanced osteoclastogenesis and bone loss in 〈i〉Slc7a5〈/i〉-deficient mice. Last, 〈i〉Slc7a5〈/i〉 deficiency increased the expression of nuclear factor of activated T cells, cytoplasmic 1 (〈i〉Nfatc1〈/i〉) and the nuclear accumulation of NFATc1, a master regulator of osteoclast function, possibly through the canonical nuclear factor B pathway and the Akt–glycogen synthase kinase 3β signaling axis, respectively. These findings suggest that the LAT1-mTORC1 axis plays a pivotal role in bone resorption and bone homeostasis by modulating NFATc1 in osteoclasts, thereby providing a molecular connection between amino acid intake and skeletal integrity.〈/p〉
    Print ISSN: 1945-0877
    Electronic ISSN: 1937-9145
    Topics: Biology , Medicine
    Published by The American Association for the Advancement of Science (AAAS)
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  • 2
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    Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-07
    Description: The actin cytoskeleton undergoes extensive remodeling during cell morphogenesis and motility. The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a result of its phosphorylation by LIM-kinase. Cofilin was phosphorylated in N1E-115 neuroblastoma cells during lysophosphatidic acid-induced, Rho-mediated neurite retraction. This phosphorylation was sensitive to Y-27632, a specific inhibitor of the Rho-associated kinase ROCK. ROCK, which is a downstream effector of Rho, did not phosphorylate cofilin directly but phosphorylated LIM-kinase, which in turn was activated to phosphorylate cofilin. Overexpression of LIM-kinase in HeLa cells induced the formation of actin stress fibers in a Y-27632-sensitive manner. These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maekawa, M -- Ishizaki, T -- Boku, S -- Watanabe, N -- Fujita, A -- Iwamatsu, A -- Obinata, T -- Ohashi, K -- Mizuno, K -- Narumiya, S -- New York, N.Y. -- Science. 1999 Aug 6;285(5429):895-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Kyoto University Faculty of Medicine, Kyoto 606-8315, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10436159" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism ; Actin Depolymerizing Factors ; Actins/metabolism ; Amides/pharmacology ; Animals ; COS Cells ; DNA-Binding Proteins/metabolism ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Lim Kinases ; Lysophospholipids/pharmacology ; Membrane Proteins/*metabolism ; Microfilament Proteins/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Pyridines/pharmacology ; *Signal Transduction ; Tumor Cells, Cultured ; rho-Associated Kinases ; rhoB GTP-Binding Protein
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Rotational movement of the formin mDia1 along the double helical strand of an actin filament (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-12-15
    Description: Formin homology proteins (formins) elongate actin filaments (F-actin) by continuously associating with filament tips, potentially harnessing actin-generated pushing forces. During this processive elongation, formins are predicted to rotate along the axis of the double helical F-actin structure (referred to here as helical rotation), although this has not yet been definitively shown. We demonstrated helical rotation of the formin mDia1 by single-molecule fluorescence polarization (FL(P)). FL(P) of labeled F-actin, both elongating and depolymerizing from immobilized mDia1, oscillated with a periodicity corresponding to that of the F-actin long-pitch helix, and this was not altered by actin-bound nucleotides or the actin-binding protein profilin. Thus, helical rotation is an intrinsic property of formins. To harness pushing forces from growing F-actin, formins must be anchored flexibly to cell structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mizuno, Hiroaki -- Higashida, Chiharu -- Yuan, Yunfeng -- Ishizaki, Toshimasa -- Narumiya, Shuh -- Watanabe, Naoki -- New York, N.Y. -- Science. 2011 Jan 7;331(6013):80-3. doi: 10.1126/science.1197692. Epub 2010 Dec 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Single-Molecule Cell Biology, Tohoku University Graduate School of Life Sciences, 6-3 Aoba, Aramaki-Aza, Aoba-ku, Sendai, Miyagi 980-8578, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21148346" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/chemistry/*metabolism/ultrastructure ; Actins/chemistry/*metabolism ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Carrier Proteins/chemistry/*metabolism ; Fluorescence Polarization ; Mice ; Models, Biological ; Profilins/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Secondary ; Rabbits ; Recombinant Fusion Proteins/chemistry/metabolism ; Rotation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: The Rho guanosine 5'-triphosphatase (GTPase) cycles between the active guanosine triphosphate (GTP)-bound form and the inactive guanosine diphosphate-bound form and regulates cell adhesion and cytokinesis, but how it exerts these actions is unknown. The yeast two-hybrid system was used to clone a complementary DNA for a protein (designated Rhophilin) that specifically bound to GTP-Rho. The Rho-binding domain of this protein has 40 percent identity with a putative regulatory domain of a protein kinase, PKN. PKN itself bound to GTP-Rho and was activated by this binding both in vitro and in vivo. This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watanabe, G -- Saito, Y -- Madaule, P -- Ishizaki, T -- Fujisawa, K -- Morii, N -- Mukai, H -- Ono, Y -- Kakizuka, A -- Narumiya, S -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):645-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Kyoto University Faculty of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571126" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/chemistry/*metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Membrane Proteins/*metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C/chemistry/*metabolism ; *Protein-Serine-Threonine Kinases ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Signal Transduction ; ras Proteins ; *rho GTP-Binding Proteins ; rhoA GTP-Binding Protein ; rhoB GTP-Binding Protein
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Comparison of the kinetic disposition of and serum gastrin change by lansoprazole versus rabeprazole during an 8-day dosing scheme in relation to CYP2C19 polymorphism (2001)
    Springer
    Details
    Publication Date: 2001-09-01
    Print ISSN: 0031-6970
    Electronic ISSN: 1432-1041
    Topics: Chemistry and Pharmacology , Medicine
    Published by Springer
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  • 6
    Electronic Resource
    Electronic Resource
    Chronobiological studies on the blood-brain barrier (1981)
    Springer
    Cellular and molecular life sciences 37 (1981), S. 1013-1015 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Horseradish peroxidase (HRP) is a useful tracer for a study of the transportation of exogenous materials across vascular walls. After i.v. administration of HRP, reaction products of HRP can be recognized in the granular perithelial cells of small cerebral blood vessels at particular times of day. It suggests that there is a time-dependent fluctuation in the permeability of small cerebral blood vessels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01971811
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  • 7
    Electronic Resource
    Electronic Resource
    Antipyrine clearance in patients with Gilbert's syndrome (1984)
    Springer
    European journal of clinical pharmacology 27 (1984), S. 297-302 
    Details
    ISSN: 1432-1041
    Keywords: Gilbert's syndrome ; antipyrine clearance ; drug oxidizing capacity ; smoking habit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The pharmacokinetic parameters of antipyrine (AP) were examined in 45 normal healthy subjects (18 heavy smokers, 5 mild smokers, and 22 nonsmokers) and in 12 patients with Gilbert's syndrome (GS), amongst whom 2 mild and 1 heavy smokers were included. Heavy smokers were defined as persons smoking more than 20 cigarettes/day and mild smokers as those smoking less than 10 cigarettes/day. Significant differences (unpaired Student's t-test) in the elimination t1/2 of AP among the study groups and in its total plasma clearance (CL) were observed without any change in the apparent volume of distribution. The individual CL values varied within the same study groups, but the mean±SD (0.026±0.004 l/h/kg) in the GS patients did not significantly differ from that in normal nonsmokers (0.025±0.006 l/h/kg) or in normal mild smokers (0.028±0.001 l/h/kg). When the 3 patients with GS who smoked were excluded, the mean CL of the group (0.025 l/h/kg) was again comparable to that of the normal nonsmokers and mild smokers. The mean (±SD) CL in normal heavy smokers (0.040±0.012 l/h/kg) was significantly greater than in normal mild smokers (p〈0.05), in normal nonsmokers (p〈0.001) and in patients with GS (p〈0.001). The results suggest that drug oxidation capacity estimated from the total plasma CL of AP appears unimpaired in GS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00542163
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  • 8
    Electronic Resource
    Electronic Resource
    Serum doxapram and respiratory neuromuscular drive in normal man (1988)
    Springer
    European journal of clinical pharmacology 34 (1988), S. 55-59 
    Details
    ISSN: 1432-1041
    Keywords: doxapram ; ventilatory function ; occlusion pressure ; serum drug concentration ; concentration-effect relationship
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary To investigate the means by which doxapram affects the control of ventilation, ventilatory function and P0.1 have been related to serum doxapram concentration during a 45-min infusion of doxapram hydrochloride in 7 healthy, conscious subjects under normoxic conditions. Serum doxapram concentrations increased during the infusion: 1.88, 2.48, 3.42, and 3.97 µg/ml after 5, 10, 30 and 45 min, respectively. The majority of significant changes in the measurements from the baseline were observed at 30 and 45 min: $${{\dot V}}_{{E}}$$ , VT, P0.1, P0.1/end-tidal CO2 tension, VT/Ti and blood pressure were increased, and end-tidal CO2 tension was decreased. No significant changes in Pdimax, Ti/Ttot, $${{\dot V}}_{{E}}$$ /P0.1, and P0.1/(VT/Ti) were observed. A correlation was observed between the % increases in P0.1 and $${{\dot V}}_{{E}}$$ and doxapram concentration, and between $${{\dot V}}_{{E}}$$ and P0.1. The doxapram-induced increase in $${{\dot V}}_{{E}}$$ appears to be caused by increased neural drive. It is related to the serum drug concentration in the conscious subject.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01061418
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of theophylline on respiratory neuromuscular drive (1987)
    Springer
    European journal of clinical pharmacology 33 (1987), S. 85-88 
    Details
    ISSN: 1432-1041
    Keywords: theophylline ; aminophylline ; incremental concentration ; occlusion pressure ; maximum inspiratory pressure ; transdiaphragmatic pressure ; ventilatory function
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary To investigate the possible mechanisms by which theophylline affects the control of ventilation, neuromuscular drive and ventilatory function were examined in 7 healthy men receiving an incremental intravenous aminophylline dosing schedule to achieve plasma theophylline concentrations of 5, 10, and 15 µg/ml. As compared with the baseline (predose) values, the 3 incremental aminophylline doses significantly (p〈0.05 to 0.01) increased occlusion pressure (P0.1) and maximum inspiratory pressure static (MIPS) at functional residual capacity (FRC). This was not observed for ventilatory flow $$(\dot V)$$ , tidal volume (VT), inspiratory time to total breathing cycle time ratio (Ti/Ttot), VT/Ti, and effective impedance [P0.1/(VT/Ti)]. When maximum electrical activity of diaphragm (Edimax) and transdiaphragmatic pressure (Pdimax) were examined in 3 of the 7 subjects, Pdi/Edi tended to increase with increasing theophylline concentrations, while Edimax did not. Our results suggest that the increase in P0.1 during the increase in aminophylline dose is caused by an improvement in respiratory muscle contractility, rather than by a central effect or by an increase in neural drive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00610386
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  • 10
    Electronic Resource
    Electronic Resource
    Genetically determined N-acetylation and oxidation capacities in Japanese patients with non-occupational urinary bladder cancer (1989)
    Springer
    European journal of clinical pharmacology 37 (1989), S. 581-587 
    Details
    ISSN: 1432-1041
    Keywords: metoprolol ; dapsone ; bladder cancer ; acetylator phenotype ; oxidative phenotype ; pharmacogenetics ; Japanese
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Genetically determined polymorphisms of N-acetylation and oxidative capacity have been studied using dapsone and metoprolol in 51 Japanese patients with spontaneous bladder cancer and 203 healthy control subjects. The results for N-acetylation pharmacogenetics were against the initial expectation that there would be a preponderance of slow acetylators in the cancer group, as 3 such patients (5.9%) were found as compared to 13 (6.4%) in the healthy group. There was no poor metabolizer (PM) of metoprolol in the cancer group, whereas in the healthy group one (0.5%) was a PM. There were no significant differences between the groups in the frequency of slow acetylator and poor oxidiser phenotypes, or in the frequency distribution profiles of acetylation (monoacetyldapsone/dapsone) and oxidative metabolic ratio (log metoprolol/α-hydroxymetoprolol). The results indicate that neither N-acetylation nor the debrisoquine/sparteine-type oxidative phenotype and/or capacity represent a genetic predisposition to spontaneous bladder carcinogenesis in Japanese patients. In the normal Japanese population there is a great predominance of rapid acetylators and extensive oxidisers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00562549
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