Cited by 208Autophagy in Disease and TherapyPI3K/AKT/mTOR signaling in cancerMuscle metabolism and nutrition

The DOI matches its Crossref record; 56 of the 57 references it cites were found in a registry or an index.

Amino Acids and Insulin Control Autophagic Proteolysis through Different Signaling Pathways in Relation to mTOR in Isolated Rat Hepatocytes

Open access

Kanazawa, Takumi, Taneike, Ikue, Akaishi, Ryuichiro, Yoshizawa, Fumiaki, Furuya, Norihiko, Fujimura, Shinobu, Kadowaki, Motoni·2004·Journal of Biological Chemistry

DOI 10.1074/jbc.m306337200

Open this paper in CoChat — free account

Abstract

Autophagy, a major bulk proteolytic pathway, contributes to intracellular protein turnover, together with protein synthesis. Both are subject to dynamic control by amino acids and insulin. The mechanisms of signaling and cross-talk of their physiological anabolic effects remain elusive. Recent studies established that amino acids and insulin induce p70 S6 kinase (p70(S6k)) phosphorylation by mTOR, involved in translational control of protein synthesis. Here, the signaling mechanisms of amino acids and insulin in macroautophagy in relation to mTOR were investigated. In isolated rat hepatocytes, both regulatory amino acids (RegAA) and insulin coordinately activated p70(S6k) phosphorylation, which was completely blocked by rapamycin, an mTOR inhibitor. However, rapamycin blocked proteolytic suppression by insulin, but did not block inhibition by RegAA. These contrasting results suggest that insulin controls autophagy through the mTOR pathway, but amino acids do not. Furthermore, micropermeabilization with Saccharomyces aureus alpha-toxin completely deprived hepatocytes of proteolytic responsiveness to RegAA and insulin, but still maintained p70(S6k) phosphorylation by RegAA. In contrast, Leu(8)-MAP, a non-transportable leucine analogue, did not mimic the effect of leucine on p70(S6k) phosphorylation, but maintained the activity on proteolysis. Finally, BCH, a System L-specific amino acid, did not affect proteolytic suppression or mTOR activation by leucine. All the results indicate that mTOR is not common to the signaling mechanisms of amino acids and insulin in autophagy, and that the amino acid signaling starts extracellularly with their "receptor(s)," probably other than transporters, and is mediated through a novel route distinct from the mTOR pathway employed by insulin.

Integrity signals

Registry

Crossref · 10.1074/jbc.m306337200

Cites

56 of 56 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Chapter 4 Preparation of Isolated Rat Liver Cells
Seglen, P. O. (1976) · Methods in cell biology · doi:10.1016/s0091-679x(08)61797-5 · Cited by 5,297
Autophagy as a Regulated Pathway of Cellular Degradation
Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630
TOR, a Central Controller of Cell Growth
Schmelzle, T., & Hall, M. N. (2000) · Cell · doi:10.1016/s0092-8674(00)00117-3 · Cited by 1,914
Amino Acid Sufficiency and mTOR Regulate p70 S6 Kinase and eIF-4E BP1 through a Common Effector Mechanism
Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14484 · Cited by 1,370
Dissection of Autophagosome Formation Using Apg5-Deficient Mouse Embryonic Stem Cells
Mizushima, N., Yamamoto, A., Hatano, M., Kobayashi, Y., Kabeya, Y., Suzuki, K., Tokuhisa, T., Ohsumi, Y., & Yoshimori, T. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.657 · Cited by 1,361
Tor, a Phosphatidylinositol Kinase Homologue, Controls Autophagy in Yeast
Noda, T., & Ohsumi, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.7.3963 · Cited by 1,303
Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex
Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M., & Ohsumi, Y. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1507 · Cited by 1,145

Show all 57 references

Research works printed but not linked: 5

Fafournoux, 2000, Biochem. J., 351, 1, 10.1042/bj3510001 · DOI
van Sluijters, 2000, Biochem. J., 351, 545, 10.1042/bj3510545 · DOI
Seglen, 1976, 13, 29
Pacitti, 1993, Am. J. Physiol., 265, G90
Shah, 2000, Am. J. Physiol., 279, E74

Sorted by citations

Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,094
Autophagy and signaling: their role in cell survival and cell death
Codogno, P., & Meijer, A. J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401751 · Cited by 1,106
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967
Autophagy gone awry in neurodegenerative diseases
Wong, E., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 815
Autophagy regulation by nutrient signaling
Russell, R. C., Yuan, H., & Guan, K. (2013) · Cell Research · doi:10.1038/cr.2013.166 · Cited by 740
Autophagy: A lysosomal degradation pathway with a central role in health and disease
Eskelinen, E., & Säftig, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.014 · Cited by 716
Autophagy, amyloidogenesis and Alzheimer disease
Nixon, R. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.019265 · Cited by 749
Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling
Wang, X., Hu, Z., Hu, J., Du, J., & Mitch, W. E. (2006) · Endocrinology · doi:10.1210/en.2006-0251 · Cited by 600
Methods for Monitoring Autophagy from Yeast to Human
Klionsky, D. J., Cuervo, A. M., & Seglen, P. O. (2007) · Autophagy · doi:10.4161/auto.3678 · Cited by 656
Synergistic Augmentation of Rapamycin-Induced Autophagy in Malignant Glioma Cells by Phosphatidylinositol 3-Kinase/Protein Kinase B Inhibitors
Takeuchi, H., Kondo, Y., Fujiwara, K., Kanzawa, T., Aoki, H., Mills, G. B., & Kondo, S. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3640 · Cited by 545
Regulation of macroautophagy by mTOR and Beclin 1 complexes
Pattingre, S., Espert, L., Biard‐Piechaczyk, M., & Codogno, P. (2007) · Biochimie · doi:10.1016/j.biochi.2007.08.014 · Cited by 535
Programmed Autophagy in the Drosophila Fat Body Is Induced by Ecdysone through Regulation of the PI3K Pathway
Rusten, T. E., Lindmo, K., Juhász, G., Sass, M., Seglen, P. O., Brech, A., & Stenmark, H. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.07.005 · Cited by 487
Ceramide-mediated Macroautophagy Involves Inhibition of Protein Kinase B and Up-regulation of Beclin 1
Scarlatti, F., Bauvy, C., Ventruti, A., Sala, G., Cluzeaud, F., Vandewalle, A., Ghidoni, R., & Codogno, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313561200 · Cited by 388
Microtubules Facilitate Autophagosome Formation and Fusion of Autophagosomes with Endosomes
Köchl, R., Hu, X. W., Chan, E. Y. W., & Tooze, S. A. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00368.x · Cited by 436
Functions of autophagy in normal and diseased liver
Czaja, M. J., Ding, W., Donohue, T. M., Friedman, S. L., Js, K., Komatsu, M., Lemasters, J. J., Lemoine, A., Lin, J. D., Ou, J. J., et al. (2013) · Autophagy · doi:10.4161/auto.25063 · Cited by 438
Regulation of adipocyte lipolysis
Frühbeck, G., Méndez-Giménez, L., Fernández‐Formoso, J. A., Fernández, S., & Rodrı́guez, A. (2014) · Nutrition Research Reviews · doi:10.1017/s095442241400002x · Cited by 447
Altered lipid content inhibits autophagic vesicular fusion
Koga, H., Kaushik, S., & Cuervo, A. M. (2010) · The FASEB Journal · doi:10.1096/fj.09-144519 · Cited by 395
Amino acid regulation of TOR complex 1
Avruch, J., Long, X., Ortiz-Vega, S., Rapley, J., Papageorgiou, A., & Dai, N. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90645.2008 · Cited by 400
The role of leucine and its metabolites in protein and energy metabolism
Duan, Y., Li, F., Li, Y., Tang, Y., Kong, X., Feng, Z., Anthony, T. G., Watford, M., Hou, Y., Wu, G., et al. (2015) · Amino Acids · doi:10.1007/s00726-015-2067-1 · Cited by 364
Regulation of Liver Metabolism by Autophagy
Madrigal‐Matute, J., & Cuervo, A. M. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.09.042 · Cited by 319
Liver autophagy contributes to the maintenance of blood glucose and amino acid levels
Ezaki, J., Matsumoto, N., Takeda‐Ezaki, M., Komatsu, M., Takahashi, K., Hiraoka, Y., Taka, H., Fujimura, T., Takehana, K., Yoshida, M., et al. (2011) · Autophagy · doi:10.4161/auto.7.7.15371 · Cited by 296
Self-citation
Attenuated mTOR Signaling and Enhanced Autophagy in Adipocytes from Obese Patients with Type 2 Diabetes
Öst, A., Svensson, K., Ruishalme, I., Brännmark, C., Franck, N., Krook, H., Sandström, P., Kjølhede, P., & Strålfors, P. (2010) · Molecular Medicine · doi:10.2119/molmed.2010.00023 · Cited by 274
Autophagy in cardiac myocyte homeostasis, aging, and pathology
Terman, A., & Brunk, U. T. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.08.014 · Cited by 270
TOR-dependent control of autophagy: biting the hand that feeds
Neufeld, T. P. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.005 · Cited by 261
Autophagy in the liver
Yin, X., Ding, W., & Gao, W. (2008) · Hepatology · doi:10.1002/hep.22146 · Cited by 253
The serine/threonine kinase ULK1 is a target of multiple phosphorylation events
Bach, M., Larance, M., James, D. E., & Ramm, G. (2011) · Biochemical Journal · doi:10.1042/bj20101894 · Cited by 233
Signalling and autophagy regulation in health, aging and disease
Meijer, A. J., & Codogno, P. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.002 · Cited by 252
Preservation of Liver Protein Synthesis during Dietary Leucine Deprivation Occurs at the Expense of Skeletal Muscle Mass in Mice Deleted for eIF2 Kinase GCN2
Anthony, T. G., McDaniel, B. J., Reinert, R. B., McGrath, B. C., Cavener, D. R., McNurlan, M. A., & Wek, R. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404559200 · Cited by 232
The amino acid sensitive TOR pathway from yeast to mammals
Dann, S. G., & Thomas, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.068 · Cited by 216
Inhibition of Akt signaling and enhanced ERK1/2 activity are involved in induction of macroautophagy by triterpenoid B-group soyasaponins in colon cancer cells
Ellington, A. A., Berhow, M. A., & Singletary, K. W. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi214 · Cited by 209
Autophagy: Regulation and role in disease
Meijer, A. J., & Codogno, P. (2009) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360903044068 · Cited by 215
Natural products to prevent drug resistance in cancer chemotherapy: a review
Yuan, R., Hou, Y., Sun, W. C., Yu, J. Z., Liu, X., Niu, Y., Lu, J., & Chen, X. (2017) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13387 · Cited by 201
Amino Acids Activate Mammalian Target of Rapamycin Complex 2 (mTORC2) via PI3K/Akt Signaling
Tato, I., Bartrons, R., Ventura, F., & Rosa, J. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166991 · Cited by 201
Regulation of autophagy by amino acids and MTOR-dependent signal transduction
Meijer, A. J., Lorin, S., Blommaart, E. F. C., & Codogno, P. (2014) · Amino Acids · doi:10.1007/s00726-014-1765-4 · Cited by 202
Systemic autophagy insufficiency compromises adaptation to metabolic stress and facilitates progression from obesity to diabetes
Lim, Y.-M., Lim, H., Hur, K. Y., Quan, W., Lee, H.-Y., Cheon, H., Ryu, D., Koo, S.-H., Kim, H. L., Kim, J., et al. (2014) · Nature Communications · doi:10.1038/ncomms5934 · Cited by 189
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189
“sents an alternative strategy for regulating autophagy in an MTOR-independent fashion: amino acid starvation induces autophagy, whereas amino acid provision results in RPS6KB/ p70S6K phosphorylation and autophagy suppression [512].”
Background
Autophagic Stress in Neuronal Injury and Disease
Chu, C. T. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229233.75253.be · Cited by 211
All-you-can-eat: autophagy in neurodegeneration and neuroprotection
Jaeger, P. A., & Wyss‐Coray, T. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-16 · Cited by 181
Induction of autophagy promotes differentiation of glioma‐initiating cells and their radiosensitivity
Zhuang, W., Li, B.-Z., Long, L., Chen, L., Huang, Q., & Liang, Z. (2011) · International Journal of Cancer · doi:10.1002/ijc.25975 · Cited by 170
Utilizing flow cytometry to monitor autophagy in living mammalian cells
Shvets, E., Fass, E., & Elazar, Z. (2008) · Autophagy · doi:10.4161/auto.5939 · Cited by 163
Salmon spawning migration and muscle protein metabolism: the August Krogh principle at work
Mommsen, T. P. (2004) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpc.2004.09.018 · Cited by 163
New Insights into the Mechanisms of Macroautophagy in Mammalian Cells
Eskelinen, E. (2008) · International review of cytology · doi:10.1016/s1937-6448(07)66005-5 · Cited by 161
Autophagy Signaling and the Cogwheels of Cancer
Botti, J., Djavaheri‐Mergny, M., Pilatte, Y., & Codogno, P. (2006) · Autophagy · doi:10.4161/auto.2.2.2458 · Cited by 154
Silencing mammalian target of rapamycin signaling by small interfering RNA enhances rapamycin-induced autophagy in malignant glioma cells
Iwamaru, A., Kondo, Y., Iwado, E., Aoki, H., Fujiwara, K., Yokoyama, T., Mills, G. B., & Kondo, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209992 · Cited by 149
Redox Control of Protein Kinase C: Cell- and Disease-Specific Aspects
Giorgi, C., Agnoletto, C., Baldini, C., Bononi, A., Bonora, M., Marchi, S., Missiroli, S., Patergnani, S., Poletti, F., Rimessi, A., et al. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2825 · Cited by 152
The role of macroautophagy in the ageing process, anti-ageing intervention and age-associated diseases
Bergamini, E., Cavallini, G., Donati, A., & Gori, Z. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.05.007 · Cited by 145
Regulation of mTOR by amino acids and resistance exercise in skeletal muscle
Deldicque, L., Theisen, D., & Francaux, M. (2005) · European Journal of Applied Physiology · doi:10.1007/s00421-004-1255-6 · Cited by 147
Isoleucine, a Blood Glucose-Lowering Amino Acid, Increases Glucose Uptake in Rat Skeletal Muscle in the Absence of Increases in AMP-Activated Protein Kinase Activity
Doi, M., Yamaoka, I., Nakayama, M., Mochizuki, S., Sugahara, K., & Yoshizawa, F. (2005) · Journal of Nutrition · doi:10.1093/jn/135.9.2103 · Cited by 140
Self-citation
The Role of Autophagy in Aging
Bergamini, E., Cavallini, G., Donati, A., & Gori, Z. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1396.020 · Cited by 136
Chapter 13 Cytosolic LC3 Ratio as a Quantitative Index of Macroautophagy
Kadowaki, M., & Karim, M. R. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03613-6 · Cited by 133
Self-citation
Glutamine Increases Autophagy Under Basal and Stressed Conditions in Intestinal Epithelial Cells
Sakiyama, T., Musch, M. W., Ropeleski, M. J., Tsubouchi, H., & Chang, E. B. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.12.002 · Cited by 133
Decreased Insulin-Receptor Signaling Promotes the Autophagic Degradation of β-Amyloid Peptide inC. elegans
Florez‐McClure, M. L., Hohsfield, L. A., Fonte, G., Bealor, M. T., & Link, C. D. (2007) · Autophagy · doi:10.4161/auto.4776 · Cited by 130
Cytosolic LC3 Ratio as a Sensitive Index of Macroautophagy in Isolated Rat Hepatocytes and H4-II-E Cells
Karim, M. R., Kanazawa, T., Daigaku, Y., Fujimura, S., Miotto, G., & Kadowaki, M. (2007) · Autophagy · doi:10.4161/auto.4615 · Cited by 120
Self-citation
Skeletal Muscle-derived Myonectin Activates the Mammalian Target of Rapamycin (mTOR) Pathway to Suppress Autophagy in Liver
Seldin, M. M., Lei, X., Tan, S. Y., Stanson, K. P., Wei, Z., & Wong, G. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500736 · Cited by 124
Tuning Cell Autophagy by Diversifying Carbon Nanotube Surface Chemistry
Wu, L., Zhang, Y., Zhang, C., Cui, X., Zhai, S., Liu, Y., Li, C., Zhu, H., Qu, G., Jiang, G., et al. (2014) · ACS Nano · doi:10.1021/nn500376w · Cited by 121
Autophagy and Tau Protein
Hamano, T., Enomoto, S., Shirafuji, N., Ikawa, M., Yamamura, O., Yen, S.-H. C., & Nakamoto, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147475 · Cited by 122
Intracellular network of phosphatidylinositol 3-kinase, mammalian target of the rapamycin/70 kDa ribosomal S6 kinase 1, and mitogen-activated protein kinases pathways for regulating mycobacteria-induced IL-23 expression in human macrophages
Yang, C., Song, C., Lee, J., Jung, S.-B., Oh, J.-H., Park, J., Kim, H., Park, J., Paik, T.-H., & Jo, E. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00699.x · Cited by 107
Glutamine metabolism and signaling in the liver
Häussinger, D. (2006) · Frontiers in bioscience · doi:10.2741/2070 · Cited by 106
An obligatory requirement for the heterotrimeric G protein G i3 in the antiautophagic action of insulin in the liver
Gohla, A., Klement, K., Piekorz, R. P., Pexa, K., Dahl, S. V., Spicher, K., Dreval', V. I., Häussinger, D., Birnbaumer, L., & Nürnberg, B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611434104 · Cited by 105
Rapamycin Inhibits Polyglutamine Aggregation Independently of Autophagy by Reducing Protein Synthesis
King, M. A., Hands, S., Hafiz, F., Mizushima, N., Tolkovsky, A. M., & Wyttenbach, A. (2008) · Molecular Pharmacology · doi:10.1124/mol.107.043398 · Cited by 120
Leucine suppresses myofibrillar proteolysis by down-regulating ubiquitin–proteasome pathway in chick skeletal muscles
Nakashima, K., Ishida, A., Yamazaki, M., & Abé, H. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.138 · Cited by 102
Structure–activity relations of leucine derivatives reveal critical moieties for cellular uptake and activation of mTORC1-mediated signaling
Nagamori, S., Wiriyasermkul, P., Okuda, S., Kojima, N., Hari, Y., Kiyonaka, S., Mori, Y., Tominaga, H., Ohgaki, R., & Kanai, Y. (2016) · Amino Acids · doi:10.1007/s00726-015-2158-z · Cited by 96
Autophagy: a new target for nonalcoholic fatty liver disease therapy
Mao, Y., Yu, F., Wang, J., Guo, C., & Fan, X. (2016) · Hepatic Medicine Evidence and Research · doi:10.2147/hmer.s98120 · Cited by 101
Branched-chain amino acid-enriched supplementation improves insulin resistance in patients with chronic liver disease
Kawaguchi, T., Nagao, Y., Matsuoka, H., Ide, T., & Sata, M. (2008) · International Journal of Molecular Medicine · doi:10.3892/ijmm.22.1.105 · Cited by 98
Eugenol-Induced Autophagy and Apoptosis in Breast Cancer Cells via PI3K/AKT/FOXO3a Pathway Inhibition
Abdullah, M. L., Al‐Shabanah, O. A., Hassan, Z. K., & Hafez, M. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179243 · Cited by 96
Cardioprotection requires taking out the trash
Gottlieb, R. A., Finley, K. D., & Mentzer, R. M. (2009) · Basic Research in Cardiology · doi:10.1007/s00395-009-0011-9 · Cited by 97
Autophagy, nutrition and immunology
Cuervo, A. M., & Macián, F. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.09.001 · Cited by 98
Regulation of Autophagy Enzymes by Nutrient Signaling
King, K. E., Losier, T. T., & Russell, R. C. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.01.006 · Cited by 92
Nucleocytoplasmic localization of p70 S6K1, but not of its isoforms p85 and p31, is regulated by TSC2/mTOR
Rosner, M., & Hengstschläger, M. (2011) · Oncogene · doi:10.1038/onc.2011.165 · Cited by 92
Postprandial Regulation of Hepatic MicroRNAs Predicted to Target the Insulin Pathway in Rainbow Trout
Mennigen, J. A., Panserat, S., Larquier, M., Plagnes‐Juan, E., Médale, F., Seiliez, I., & Cassy, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038604 · Cited by 93
Autophagy: A cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically
Bergamini, E. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.001 · Cited by 90
Dual targeting of AKT and mammalian target of rapamycin: A potential therapeutic approach for malignant peripheral nerve sheath tumor
Zou, C., Smith, K. D., Zhu, Q.-S., Liu, J., McCutcheon, I. E., Slopis, J. M., Meric‐Bernstam, F., Peng, Z., Bornmann, W. G., Mills, G. B., et al. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-1008 · Cited by 88
Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy
Menzies, F. M., Hourez, R., Imarisio, S., Raspe, M. A., Sadiq, O., Chandraratna, D., O’Kane, C. J., Rock, K. L., Reits, E. A., Goldberg, A. L., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq385 · Cited by 81
The autophagy conundrum in cancer: influence of tumorigenic metabolic reprogramming
Eng, C. H., & Abraham, R. T. (2011) · Oncogene · doi:10.1038/onc.2011.220 · Cited by 83
Nutrient control of macroautophagy in mammalian cells
Kadowaki, M., Karim, M. R., Carpi, A., & Miotto, G. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.010 · Cited by 80
Self-citation
Chapter 4 Assaying of Autophagic Protein Degradation
Bauvy, C., Meijer, A. J., & Codogno, P. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03604-5 · Cited by 79
Altered APP Processing in Insulin-Resistant Conditions Is Mediated by Autophagosome Accumulation via the Inhibition of Mammalian Target of Rapamycin Pathway
Son, S. M., Song, H., Byun, J., Park, K. S., Jang, H. C., Park, Y. J., & Mook‐Jung, I. (2012) · Diabetes · doi:10.2337/db11-1735 · Cited by 81
Isolation of Hyperactive Mutants of Mammalian Target of Rapamycin
Ohne, Y., Takahara, T., Hatakeyama, R., Matsuzaki, T., Noda, M., Mizushima, N., & Maeda, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801546200 · Cited by 70
The yeast Saccharomyces cerevisiae: An overview of methods to study autophagy progression
Delorme‐Axford, E., Guimarães, R. S., Reggiori, F., & Klionsky, D. J. (2014) · Methods · doi:10.1016/j.ymeth.2014.12.008 · Cited by 74
Interaction between mTOR pathway inhibition and autophagy induction attenuates adriamycin-induced vascular smooth muscle cell senescence through decreased expressions of p53/p21/p16
Sung, J. Y., Lee, K. Y., Kim, J., & Choi, H. C. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.08.001 · Cited by 72
Mitigating Ischemic Injury of Stem Cell-Derived Insulin-Producing Cells after Transplant
Faleo, G., Russ, H. A., Wisel, S., Parent, A. V., Nguyen, V., Nair, G. G., Freise, J. E., Villanueva, K. E., Szot, G. L., Hebrok, M., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.07.012 · Cited by 65
Amino Acid Regulation of Autophagosome Formation
Meijer, A. J. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-157-4_5 · Cited by 64
Diverse Facets of Sphingolipid Involvement in Bacterial Infections
Kunz, T. C., & Kozjak‐Pavlovic, V. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00203 · Cited by 62
Target of Rapamycin in Control of Autophagy: Puppet Master and Signal Integrator
Mugume, Y., Kazibwe, Z., & Bassham, D. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218259 · Cited by 61
Autophagy and metabolism
Lin, P., Chu, M., & Liu, H. (2020) · The Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.12299 · Cited by 53
In Rat Hepatocytes Glucagon Increases Mammalian Target of Rapamycin Phosphorylation on Serine 2448 but Antagonizes the Phosphorylation of Its Downstream Targets Induced by Insulin and Amino Acids
Mothe‐Satney, I., Gautier, N., Hinault, C., Lawrence, J. C., & OBBERGHEN, E. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405173200 · Cited by 53
Insulin-like Growth Factor-I Prevents the Accumulation of Autophagic Vesicles and Cell Death in Purkinje Neurons by Increasing the Rate of Autophagosome-to-lysosome Fusion and Degradation
Bains, M., Florez‐McClure, M. L., & Heidenreich, K. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.011791 · Cited by 52
Activating Autophagy as a Therapeutic Strategy for Parkinson’s Disease
Fowler, A. J., & Moussa, C. (2018) · CNS Drugs · doi:10.1007/s40263-018-0497-5 · Cited by 51
Autophagy restricts proliferation driven by oncogenic phosphatidylinositol 3-kinase in three-dimensional culture
Chen, N., Eritja, N., Lock, R., & Debnath, J. (2013) · Oncogene · doi:10.1038/onc.2012.277 · Cited by 50
Autophagy plays an essential role in bone homeostasis
Jaber, F. A., Khan, N. M., Ansari, M. Y., Al-Adlaan, A. A., Hussein, N. J., & Safadi, F. F. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.27071 · Cited by 50
Role of autophagy and its significance in cellular homeostasis
Awan, M. U. F., & Deng, Y. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5721-8 · Cited by 49
WWOX suppresses autophagy for inducing apoptosis in methotrexate-treated human squamous cell carcinoma
Tsai, C.-W., Lai, F.-J., Sheu, H.-M., Lin, Y.-S., Chang, T.-H., Jan, M.-S., Chen, S. M., Hsu, P.-C., Huang, T.-T., Huang, T.-C., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.308 · Cited by 48
Molecular mechanisms relating to amino acid regulation of protein synthesis
Cao, Y., Liu, S., Liu, K., Abbasi, I. H. R., Cai, C., & Yao, J. (2019) · Nutrition Research Reviews · doi:10.1017/s0954422419000052 · Cited by 49
Cell hydration and mTOR‐dependent signalling
Schliess, F., Richter, L., Dahl, S. V., & Häussinger, D. (2006) · Acta Physiologica · doi:10.1111/j.1748-1716.2006.01547.x · Cited by 48
Adiponectin Lowers Glucose Production by Increasing SOGA
Cowerd, R. B., Asmar, M. M., Alderman, J. M., Alderman, E. A., Garland, A. L., Busby, W. H., Bodnar, W. M., Rusyn, I., Medoff, B. D., Tisch, R., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.100363 · Cited by 46
In yeast, loss of Hog1 leads to osmosensitivity of autophagy
Prick, T., Thumm, M., Köhrer, K., Häussinger, D., & Dahl, S. V. (2006) · Biochemical Journal · doi:10.1042/bj20051243 · Cited by 46
Macroautophagy: The key ingredient to a healthy diet?
Hannigan, A. M., & Gorski, S. M. (2009) · Autophagy · doi:10.4161/auto.5.2.7529 · Cited by 43
Techniques to Study Autophagy in Plants
Mitou, G., Budak, H., & Gözüaçık, D. (2009) · International Journal of Plant Genomics · doi:10.1155/2009/451357 · Cited by 46
Developmental Commitment in Dictyostelium discoideum
Katoh‐Kurasawa, M., Chen, G., Roberge, E., Shaulsky, G., & Kuspa, A. (2007) · Eukaryotic Cell · doi:10.1128/ec.00223-07 · Cited by 40
Suppression of myofibrillar proteolysis in chick skeletal muscles by α-ketoisocaproate
Nakashima, K., Yakabe, Y., Ishida, A., Yamazaki, M., & Abé, H. (2006) · Amino Acids · doi:10.1007/s00726-006-0404-0 · Cited by 38

Authors: Kanazawa, T., Taneike, I., Akaishi, R., Yoshizawa, F., Furuya, N., Fujimura, S., & Kadowaki, M.
Affiliations: Niigata University (JP)
Utsunomiya University (JP)
Corresponding author: Kadowaki, Motoni
ORCID: Yoshizawa, Fumiaki
Furuya, Norihiko
Fujimura, Shinobu
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2004-02
Volume: 279
Issue: 9
Pages: 8452-8459
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m306337200
OpenAlex: W2054125361
Cited by: 208
References: 57
Citations by year: 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 5 · 2021: 7 · 2020: 6 · 2019: 13 · 2018: 5 · 2017: 10 · 2016: 7 · 2015: 8 · 2014: 16 · 2013: 12 · 2012: 9
FWCI: 12.69
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6100 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords: autophagy, amino acids, insulin, mTOR, p70 S6 kinase, hepatocytes, leucine, rapamycin, protein turnover, amino acid signaling, alpha-toxin, BCH
MeSH terms: Amino Acids, Amino Acids, Cyclic, Animals, Bacterial Toxins, Cell Membrane, Enzyme Inhibitors, Hemolysin Proteins, Insulin, Leucine, Male, Peptide Hydrolases, Phosphorylation, Protein Kinases, Signal Transduction, Rats, Wistar, Sirolimus, Hepatocytes, Ribosomal Protein S6 Kinases, 70-kDa, Protein Kinase Inhibitors, Rats, TOR Serine-Threonine Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Amino Acids and Insulin Control Autophagic Proteolysis through Different Signaling Pathways in Relation to mTOR in Isolated Rat Hepatocytes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks