The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index; none of the 2 sources its claims cite is checked for support yet.
Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
Open accessAbstract
During starvation-induced autophagy in mammals, autophagosomes form and fuse with lysosomes, leading to the degradation of the intra-autophagosomal contents by lysosomal proteases. During the formation of autophagosomes, LC3 is lipidated, and this LC3-phospholipid conjugate (LC3-II) is localized on autophagosomes and autolysosomes. While intra-autophagosomal LC3-II may be degraded by lysosomal hydrolases, recent studies have regarded LC3-II accumulation as marker of autophagy. The effect of lysosomal turnover of endogenous LC3-II in this process, however, has not been considered. We therefore investigated the lysosomal turnover of endogenous LC3-II during starvation-induced autophagy using E64d and pepstatin A, which inhibit lysosomal proteases, including cathepsins B, D and L. We found that endogenous LC3-II significantly accumulated in the presence of E64d and pepstatin A under starvation conditions, increasing about 3.5 fold in HEK293 cells and about 6.7 fold in HeLa cells compared with that in their absence, whereas the amount of LC3-II in their absence is cell-line dependent. Morphological analyses indicated that endogenous LC3-positive puncta and autolysosomes increased in HeLa cells under starvation conditions in the presence of these inhibitors. These results indicate that endogenous LC3-II is considerably degraded by lysosomal hydrolases after formation of autolysosomes, and suggest that lysosomal turnover, not a transient amount, of this protein reflects starvation-induced autophagic activity.
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TL;DR
The paper shows that endogenous LC3-II is rapidly degraded by lysosomal hydrolases during starvation-induced autophagy, so the cellular level of LC3-II alone does not reliably indicate autophagic activation. Measuring LC3-II in the presence versus absence of E64d and pepstatin A reveals lysosomal turnover and better estimates autophagy.
Key findings
- Under starvation conditions, endogenous LC3-II was about 3.5-fold higher in HEK293 cells and about 6.7-fold higher in HeLa cells when treated with E64d and pepstatin A than without these inhibitors.
- In HEK293 cells, without inhibitors LC3-II increased 2 h after starvation induction but slightly decreased at 4 h; with E64d and pepstatin A, LC3-II increased dramatically in a time-dependent manner.
- In HeLa cells, LC3-positive puncta and autolysosomes accumulated with E64d and pepstatin A under starvation; autolysosomes per 100 µm² of cytoplasmic area were about 7.3-fold higher with inhibitors than without.
- In A431, MDA-MB-231, and SK-N-SH cells, endogenous LC3-II was present under nutrient-rich conditions despite S6RP phosphorylation, suggesting LC3-II levels are not a simple marker for autophagic activity.
Methods
- HeLa and HEK293 cells were cultured in DMEM with 10% FCS and starved in Krebs-Ringer medium; E64d (10 µg/ml) and pepstatin A (10 µg/ml) were used to inhibit lysosomal proteases.
- Endogenous LC3-I and LC3-II were analyzed by immunoblotting with anti-human LC3 antibody and densitometry; Tor pathway activity was monitored using phospho- and total S6RP, S6K, and Tor antisera.
- LC3 localization was examined by immunofluorescence with Alexa Fluor594-conjugated anti-LC3 antibody and 2D blind deconvolution; autophagosomes/autolysosomes were examined by electron microscopy.
Limitations
- Stated: the anti-human LC3 antibody was not suitable for immunoelectron microscopy, so the relationship between LC3 and autolysosomes could not be directly confirmed by immunoelectron microscopy.
- Stated: there is no evidence for a Cvt-like pathway in mammalian cells, which is offered as one possible explanation for LC3-II under nutrient-rich conditions.
- Evident: the conclusions rely on pharmacological protease inhibitors and cultured cell lines; no in vivo animal validation is described in this paper. The comparison of endogenous LC3 with GFP-human LC3 is cited as unpublished results and is not shown.
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0 of 2 cited sources checked · 0 supported · 0 flagged
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In the presence of these inhibitors, LC3-II dramatically accumulates under starvation conditions in both HeLa and HEK293 cells, as do LC3-positive puncta and autolysosomal structures.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: E64d and pepstatin A inhibit the proteolytic activities of cathepsins B, D and L, causing autolysosomes containing cytosolic components to accumulate.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“When we compared the lysosomal degradation of endogenous LC3 with that of GFP-human LC3, we found that GFP-human LC3 tended to accumulate less than endogenous LC3 in the presence of E64d and pepstatin A under starvation conditions (Tanida I, Ueno T, Kominami E, unpublished results”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In the presence of these inhibitors, LC3-II dramatically accumulates under starvation conditions in both HeLa and HEK293 cells, as do LC3-positive puncta and autolysosomal structures.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: E64d and pepstatin A inhibit the proteolytic activities of cathepsins B, D and L, causing autolysosomes containing cytosolic components to accumulate.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In the presence of these inhibitors, LC3-II dramatically accumulates under starvation conditions in both HeLa and HEK293 cells, as do LC3-positive puncta and autolysosomal structures.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: E64d and pepstatin A inhibit the proteolytic activities of cathepsins B, D and L, causing autolysosomes containing cytosolic components to accumulate.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Furthermore, in HeLa cells, LC3-II decreases under starvation conditions in the absence of E64d and pepstatin A, while it increases under the same conditions in HEK293 cells.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Furthermore, in HeLa cells, LC3-II decreases under starvation conditions in the absence of E64d and pepstatin A, while it increases under the same conditions in HEK293 cells.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In some cell lines, however, LC3-II remains present under nutrient-rich conditions without inactivation of Tor kinase.”
- Also stated in: § Autophagy 89 · plain
“In some cell lines, including HeLa, A431, MDA-MB-231, and SK-N-SH cells, endogenous LC3-II is present even under nutrientrich conditions without inactivation of Tor kinase.”
§ Isei > Autophagy 89
Load-bearingStrength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Also stated in: § Autophagy 89 · plain
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“These results indicate that the lysosomal degradation of intra-autophagosomal components (Fig. 1, Step 3) significantly affects the amount of endogenous LC3-II after the formation of autophagosomes.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Rests on an assumption: E64d and pepstatin A inhibit the proteolytic activities of cathepsins B, D and L, causing autolysosomes containing cytosolic components to accumulate.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Therefore, measurement of endogenous LC3 is better for estimating lysosomal degradation.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIn the paper
“Furthermore, inhibiting the fusion of autophagosomes with lysosomes using rab7 RNAi led to the accumulation of LC3-II, indicating that during the impairment of autophagosome-lysosome fusion LC3 is lipidated and LC3-II accumulates.52”
§ Isei > Autophagy 89
What the sources say
- Not matchedcites [52]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passes- Not matched
- It may state two separate claims as one. 2
In the paper
“Furthermore, inhibiting the fusion of autophagosomes with lysosomes using rab7 RNAi led to the accumulation of LC3-II, indicating that during the impairment of autophagosome-lysosome fusion LC3 is lipidated and LC3-II accumulates.52”
§ Isei > Autophagy 89
What the sources say
- Not matchedcites [52]
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- Not matched
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“However, an increase in the amount of endogenous LC3-II can occur under three conditions: (1) lipidation of LC3-I to form LC3-II during autophagosome-formation, (2) inhibition of the fusion of autophagosomes with lysosomes, and (3) inhibition of lysosomal degradation.”
§ Isei > Autophagy 89
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
The paper relies on this without support.
E64d and pepstatin A inhibit the proteolytic activities of cathepsins B, D and L, causing autolysosomes containing cytosolic components to accumulate.
“When E64d and pepstatin A are added to the medium, the proteolytic activities of these cathepsins are inhibited, and autolysosomes containing cytosolic components accumulate.”
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?
In the citing paper
“LC3 is a cytosolic protein that plays a crucial role in the formation of autophagosomes (Tanida et al., 2005).”
From Nilotinib restores memory function by preventing dopaminergic neuron degeneration in a mouse model of Alzheimer’s Disease (2021) · cites this paper as Tanida et al., 2005
In the citing paper
“Autophagy involves the delivery of cytoplasmic substrates (cellular proteins and damaged organelles) to lysosomes for degradation and impairment of this process is associated with premature ageing and age-associated decline in tissue function [58], [71].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [58]
In the citing paper
“LC3-II: LC3-I ratio is not a reliable indicator of autophagy in cells possessing dysfunctional lysosomes and so was not evaluated for the senescent cells [58].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [58]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Figure 3B is cited as starvation-condition LC3-II evidence
MinorThe text cites Figure 3B for increased LC3-II under starvation, but the figure caption identifies panel B as a nutrient-rich-condition fluorescence image. The caption assigns starvation conditions to other panels.
“Together with our finding that the amount of endogenous LC3-II increased under starvation conditions in the presence of E64d and pepstatin A (Fig. 3B), these results indicate that this increase in LC3-II correlates with an increase in LC3-positive puncta.”
“HeLa cells were cultured in DMEM containing 10% FCS (Nutrient-rich, A and B) or transferred to KRB medium for 4 h (Starvation, C, D and G-J).”
Citations
Cites
The publisher hasn’t deposited this paper’s reference list.
Research works printed but not linked: 8
- Ohsumi Y. Molecular dissection of autophagy: Two ubiquitin-like systems. Nat Rev Mol Cell Biol 2001; 2:211-6.
- Bursch W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ 2001; 8:569-81.
- Klionsky DJ. Cell biology: Regulated self-cannibalism. Nature 2004; 431:31-2.
- Pfeifer U. Functional morphology of the lysosomal apparatus. In: Glaumann H, Ballard FJ, eds. Lysosomes: Their role in protein breakdown. London: Academic Press, 1987:3-59.
- Seglen PO. Regulation of autophagic protein degradation in isolated liver cells. In: Glaumann H, Ballard FJ, eds. Lysosomes: Their role in protein breakdown. London: Academic Press, 1987:371-414.
- Andersson G, Glaumann H. Current Methods for the isolation of coated vesicles, endo- cytic vesicles, the Golgi complex, lysosomes and autophagic vacuoles. In: Glaumann H, Ballard FJ, eds. Lysosomes: Their role in protein breakdown. London: Academic Press, 1987:61-113.
- Kirschke H, Barrett AJ. Chemistry of lysosomal proteases. In: Glaumann H, Ballard FJ, eds. Lysosomes: Their role in protein breakdown. London: Academic Press, 1987:193-238.
- Mizushima N. Methods for monitoring autophagy. Int J Biochem Cell Biol 2004; 36:2491-502.
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Enhanced mitophagy in bronchial fibroblasts from severe asthmatic patients
Ramakrishnan, R. K., Bajbouj, K., Hachim, M. Y., Mogas, A. K., Mahboub, B. H., Olivenstein, R., Hamoudi, R., Halwani, R., & Hamid, Q. A. (2020) · PLoS ONE · doi:10.1371/journal.pone.0242695 · Cited by 27
Inhibition of phospholipase D2 induces autophagy in colorectal cancer cells
Hwang, W. C., Kim, M. K., Song, J., Choi, K.-Y., & Min, D.-S. (2014) · Experimental and Molecular Medicine · doi:10.1038/emm.2014.74 · Cited by 23
Autophagy in Pancreatic Acinar Cells in Caerulein-treated Mice
Zhang, L. W., Zhang, J., Shea, K. I., Xu, L., Tobin, G., Knapton, A. D., Stewart, S. R., & Rouse, R. L. (2013) · Toxicologic Pathology · doi:10.1177/0192623313486967 · Cited by 26
“VMP1 expression promotes the conversion of LC3-I to LC3II (Itakura and Mizushima 2010; Tanida et al. 2005) allowing LC3-II to translocate from the cytoplasm to the autophagosomal membrane.”
BackgroundAutophagy as a Therapeutic Target of Natural Products Enhancing Embryo Implantation
Park, H., Cho, M., Do, Y., Park, J.-K., Bae, S., Joo, J., & Ha, K. (2021) · Pharmaceuticals · doi:10.3390/ph15010053 · Cited by 25
“During the autophagy process, Lc3b-II bound to the autophagosomal inner membrane is degraded by lysosomal enzymes, whereas those located in the autophagosomal outer membrane are released into the cytosol and recycled [56].”
BackgroundKim, N. Y., Jung, Y. Y., Yang, M. H., Chinnathambi, A., Govindasamy, C., Narula, A. S., Namjoshi, O. A., Blough, B. E., & Ahn, K. S. (2022) · Biochimie · doi:10.1016/j.biochi.2022.05.018 · Cited by 24
Payne, C. M., Crowley-Skillicorn, C., Holubec, H., Dvorak, K., Bernstein, C., Moyer, M. P., Garewal, H. S., & Bernstein, H. (2009) · Journal of Toxicology · doi:10.1155/2009/785907 · Cited by 24
“CuDIPS: 100 μM [15]; Bafilomycin A1: 1 nM [41, 42]; Catalase: 1000 U/mg; E-64d: 10 μg/mL [43]; 3-MA: 4 mM; HBED: 100 μM [44, 45]; HCS: 10 μM [46]; MnTBAP: 100 μM [47]; Pepstatin A: 10 μg/mL [43]; Rapa: 100 μM.”
Yamamoto, K., Seki, T., Adachi, N., Takahashi, T., Tanaka, S., Hide, I., Saito, N., & Sakai, N. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01395.x · Cited by 24
“To further confirm the increase in LC3-II by rapamycin, we assessed the level of LC3-II in the presence of the lysosomal protease inhibitors pepstatin A and E64d because LC3-II is degraded by lysosomal proteases (Tanida et al. 2005).”
BackgroundHe, H., Sun, Y., Zheng, L., et al. (2015) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2015.16.3.1169 · Cited by 24
“Therefore, the cellular level of LC3 II has been regarded that reflects the activation of autophagy (Tanida et al., 2005).”
Feleciano, D. R., Juenemann, K., Iburg, M., Brás, I. C., Holmberg, C. I., & Kirstein, J. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00009 · Cited by 27
Kang, S. H., Bak, D., Chung, B. Y., Bai, H., & Kang, B. S. (2020) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2020.24.5.413 · Cited by 25
“The protein LC3 is well-known as an autophagosomal marker, and the formation of autophagosomes is commonly considered the standard of autophagy induction [23].”
BackgroundIkezoe, K., Furuya, H., Arahata, H., Nakagawa, M. M., Tateishi, T., Fujii, N., & Kira, J. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0488-1 · Cited by 25
Cost-effectiveness of immunization in The Gambia.
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Sato, T., Ito, Y., & Nagasawa, T. (2016) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2016.1210499 · Cited by 26
Stempels, F. C., Janssens, M. H., ter Beest, M., Mesman, R., Revelo, N. H., Ioannidis, M., & van den Bogaart, G. (2022) · FEBS Letters · doi:10.1002/1873-3468.14280 · Cited by 25
Developing a set of guidelines for your research field: a practical approach
Klionsky, D. J. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-09-0618 · Cited by 23
“The seminal paper making this point was published in 2005 (Tanida et al., 2005); however, I routinely see papers submitted to Autophagy in which the authors did not adequately address this issue.”
BackgroundCrosstalk from survival to necrotic death coexists in DU-145 cells by curcumin treatment
Kang, D., Park, W., Lee, S., Kim, J.-H., & Song, J. J. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.01.014 · Cited by 23
Turzanski, J., Daniels, I., & Haynes, A. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07555.x · Cited by 24
“Briefly, 5 lg of total cellular protein was separated on 15% wt/vol polyacrylamide gels, transferred to polyvinylidene fluoride membranes and probed for LC3II (Tanida et al, 2005).”
BackgroundMethodE2F-1 lacking the transcriptional activity domain induces autophagy
García‐García, A., Rodríguez‐Rocha, H., Tseng, M. T., Montes‐de‐Oca‐Luna, R., Zhou, H. S., McMasters, K. M., & Gómez-Gutiérrez, J. G. (2012) · Cancer Biology & Therapy · doi:10.4161/cbt.21143 · Cited by 25
“LC3-II accumulation is a hallmark of autophagy.(31,32) We analyzed the expression of LC3 and the conversion of LC3-I to LC3-II.”
BackgroundDuan, J., Yin, J., Ren, W., Wu, M. M., Chen, S., Cui, Z. J., Wu, X., Huang, R., Li, T. J., & Yin, Y. (2014) · Free Radical Research · doi:10.3109/10715762.2014.993627 · Cited by 24
Long-Lived Protein Degradation During Autophagy
Dupont, N., Leroy, C., Hamaï, A., & Codogno, P. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.074 · Cited by 23
Compensatory increases of select proteostasis networks after Hsp70 inhibition in cancer cells
Sannino, S., Guerriero, C. J., Sabnis, A. J., Stolz, D. B., Wallace, C. T., Wipf, P., Watkins, S. C., Bivona, T. G., & Brodsky, J. L. (2018) · Journal of Cell Science · doi:10.1242/jcs.217760 · Cited by 23
“…an HDAC6 inhibitor that perturbs both autophagolysosome formation and the recruitment of ubiquitylated proteins to nascent autophagosomes (Bennett et al., 2005; Hubbert et al., 2002; Kawaguchi et al., 2003; Manic et al., 2014; Mizushima et al., 2011; Pandey et al., 2007; Tanida et al., 2005).”
BackgroundLi, T. X., Cheng, F., Wang, L., et al. (2019) · Molecules · doi:10.3390/molecules24061091 · Cited by 23
“The level of LC3-II is related to the amount of autophagosomes in the cell; thus, LC3-II acts as a reliable marker of autophagy [31].”
BackgroundFogde, D. L., Xavier, C. P. R., Balnytė, K., Holland, L. K. K., Stahl-Meyer, K., Dinant, C., Corcelle–Termeau, E., Pereira‐Wilson, C., Maeda, K., & Jäättelä, M. (2022) · Cells · doi:10.3390/cells11244079 · Cited by 26
“The RLuc-LC3/RLuc-LC3(G120A) ratio inversely reflects autophagic flux, as only the RLuc-LC3 is degraded by autophagy [51].”
BackgroundGenipin increases oxaliplatin-induced cell death through autophagy in gastric cancer
Kim, B. R., Jeong, Y. A., Kim, D. Y., Kim, J. L., Jeong, S., Na, Y. J., Yun, H. K., Park, S. H., Jo, M. J., Ashktorab, H., et al. (2019) · Journal of Cancer · doi:10.7150/jca.34773 · Cited by 24
“As LC3 is a marker of autophagosomal membranes, change of LC3-II expression are associated with the autophagic activity via lysosome [16].”
BackgroundAnthrax Lethal Toxin Downregulates Claudin-5 Expression in Human Endothelial Tight Junctions
D’Agnillo, F., Williams, M. C., Moayeri, M., & Warfel, J. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062576 · Cited by 22
“To further examine the involvement of the lysosomal pathway, cells were treated with the combination of E-64, an inhibitor of cysteine proteases, and pepstatin A, an inhibitor of aspartic proteases (EP) [33,34].”
Wang, H.-J., Chen, S., & Lo, W. (2016) · Scientific Reports · doi:10.1038/srep35372 · Cited by 22
Jiao, H., Nie, X., Zhu, H., Li, B., Pang, F., Xiao-hong, Y., Cao, R., Yang, X., Zhu, S., Peng, D., et al. (2020) · BioMed Research International · doi:10.1155/2020/1953242 · Cited by 22
“3e presence of LC3 in autophagosomes and the conversion of LC3-I to the lower migrating form LC3-II have been used as indicators of autophagy [30].”
MethodEffects and mechanisms of Chinese herbal medicine on IgA nephropathy
Ma, S., Zhao, M., Chang, M., Shi, X., Shi, Y. X., & Zhang, Y. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154913 · Cited by 23
HIV-1 differentially modulates autophagy in neurons and astrocytes.
Mehla, R., & Chauhan, A. (2015) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2015.06.001 · Cited by 26
“To investigate the role of the autophagy pathway in HIV-1-induced astrocyte toxicity, we treated HFA with HIV-1 particles and monitored temporal expression of LC3 protein, which is a marker for autophagosome formation (Tanida et al., 2005; Klionsky et al., 2008).”
Autophagy upregulation and loss of NF-κB in oxidative stress-related immunodeficient SAMP8 mice
Caballero, B., Vega‐Naredo, I., Sierra, V., de Gonzalo‐Calvo, D., Medrano‐Campillo, P., Guerrero, J. M., Tolivia, D., Rodríguez‐Colunga, M. J., & Coto‐Montes, A. M. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.09.001 · Cited by 22
Mukhopadhyay, S., Sinha, N., Das, D. N., Panda, P. K., Naik, P. P., & Bhutia, S. K. (2016) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2015.1135103 · Cited by 22
Autophagy – molecular mechanism, apoptosis and cancer
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“[90] Tanida I.”
BackgroundNiimi, N., Yako, H., Tsukamoto, M., Takaku, S., Yamauchi, J., Kawakami, E., Yanagisawa, H., Watabe, K., Utsunomiya, K., & Sango, K. (2016) · European Journal of Neuroscience · doi:10.1111/ejn.13268 · Cited by 22
“tion for 24 h in the presence or absence of inhibitors of lysosomal protein degradation, such as E64d (Sigma, 10 lg/mL) and pepstatin A (Sigma, 10 lg/mL) (Tanida et al., 2005).”
BackgroundHe, Y., Zhu, J., Huang, Y., Heng Jun, G. A. O., & Zhao, Y. (2015) · Acta Diabetologica · doi:10.1007/s00592-015-0763-7 · Cited by 24
“If cells are treated with the lysosomal proton pump inhibitor bafilomycin A1 (BA), the degradation of LC3-II is blocked, resulting in the accumulation of LC3-II [26].”
BackgroundShi, J., Shi, S. R., Wu, B., Zhang, J., Li, Y., Wu, X., Zhang, J., Wang, K., Zhao, B., Cai, W., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20771 · Cited by 24
“And the changes in the LC3-II/LC3-I ratio are indicative of autophagic capacity [13, 14, 45].”
Qin, F., Yao, J., Zhou, G., Xia, W., Lyu, J., Li, X., Zhao, T., Zhang, G., Zhao, N., & Yang, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01881 · Cited by 23
“The amount of LC3-II is widely used for the quantification of autophagosome formation (21).”
BackgroundArsenite-induced apoptosis can be attenuatedviadepletion of mTOR activity to restore autophagy
Wu, C., Lin, P.-J., Tsai, J.-S., Lin, C.-Y., & Lin, L. (2018) · Toxicology Research · doi:10.1039/c8tx00238j · Cited by 23
Yang, Y., Wang, Z., Cao, Y., Liu, J., Li, P., Li, H., & Liu, M. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01041 · Cited by 22
Autophagy as a Vital Therapy Target for Renal Cell Carcinoma
He, Y.-H., & Tian, G. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.518225 · Cited by 23
Autophagosomes accumulate in differentiated and hypertrophic adipocytes in a p53-independent manner
Mikami, K., Okita, N., Tokunaga, Y., Ichikawa, T., Okazaki, T., Takemoto, K., Nagai, W., Matsushima, S., & Higami, Y. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.09.134 · Cited by 22
Autophagy and cardiometabolic risk factors
Juárez-Rojas, J. G., Reyes‐Soffer, G., Conlon, D., & Ginsberg, H. N. (2014) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-014-9295-7 · Cited by 21
“After autophagosome and lysosome fusion, degradation of the inner vesicle is dependent on a series of lysosomal/vacuolar acid hydrolases, such as proteinases A and B (encoded by PEP4 and PRB1, respectively) and cathepsins B, D and L [40].”
BackgroundMitophagy in the aging nervous system
Rappe, A., & McWilliams, T. G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.978142 · Cited by 22
A noncanonical function of SKP1 regulates the switch between autophagy and unconventional secretion
Li, J., Krause, G. J., Gui, Q., Kaushik, S., Róna, G., Zhang, Q., Liang, F., Dhabaria, A., Anerillas, C., Martindale, J. L., et al. (2023) · Science Advances · doi:10.1126/sciadv.adh1134 · Cited by 21
“…compartments) as changes in the abundance of LC3B-II (integral component of autophagic vesicles) upon blocking endolysosomal proteolysis by treatment of cells with a combination of ammonium chloride (to neutralize lysosomal acidification) and leupeptin (to inhibit endo-lysosomal proteases) ( 36 ).”
Kumari, S., Singh, P., & Singh, R. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111272 · Cited by 21
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Silencing of cadherin-17 enhances apoptosis and inhibits autophagy in colorectal cancer cells
Xia, T., Han, Z., Zhu, Q., Tan, J., Liu, W., Wang, Y., Chen, W., Zou, Y., Cai, Y., Huang, S., et al. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.09.020 · Cited by 23
Nazim, U. M., Yin, H., & Park, S. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9757 · Cited by 21
RetractedMethods for Monitoring Matrix-Induced Autophagy
Chen, C. G., Kapoor, A., & Iozzo, R. V. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9133-4_14 · Cited by 20
“Immunofluorescence especially comes in handy to analyze different steps of autophagy in which autophagosomal marker proteins such as microtubule-associated light chain β (LC3β) and sequestosome-1 (p62/SQSTM1) are stained or tagged with fluorophores (81).”
BackgroundSikder, S., Kumari, S., Mustafi, P., Ramdas, N. M., Padhi, S., Saha, A., Bhaduri, U., Banerjee, B., Manjithaya, R. R., & Kundu, T. K. (2019) · FEBS Journal · doi:10.1111/febs.14952 · Cited by 22
S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux
Hać, A., Pierzynowska, K., & Herman-Antosiewicz, A. (2021) · Cells · doi:10.3390/cells10040929 · Cited by 21
Neuronal Cell Death: An Overview of Its Different Forms in Central and Peripheral Neurons
Lossi, L., Castagna, C., & Merighi, A. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2152-2_1 · Cited by 22
A Glimmer of Hope: Maintain Mitochondrial Homeostasis to Mitigate Alzheimer’s Disease
Li, W., Kui, L., Tsirukis, D. I., Gong, X., & Tang, M. (2020) · Aging and Disease · doi:10.14336/ad.2020.0105 · Cited by 21
“The signal of LC3-II increases in the presence of one of the above inhibitors when the autophagic flux is occurring as the transition of LC3-II is blocked [97-99].”
BackgroundNon-coding RNA-mediated autophagy in cancer: A protumor or antitumor factor?
Liang, J., Zhang, L., & Cheng, W. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188642 · Cited by 20
Tp47 promoted the phagocytosis of HMC3 cells though autophagy induced by endoplamic reticlum stress
Li, W., Li, Q., Xu, Q. ‐., Wang, X., & Yang, T. (2022) · Journal of the European Academy of Dermatology and Venereology · doi:10.1111/jdv.18295 · Cited by 20
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Metadata
- Authors
- Tanida, I., Minematsu-Ikeguchi, N., Ueno, T., & Kominami, E.
- Affiliations
- Juntendo University (JP)
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2005-07-05
- Volume
- 1
- Issue
- 2
- Pages
- 84-91
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- OpenAlex
- W1990138203
- Semantic Scholar
- 0b28240a0597c546157837f2fb3739b45c71db72
- Cited by
- 1,108
- References
- 0
- Citations by year
- 2026: 27 · 2025: 36 · 2024: 30 · 2023: 42 · 2022: 63 · 2021: 79 · 2020: 67 · 2019: 87 · 2018: 61 · 2017: 70 · 2016: 62 · 2015: 58 · 2014: 54 · 2013: 72 · 2012: 55
- FWCI
- 20.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Autophagy (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Private School Promotion Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- LC3-II, starvation-induced autophagy, autolysosomes, lysosomal proteases, cathepsins, E64d, pepstatin A, autophagosome formation, autophagy markers, LC3 lipidation
- MeSH terms
- Autophagy, Biological Transport, Active, Cell Line, Humans, Hydrolases, Leucine, Lysosomes, Microtubule-Associated Proteins, Pepstatins, Phagosomes, Biomarkers, Microscopy, Electron, Transmission
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