Latkripiini 1
2.
Batool S, Joseph TP, Hussain M, Vuai MS, Khinsar KH, Din SRU, Padhiar AA, Zhong M, Ning A, Zhang W, Cao J, Huang M.
Int J Mol Sci. 2018 Sep 30;19(10). pii: E2986. doi: 10.3390/ijms19102986.PMID:30274346
Present study aimed to elucidate the
anticancer effect and the possible molecular mechanism underlying the
action of Latcripin 1 (LP1), from the mushroom Lentinula edodes strain C91-3
against gastric cancer cell lines SGC-7901 and BGC-823. Cell viability
was measured by Cell Counting Kit-8 (CCK-8); morphological changes were
observed by phase contrast microscope; autophagy was determined by
transmission electron microscope and fluorescence microscope. Apoptosis
and cell cycle were assessed by flow cytometer; wound-healing, transwell
migration and invasion assays were performed to investigate the effect
of LP1 on gastric cancer cell's migration and invasion. Herein, we found
that LP1 resulted in the induction of autophagy by the formation of autophagosomes
and conversion of light chain 3 (LC3I into LC3II.
LP1 up-regulated the expression level of autophagy-related gene (Atg7, Atg5, Atg12, Atg14) and Beclin1; increased and decreased the expression level of pro-apoptotic (Bax) and anti-apoptotic (Bcl-2) proteins respectively, along with the activation of Caspase-3.
At lower-doses, LP1 have shown to arrest cells in the S phase of the cell cycle and decreased the expression level of matrix metalloproteinase MMP-2 and MMP-9.
In addition, it has also been shown to regulate the phosphorylation of one of the most hampered gastric cancer pathway, that is, protein kinase B/mammalian target of rapamycin (Akt/mTOR) channel and resulted in cell death.
These findings suggested LP1 as a potential natural anti-cancer agent, for exploring the gastric cancer therapies and as a contender for further in vitro and in vivo investigations.KEYWORDS:
LP1 up-regulated the expression level of autophagy-related gene (Atg7, Atg5, Atg12, Atg14) and Beclin1; increased and decreased the expression level of pro-apoptotic (Bax) and anti-apoptotic (Bcl-2) proteins respectively, along with the activation of Caspase-3.
At lower-doses, LP1 have shown to arrest cells in the S phase of the cell cycle and decreased the expression level of matrix metalloproteinase MMP-2 and MMP-9.
In addition, it has also been shown to regulate the phosphorylation of one of the most hampered gastric cancer pathway, that is, protein kinase B/mammalian target of rapamycin (Akt/mTOR) channel and resulted in cell death.
These findings suggested LP1 as a potential natural anti-cancer agent, for exploring the gastric cancer therapies and as a contender for further in vitro and in vivo investigations.KEYWORDS:
Latcripin 1; Lentinula edodes; apoptosis; autophagy; gastric cancer; metastasis
3.
Akhtar MJ, Ahamed M, Alhadlaq HA, Alrokayan SA.
J Trace Elem Med Biol. 2018 Dec;50:283-290. doi: 10.1016/j.jtemb.2018.07.016. Epub 2018 Jul 20.PMID:30262293
4.
Li CX, Cui LH, Zhuo YZ, Hu JG, Cui NQ, Zhang SK.
Life Sci. 2018 Sep 1;208:276-283. doi: 10.1016/j.lfs.2018.07.049. Epub 2018 Jul 26.PMID:30056017
AbstractAIMS:Autophagy
is an intracellular metabolic process that degrades and recycles own
constituents to maintain homeostasis and supply substrates. Disruption
of collagen degradation is one of the pathogenesis of pancreatic
fibrosis. In this study, we investigated the effects of inhibiting
autophagy on the collagen degradation of PSCs. MAIN METHODS:
... Autophagosome
was confirmed by transmission electron microscope. Immunofluorescence
for LC3B and α-SMA were applied to assess autophagy and activated PSCs.
The effects of autophagy inhibition of 3-MA on the expressions of LC3B,
Atg5, and Beclin-1 were investigated by real-time PCR and Western
blotting, as well as the α-SMA, TGF-β1, ColI, Col III, FN, MMP-2, MMP-13, TIMP-1 and TIMP-2. Meanwhile, the secretion of ColI, Col III and FN were investigated by ELISA. KEY FINDINGS:
The LC3-II/I ratio was increased in rat CP model. Autophagosomes
and an increased autophagic level were observed during PSCs activation.
Inhibiting autophagy could down-regulate the expressions of α-SMA,
TGF-β1, FN, ColI, Col III, TIMP-1 and TIMP-2, while the expressions of MMP-2 and MMP-13 were increased. SIGNIFICANCE: This
study confirmed that autophagic level is increased during PSCs
activation in vivo and in vitro. Inhibiting autophagy prevents the
activation of PSCs, and suppresses fibrosis through promoting
extracellular matrix (ECM) degradation by decreasing the expression of
TGF-β1 and increasing MMPs/TIMPs ratio.Copyright © 2018 Elsevier Inc. All rights reserved.KEYWORDS:
Autophagy; Collagen; LC3B; Pancreatic stellate cells; α-SMA
5.
Meng Z, Shen B, Gu Y, Wu Z, Yao J, Bian Y, Zeng D, Chen K, Cheng S, Fu J, Peng L, Zhao Y.
J Cell Biochem. 2018 Jun 28. doi: 10.1002/jcb.27145. [Epub ahead of print] PMID: 29953665
Accumulating evidence suggests that
autophagy plays a protective role in chondrocytes and prevents cartilage
degeneration in osteoarthritis (OA). The objective of this study was to
investigate the effect of diazoxide on chondrocyte death and cartilage
degeneration and to determine whether these effects are correlated to
autophagy in experimental OA. In this study, a cellular OA model was
established by stimulating SW1353 cells with interleukin 1β. A rat OA
model was generated by transecting the anterior cruciate ligament
combined with the resection of the medial menisci, followed by treatment
with diazoxide or diazoxide combination with 3-methyladenine. The
percentage of viable cells was evaluated using
calcein-acetoxymethyl/propidium iodide double staining. The messenger
RNA expression levels of collagen type II alpha 1 chain (COL2A1), matrix
metalloproteinase 13 (MMP-13),
TIMP metallopeptidase inhibitor 1 (TIMP-1), and a disintegrin and
metalloproteinase with thrombospondin motifs 5 (ADAMTS5) were determined
using quantitative real-time polymerase chain reaction. The cartilage
thickness and joint space were evaluated using ultrasound. SW1353 cell
degeneration and autophagosomes
were observed using transmission electron microscopy. The expression
levels of microtubule-associated protein 1 light chain 3 (LC3),
beclin-1, P62, COL2A1, and MMP-13
were evaluated using immunofluorescence staining and Western blot
analysis. Diazoxide significantly attenuated articular cartilage
degeneration and SW1353 cell death in experimental OA. The restoration
of autophagy was observed in the diazoxide-treated group. The beneficial
effects of diazoxide were markedly blocked by 3-methyladenine.
Diazoxide treatment also modulated the expression levels of OA-related
biomarkers. These results demonstrated that diazoxide exerted a
chondroprotective effect and attenuated cartilage degeneration by
restoring autophagy via modulation of OA-related biomarkers in
experimental OA. Diazoxide treatment might be a promising therapeutic
approach to prevent the development of OA.KEYWORDS:
SW1353 cell; autophagy; diazoxide; osteoarthritis; osteoarthritis-related biomarker
(Ajatuksia herättävä artikkeli: siis modulointia solukaliumin ja kalsiumin suhteen nivelrustotasossa!)
(Ajatuksia herättävä artikkeli: siis modulointia solukaliumin ja kalsiumin suhteen nivelrustotasossa!)
7.
Hong JM, Shin JK, Kim JY, Jang MJ, Park SK, Lee JH, Choi JH, Lee SM.
Biol Pharm Bull. 2018 Aug 1;41(8):1257-1268. doi: 10.1248/bpb.b18-00207. Epub 2018 May 23.
- PMID:
- 29794403
8.
Lin H, Zhang C, Zhang H, Xia YZ, Zhang CY, Luo J, Yang L, Kong LY.
Phytomedicine. 2018 Mar 15;42:190-198. doi: 10.1016/j.phymed.2018.03.046. Epub 2018 Mar 19.
- PMID:
- 29655686
9.
Yang F, Liao J, Pei R, Yu W, Han Q, Li Y, Guo J, Hu L, Pan J, Tang Z.
Chemosphere. 2018 Aug;204:36-43. doi: 10.1016/j.chemosphere.2018.03.192. Epub 2018 Mar 29.
- PMID:
- 29649662
10.
You P, Wu H, Deng M, Peng J, Li F, Yang Y.
Biomed Pharmacother. 2018 Feb;98:619-625. doi: 10.1016/j.biopha.2017.12.057. Epub 2017 Dec 29.
- PMID:
- 29289836
11.
Hong YJ, Ahn HJ, Shin J, Lee JH, Kim JH, Park HW, Lee SK.
J Reprod Immunol. 2018 Feb;125:56-63. doi: 10.1016/j.jri.2017.12.001. Epub 2017 Dec 14.
- PMID:
- 29253794
12.
Lombardo T, Folgar MG, Salaverry L, Rey-Roldán E, Alvarez EM, Carreras MC, Kornblihtt L, Blanco GA.
Basic Clin Pharmacol Toxicol. 2018 May;122(5):489-500. doi: 10.1111/bcpt.12945. Epub 2018 Jan 3.
- PMID:
- 29205851
13.
Lv W, Sui L, Yan X, Xie H, Jiang L, Geng C, Li Q, Yao X, Kong Y, Cao J.
Chem Biol Interact. 2018 Jan 5;279:136-144. doi: 10.1016/j.cbi.2017.11.013. Epub 2017 Nov 24.
- PMID:
- 29179951
14.
Wu Q, Gao C, Wang H, Zhang X, Li Q, Gu Z, Shi X, Cui Y, Wang T, Chen X, Wang X, Luo C, Tao L.
Int J Biochem Cell Biol. 2018 Jan;94:44-55. doi: 10.1016/j.biocel.2017.11.007. Epub 2017 Nov 22.
- PMID:
- 29174311
15.
Bai F, Huang Q, Nie J, Lu S, Lu C, Zhu X, Wang Y, Zhuo L, Lu Z, Lin X.
Cell Physiol Biochem. 2017;44(2):436-446. doi: 10.1159/000485009. Epub 2017 Nov 15.
- PMID:
- 29141243
16.
Ansari MY, Khan NM, Haqqi TM.
Biomed Pharmacother. 2017 Dec;96:198-207. doi: 10.1016/j.biopha.2017.09.140. Epub 2017 Oct 6.
- PMID:
- 28987943
17.
Yang F, Zhang L, Gao Z, Sun X, Yu M, Dong S, Wu J, Zhao Y, Xu C, Zhang W, Lu F.
Cell Physiol Biochem. 2017;43(3):1168-1187. doi: 10.1159/000481758. Epub 2017 Oct 5.
- PMID:
- 28977784
18.
Ling Y, Gong Q, Xiong X, Sun L, Zhao W, Zhu W, Lu Y.
Oncotarget. 2017 May 7;8(31):51066-51075. doi: 10.18632/oncotarget.17654. eCollection 2017 Aug 1.
- PMID:
- 28881630
19.
Li Q, Kang J, Xiong X, Liu Y, Cao W, Liu Y, Li Y.
Oncol Lett. 2017 Aug;14(2):2097-2102. doi: 10.3892/ol.2017.6394. Epub 2017 Jun 16.
- PMID:
- 28789437
20.
Song D, Ma J, Chen L, Guo C, Zhang Y, Chen T, Zhang S, Zhu Z, Tian L, Niu P.
Metallomics. 2017 Sep 20;9(9):1251-1259. doi: 10.1039/c7mt00085e.
- PMID:
- 28661534
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