Low lysophosphatidylcholine induces skeletal muscle myopathy that is aggravated by high‐fat diet feeding

Ferrara, Patrick J.; Verkerke, Anthony R.P.; Maschek, J. Alan; Shahtout, Justin L; Siripoksup, Piyarat; Eshima, Hiroaki; Johnson, Jordan M.; Petrocelli, Jonathan J; Mahmassani, Ziad; Green, Thomas D.; McClung, Joseph M.; Cox, James E.; Drummond, Micah J.; Funai, Katsuhiko

doi:10.1096/fj.202101104r

Cited by 21 publications

(19 citation statements)

References 42 publications

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“…Interestingly, previous studies have found that obesity leads to a reduction in muscle lysoPC 30 . Additionally, in skeletal muscle, LysoPC is mainly regulated by LPCAT3, which is acylated to produce PC, and consistent with this finding, lysoPC is reduced when skeletal muscle LPCAT3 is overexpressed 53 . Thus, we suggest that LPCAT3 may be closely associated with the development of skeletal muscle myopathy through the regulation of lysoPC expression.…”

Section: Role Of Lpcat3 In Different Diseasessupporting

confidence: 76%

Research progress in the role and mechanism of LPCAT3 in metabolic related diseases and cancer

Shao¹,

Qian²,

Lu³

et al. 2022

J. Cancer

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Lysophosphatidylcholine acyltransferases (LPCATs) are among the lysophopholipid acyltransferases (LPLATs) that specifically regulate the abundance of different phosphatidylcholine (PC) species in a variety of cell and tissue types, thereby playing an important role in lipid metabolism and homeostasis. Lysophosphatidylcholine acyltransferase 3 (LPCAT3, MBOAT5) is a member of the LPCAT family that primarily regulates the levels of arachidonic PC species. LPCAT3 is regulated by the liver X receptor, which plays an important role in lipoprotein production in the liver and small intestine. Increasing lines of research have demonstrated that LPCAT3 plays important roles in the occurrence and development of many diseases, such as atherosclerosis, intestinal tumors, and nonalcoholic steatohepatitis (NASH). The development of many diseases has been linked to the proinflammatory effects of LPCAT3. This review focuses on the current knowledge of LPCAT3, including its function and mechanism in different diseases. We aim to provide a comprehensive and in-depth understanding of LPCAT3 and to provide new ideas for the treatment of some diseases.

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Section: Role Of Lpcat3 In Different Diseasessupporting

confidence: 76%

Research progress in the role and mechanism of LPCAT3 in metabolic related diseases and cancer

Shao¹,

Qian²,

Lu³

et al. 2022

J. Cancer

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“…GPx4 primarily neutralizes LOOH but it also exhibits some activity towards other peroxides [19]. To confirm that the effects of GPx4 deletion to promote atrophy is specific to LOOH, we diminished the ability of cells to incorporate PUFAs into phospholipids by deleting lysophosphatidylcholine acyltransferase 3 (LPCAT3) [20–22]. LPCAT3 is an enzyme of Lands cycle that preferentially acylates lysophospholipids with PUFAs, and thus an essential component of ferroptosis [13].…”

Section: Resultsmentioning

confidence: 99%

“…16 To confirm that the effects of GPx4 deletion to promote atrophy is specific to LOOH, we diminished the ability of cells to incorporate polyunsaturated fatty acids (PUFAs) into phospholipids by deleting lysophosphatidylcholine acyltransferase 3 (LPCAT3). [17][18][19] LPCAT3 is an enzyme of Lands cycle that preferentially acylates lysophospholipids with PUFAs, and thus an essential component of ferroptosis 10 . Indeed, LPCAT3 KD rescued the increase in 4-HNE induced by GPx4 KD (Fig.…”

mentioning

confidence: 99%

Lipid hydroperoxides promote sarcopenia through carbonyl stress

Eshima

Siripoksup

Shahtout

et al. 2021

Preprint

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Reactive oxygen species (ROS) is a cardinal feature of skeletal muscle atrophy. However, ROS refers to a collection of radical molecules whose cellular signals are vast, and it is unclear which downstream consequences of ROS are responsible for the loss of muscle mass and strength.1,2 Here we show that lipid hydroperoxides (LOOH) are increased with age and disuse, and the accumulation of LOOH by suppression of glutathione peroxidase 4 (GPx4) is sufficient to augment muscle atrophy. Strikingly, genetic and pharmacologic suppression of muscle LOOH robustly prevented the reduction of both muscle mass and force-generating capacity. LOOH promoted atrophy in a lysosomal-dependent, proteasomal-independent manner, and the suppression of autophagic machinery was sufficient to prevent muscle atrophy and weakness. Indeed, the lysosome is essential for the amplification of LOOH induced by oxidative stress. Our findings provide novel insights for the role of LOOH in muscle atrophy including a therapeutic implication by pharmacologic suppression.

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“…Based on previous studies, we measured CSA of VMO at 5 mm below the upper pole of the patella, the upper pole of the patella, and 5 mm above the upper pole of the patella, in order to compare the change of the CSA of VMO of the same part before surgery and at follow-up. Studies had confirmed that the CSA of muscles was related to the maximum contractility of muscles [ 47 ]. The VMO was a very important dynamic stabilizing device for the inner side of the patella.…”

Section: Discussionmentioning

confidence: 99%

Change of the cross-sectional area of vastus medialis oblique in patients with recurrent patellar dislocation treated by tibial tubercle transfer combined with medial patellofemoral ligament reconstruction on axial CT

et al. 2022

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Purpose To investigate the change of the cross-sectional area (CSA) of vastus medialis oblique (VMO) in patients with recurrent patellar dislocation (RPD) treated by tibial tubercle transfer combined with medial patellofemoral ligament (MPFL) reconstruction by imaging methods, and to guide clinical treatment and rehabilitation. Methods From October 2015 to March 2022, 23 patients with RPD who underwent tibial tubercle transfer combined with MPFL reconstruction were retrospectively enrolled. All patients were assessed by CT in the supine position with the knee fully extended and the quadriceps relaxed. The CSA of VMO and the ratio of CSA of VMO to body weight (CSA/BW) were measured at the upper pole of the patella, 5 mm above the upper pole of the patella and 5 mm below the upper pole of patella. The differences of measured parameters were compared before surgery and at follow-up, including CSA of VMO and CSA/BW. Test level α = 0.05. Results The tibial tubercle-trochlear groove (TT-TG) distance was significantly reduced at follow-up compared with that before surgery (27.91 ± 1.95 mm vs 12.33 ± 1.07 mm, P < 0.001). The CSA of VMO was significantly increased at follow-up compared with that before surgery at 5 mm below the upper pole of the patella (473.06 ± 106.32 mm2 vs 562.97 ± 157.90 mm2, P < 0.001), at the upper pole of the patella (641.23 ± 188.45 mm2 vs 700.23 ± 177.55 mm2, P = 0.029), and at 5 mm above the upper pole of the patella (788.25 ± 238.62 mm2 vs 849.79 ± 180.84 mm2, P = 0.018). The CSA/BW was significantly increased at follow-up compared with that before surgery at 5 mm below the upper pole of the patella (7.83 ± 2.52 mm2/kg vs 9.22 ± 3.54 mm2/kg, P < 0.001), at the upper pole of the patella (10.48 ± 3.62 mm2/kg vs 11.42 ± 4.14 mm2/kg, P = 0.020), and at 5 mm above the upper pole of the patella (12.86 ± 4.65 mm2/kg vs 13.68 ± 3.86 mm2/kg, P = 0.017). Conclusion After tibial tubercle transfer combined with MPFL reconstruction, CSA of VMO increased in patients with RPD, which will help to enhance patellar stability and reduce recurrence.

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Low lysophosphatidylcholine induces skeletal muscle myopathy that is aggravated by high‐fat diet feeding

Cited by 21 publications

References 42 publications

Research progress in the role and mechanism of LPCAT3 in metabolic related diseases and cancer

Research progress in the role and mechanism of LPCAT3 in metabolic related diseases and cancer

Lipid hydroperoxides promote sarcopenia through carbonyl stress

Change of the cross-sectional area of vastus medialis oblique in patients with recurrent patellar dislocation treated by tibial tubercle transfer combined with medial patellofemoral ligament reconstruction on axial CT

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