Cofilin-Induced Changes in F-Actin Detected via Cross-Linking with Benzophenone-4-maleimide

Chen, Christine K.; Benchaar, Sabrina A.; Phan, Mai; Grintsevich, Elena E.; Loo, Rachel R. Ogorzalek; Loo, Joseph A.; Reisler, Emil

doi:10.1021/bi400715z

Cited by 4 publications

(3 citation statements)

References 39 publications

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“…"non-severing"). However, a correlation between filament dynamics and thermally driven fragmentation has also been observed (31,49,50,58), suggesting that filament mechanics and the structural dynamics at boundaries can potentially play a role, even in the absence of external load. An attractive model (53) implicates allosteric propagation of cofilin-linked conformational changes (47,55,59) to bare, undecorated segments where local, stabilizing cofilin-actin interactions are absent, thus leading to fragmentation within the bare side of boundaries.…”

Section: Filament Fragmentationmentioning

confidence: 99%

Actin Mechanics and Fragmentation

Cruz

Gardel

2015

Journal of Biological Chemistry

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Cell physiological processes require the regulation and coordination of both mechanical and dynamical properties of the actin cytoskeleton. Here we review recent advances in understanding the mechanical properties and stability of actin filaments and how these properties are manifested at larger (network) length scales. We discuss how forces can influence local biochemical interactions, resulting in the formation of mechanically sensitive dynamic steady states. Understanding the regulation of such force-activated chemistries and dynamic steady states reflects an important challenge for future work that will provide valuable insights as to how the actin cytoskeleton engenders mechanoresponsiveness of living cells.

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Section: Filament Fragmentationmentioning

confidence: 99%

Actin Mechanics and Fragmentation

Cruz

Gardel

2015

Journal of Biological Chemistry

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“…[ 7 , 8 ] Cofilin can change the structure of F-actin filaments and promote the circulation of F-actin filaments. [ 9 , 10 ] This experiment simulates ischemia reperfusion injury of transplanted organ by establishing hepatocytes in vitro hypoxia/reoxygenation (H/R) injury model. Detecting the gene transcription and protein expression of HSP27 and Cofilin, observing the ultrastructure changes by electron microscope, and observing the content change of F-actin through confocal laser microscope, we are to investigate the mechanism of the injury of F-actin induced by ischemia reperfusion from the cellular and molecular levels.…”

Section: Introductionmentioning

confidence: 99%

Effect of HSP27 and Cofilin in the injury of hypoxia/reoxygenation on hepatocyte membrane F-actin microfilaments

Zhang

Wang²,

Ji³

et al. 2017

Medicine

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Hypoxia–reoxygenation (H/R) injury hepatocyte models were established to simulate the ischemia/reperfusion injury of transplanted organ. Through the study of the molecular mechanism of H/R on the F-actin damage of the liver cytomembrane, the mechanism of F-actin damage induced by ischemia and reperfusion was studied from the level of cell and molecule.The hypoxic environment of cells in vitro was simulated by chemical hypoxia agent CoCl2. Liver cells were detected by MTT, H/R group was subdivided into 3 subgroups: H/R 2, 4, and 6 h. Changes of cell shape and the growth state, apoptosis, ultrastructural changes, and the changes in F-actin microfilament content were observed. Heat shock protein 27 (HSP27), Cofilin, and F-actin gene and protein levels were determined by real-time polymerase chain reaction and western blot assay, respectively.Cells showed circular adherence growth under normal circumstances, while the spindle cells and shedding cells were significantly increased in H/R groups. Apoptosis cells in H/R group were increased significantly with the extension of hypoxia time. The number of endoplasmic reticulum was decreased significantly in the H/R group, the mitochondrion hydropic was degenerated and the glycogen was disappeared. The F-actin fibers in the H/R group were disordered, the morphology of the fibers was obviously decreased, and the fluorescence staining decreased obviously (P < .05). The transcription and expression levels of HSP27, Cofilin, and F-actin were significantly lower than those in the control group (P < .05).These results demonstrate that H/R can affect the correct assembly of F-actin microfilaments and weakens the normal cycle of F-actin microfilaments through inhibiting the protein expression and gene transcription of HSP27 and Cofilin in hepatocytes, thereby changing the skeleton of F-actin microfilaments.

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“…It plays a key role in actin dynamics by promoting the disassembly and assembly of actin filaments [13] . HSP27 is a member of a small HSP family that is constitutively expressed in cells [14] .…”

Section: Introductionmentioning

confidence: 99%

Hepatic artery bridging lessens temporary ischemic injury to bile canaliculi

Wang

Liu

Wang

et al. 2015

WJG

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Author contributions: Li YM conceived the research and critically reviewed and revised the manuscript; Wang JZ and Liu Y collected and tested the specimens, and performed data analysis; all authors participated in the operations; Wang JZ drafted the manuscript; and Li YM approved the final version of the manuscript.Supported by National Natural Science Foundation of China, No. 81170454.Institutional review board statement: The study was reviewed and approved by the Second Affiliated Hospital, Xi'an Jiaotong University School of Medicine Institutional Review Board.Institutional animal care and use committee statement: All procedures involving animals were reviewed and approved by the Institutional Animal Care and Use Committee of the Xi'an Jiaotong University (IACUC protocol number: XJTULAC20120026).Conflict-of-interest statement: All authors declare that there are no conflicting interests (including but not limited to commercial, personal, political, intellectual, or religious interests) related to the work. Abstract AIM: To study whether transfer of blood between the right gastroepiploic artery and gastroduodenal artery could lessens the damage to bile canaliculi. METHODS:Forty male Bama miniature pigs were divided into four groups as follows: a control group, two hepatic artery ischemia groups (1 h and 2 h), and a hepatic artery bridging group. The hemodynamics of the hepatic artery in the hepatic artery bridging group was measured using color Doppler ultrasound. Morphological changes in the bile canaliculus were observed by transmission electron microscopy. Cofilin, heat shock protein 27 and F-actin expression was detected by immunohistochemistry, Western blot, and real-time polymerase chain reaction. Terminal deoxynucleotidyl transferase-mediated nick end-labeling method was used to evaluate liver injury. RESULTS:The hemodynamics was not changed in the hepatic artery bridging group. The microvilli in the bile canaliculus were impaired in the two hepatic artery ischemia groups. The down-regulation of cofilin and F-actin and up-regulation of heat shock protein 27 were observed in the two hepatic artery ischemia groups, while there were no significant differences between the Basic Study ORIGINAL ARTICLEcontrol group and hepatic artery bridging group. CONCLUSION:Hepatic artery ischemia aggravates damage to bile canaliculi, and this damage can be diminished by a hepatic artery bridging duct.

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Cofilin-Induced Changes in F-Actin Detected via Cross-Linking with Benzophenone-4-maleimide

Cited by 4 publications

References 39 publications

Actin Mechanics and Fragmentation

Actin Mechanics and Fragmentation

Effect of HSP27 and Cofilin in the injury of hypoxia/reoxygenation on hepatocyte membrane F-actin microfilaments

Hepatic artery bridging lessens temporary ischemic injury to bile canaliculi

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