What's New in Cytoskeleton-Organelle Interactions?

Duden, Rainer; Ho, Wai Chang; Allan, Viki; Kreis, Thomas E.

doi:10.1016/s0344-0338(11)80478-4

Cited by 9 publications

(1 citation statement)

References 26 publications

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“…The cytoskeleton is a cellular network of structural, signaling, and adaptor molecules that regulate most cellular functions such as migration, ligand recognition, signal activation and endocytosis/phagocytosis (12) . There have been reports that oxLDL affects the cytoskeletal functions of various cell types involved in atherosclerosis.…”

Section: Introductionmentioning

confidence: 99%

Oxidized LDL induces phosphorylation of non-muscle myosin IIA heavy chain in macrophages

Park

2015

BMB Reports

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Oxidized LDL (oxLDL) performs critical roles in atherosclerosis by inducing macrophage foam cell formation and promoting inflammation. There have been reports showing that oxLDL modulates macrophage cytoskeletal functions for oxLDL uptake and trapping, however, the precise mechanism has not been clearly elucidated. Our study examined the effect of oxLDL on non-muscle myosin heavy chain IIA (MHC-IIA) in macrophages. We demonstrated that oxLDL induces phosphorylation of MHC-IIA (Ser1917) in peritoneal macrophages from wild-type mice and THP-1, a human monocytic cell line, but not in macrophages deficient for CD36, a scavenger receptor for oxLDL. Protein kinase C (PKC) inhibitor-treated macrophages did not undergo the oxLDL-induced MHC-IIA phosphorylation. Our immunoprecipitation revealed that oxLDL increased physical association between PKC and MHC-IIA, supporting the role of PKC in this process. We conclude that oxLDL via CD36 induces PKC-mediated MHC-IIA (Ser1917) phosphorylation and this may affect oxLDL-induced functions of macrophages involved in atherosclerosis. [BMB Reports 2015; 48(1): 48-53]

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Section: Introductionmentioning

confidence: 99%

Oxidized LDL induces phosphorylation of non-muscle myosin IIA heavy chain in macrophages

Park

2015

BMB Reports

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Partitioning of cytoplasmic organelles during mitosis with special reference to the Golgi complex

Thyberg

Moskalewski²

1998

Microsc. Res. Tech.

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Microtubules with altered assembly kinetics have a decreased rate of kinesin‐based transport

Redenbach

Richburg

Boekelheide

1994

Cell Motil. Cytoskeleton

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Microtubules treated with the gamma-diketone 2,5-hexanedione (2,5-HD) have altered assembly behavior characterized by precocious nucleation and rapid elongation. By measuring the rate of microtubule transport, we have examined the potential functional significance of this 2,5-HD-induced microtubule modification. 2,5-HD-treated microtubules were transported at only 70% of the rate of control microtubules in a simple kinesin-based motility assay on glass coverslips using video and computer enhanced differential interference contrast microscopy. Since 2,5-HD is capable of forming both pyrrole adducts and crosslinks with tubulin, the contributions of pyrrole formation and crosslinking to slowed microtubule transport were determined. 3-Acetyl-2,5-hexanedione (AcHD), a pyrrole forming, non-crosslinking congener of 2,5-HD which does not alter microtubule assembly, did not produce slowed microtubule transport as occurs with 2,5-HD. However, glutaraldehyde, a pyrrole-independent crosslinking agent which alters microtubule assembly in the same way as 2,5-HD, slowed microtubule transport. These results indicate that a 2,5-HD-induced microtubule modification, possibly a crosslink-related conformational change, produces both an alteration in the kinetics of assembly and an alteration in the microtubule-motor interaction.

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What's New in Cytoskeleton-Organelle Interactions?

Cited by 9 publications

References 26 publications

Oxidized LDL induces phosphorylation of non-muscle myosin IIA heavy chain in macrophages

Oxidized LDL induces phosphorylation of non-muscle myosin IIA heavy chain in macrophages

Partitioning of cytoplasmic organelles during mitosis with special reference to the Golgi complex

Microtubules with altered assembly kinetics have a decreased rate of kinesin‐based transport

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