Interleukin-6 affects pacsin3, ephrinA4 expression and cytoskeletal proteins in differentiating primary skeletal myoblasts through transcriptional and post-transcriptional mechanisms

Milewska, Magdalena; Domoradzki, Tomasz; Majewska, Alicja; Błaszczyk, Maciej; Gajewska, Małgorzata; Hulanicka, Magdalena; Grzelkowska-Kowalczyk, Katarzyna

doi:10.1007/s00441-019-03133-4

Cited by 4 publications

(8 citation statements)

References 64 publications

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“…A role for PACSIN3 in muscle biology is further supported by studies in high fat‐diet induced skeletal muscle atrophy in mice 109 and work on primary rat myoblasts in vitro 110 . In high fat‐diet fed mice, the authors found elevated phosphorylation of serine residues of PACSIN3 in skeletal muscle.…”

Section: Pacsins In Muscle Biologymentioning

confidence: 91%

“…A role for PACSIN3 in muscle biology is further supported by studies in high fat‐diet induced skeletal muscle atrophy in mice 109 and work on primary rat myoblasts in vitro. 110 In high fat‐diet fed mice, the authors found elevated phosphorylation of serine residues of PACSIN3 in skeletal muscle. The skeletal muscles of these mice present signs of atrophy, inflammation and activation of the protein degradation pathway.…”

Section: Pacsins In Muscle Biologymentioning

confidence: 98%

“…The authors discussed the potential effect of the phosphorylation of PACSIN3 as a means to inhibit its activity in glucose transport, but further studies are necessary to establish whether the phosphorylation of PACSIN3 plays a role in muscle degradation. In the in vitro study, incubation of differentiating myoblasts with IL‐6, known to be expressed in injured muscles and suspected to promote the injury, leads to the downregulation of PACSIN3 at protein level 110 …”

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

“…In the in vitro study, incubation of differentiating myoblasts with IL-6, known to be expressed in injured muscles and suspected to promote the injury, leads to the downregulation of PACSIN3 at protein level. 110 Moreover, a collection of studies demonstrate that interaction of PACSIN3 with TRPV4 is necessary for the normal function of the channel. [111][112][113] Notably, TRPV4 has been found mutated in various forms of neuromuscular disorders and skeletal dysplasias.…”

Section: Heart and Skeletal Muscle Physiology In Adult Micementioning

confidence: 99%

“…In the in vitro study, incubation of differentiating myoblasts with IL‐6, known to be expressed in injured muscles and suspected to promote the injury, leads to the downregulation of PACSIN3 at protein level. 110 …”

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

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PACSIN proteins in vivo: Roles in development and physiology

Dumont

Lehtonen

2022

Acta Physiologica

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Protein kinase C and casein kinase substrate in neurons (PACSINs), or syndapins (synaptic dynamin‐associated proteins), are a family of proteins involved in the regulation of cell cytoskeleton, intracellular trafficking and signalling. Over the last twenty years, PACSINs have been mostly studied in the in vitro and ex vivo settings, and only in the last decade reports on their function in vivo have emerged. We first summarize the identification, structure and cellular functions of PACSINs, and then focus on the relevance of PACSINs in vivo. During development in various model organisms, PACSINs participate in diverse processes, such as neural crest cell development, gastrulation, laterality development and neuromuscular junction formation. In mouse, PACSIN2 regulates angiogenesis during retinal development and in human, PACSIN2 associates with monosomy and embryonic implantation. In adulthood, PACSIN1 has been extensively studied in the brain and shown to regulate neuromorphogenesis, receptor trafficking and synaptic plasticity. Several genetic studies suggest a role for PACSIN1 in the development of schizophrenia, which is also supported by the phenotype of mice depleted of PACSIN1. PACSIN2 plays an essential role in the maintenance of intestinal homeostasis and participates in kidney repair processes after injury. PACSIN3 is abundant in muscle tissue and necessary for caveolar biogenesis to create membrane reservoirs, thus controlling muscle function, and has been linked to certain genetic muscular disorders. The above examples illustrate the importance of PACSINs in diverse physiological or tissue repair processes in various organs, and associations to diseases when their functions are disturbed.

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Section: Pacsins In Muscle Biologymentioning

confidence: 91%

Section: Pacsins In Muscle Biologymentioning

confidence: 98%

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

Section: Heart and Skeletal Muscle Physiology In Adult Micementioning

confidence: 99%

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

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PACSIN proteins in vivo: Roles in development and physiology

Dumont

Lehtonen

2022

Acta Physiologica

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Interleukin-6 mimics insulin-dependent cellular distribution of some cytoskeletal proteins and Glut4 transporter without effect on glucose uptake in 3T3-L1 adipocytes

Błaszczyk

Gajewska

Dymowska

et al. 2022

Histochem Cell Biol

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Transplantation of Umbilical Cord-Derived Mesenchymal Stem Cells Attenuates Surgical Wound-Induced Blood-Brain Barrier Dysfunction in Mice

Yang

Ran

et al. 2023

Stem Cells International

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Blood-brain barrier (BBB) is the most important component of central nervous system (CNS) to keep toxins and pathogens from CNS. Although our studies demonstrated that using interleukin-6 antibodies (IL-6-AB) reversed the increased permeability of BBB, IL-6-AB is limited in their application that only could be used a few hours before surgery and seemed delayed the surgical wounds healing process, which urges us to find another more effective method. In this study, we employed the C57BL/6J female mice to investigate the potential effects of umbilical cord-derived mesenchymal stem cells (UC-MSCs) transplantation on BBB dysfunction induced by surgical wound. Compared to IL-6-AB, the transplantation of UC-MSCs more effectively decreased the BBB permeability after surgical wound evaluated by dextran tracer (immunofluorescence imaging and luorescence quantification). In addition, UC-MSCs can largely decrease the ratio of proinflammatory cytokine IL-6 to the anti-inflammatory cytokine IL-10 in both serum and brain tissue after surgical wound. Moreover, UC-MSCs successfully increased the levels of tight junction proteins (TJs) in BBB such as ZO-1, Occludin, and Claudin-5 and extremely decreased the level of matrix metalloproteinase-9 (MMP-9). Interestingly, UC-MSCs treatment also had positive effects on wound healing while protecting the BBB dysfunction induced by surgical wound compared to IL-6-AB treatment. These findings suggest that UC-MSCs transplantation is a highly efficient and promising approach on protecting the integrity of BBB which caused by peripheral traumatic injuries.

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Interleukin-6 affects pacsin3, ephrinA4 expression and cytoskeletal proteins in differentiating primary skeletal myoblasts through transcriptional and post-transcriptional mechanisms

Cited by 4 publications

References 64 publications

PACSIN proteins in vivo: Roles in development and physiology

PACSIN proteins in vivo: Roles in development and physiology

Interleukin-6 mimics insulin-dependent cellular distribution of some cytoskeletal proteins and Glut4 transporter without effect on glucose uptake in 3T3-L1 adipocytes

Transplantation of Umbilical Cord-Derived Mesenchymal Stem Cells Attenuates Surgical Wound-Induced Blood-Brain Barrier Dysfunction in Mice

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