The Experts below are selected from a list of 2616 Experts worldwide ranked by ideXlab platform
Hirotoshi Kamata - One of the best experts on this subject based on the ideXlab platform.
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kif5a transports collagen vesicles of myofibroblasts during Pleural Fibrosis
Scientific Reports, 2017Co-Authors: Reiko Ikebe, Ann Jeffers, Shuzi Owens, Julia Wang, Jake Boren, Hirotoshi Kamata, Tsuyoshi Sakai, Yoshikazu Tsukasaki, Takahiro SuzukiAbstract:Fibrosis involves the production of extracellular matrix proteins in tissues and is often preceded by injury or trauma. In Pleural Fibrosis excess collagen deposition results in Pleural thickening, increased stiffness and impaired lung function. Myofibroblasts are responsible for increased collagen deposition, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 (Col-1) containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy and the DUO-Link technique, we found that KIF5A colocalized with Col-1 containing vesicles. KIF5A knock-down significantly reduced Col-1 secretion and attenuated TGF-β induced increment in Col-1 localization at cell peripheries. Live cell imaging revealed that GFP-KIF5A and mCherry-Col-1 containing vesicles moved together. Kymography showed that these molecules continuously move with a mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion limited process. Moreover, KIF5A was notably upregulated along with Col-1 and α-smooth muscle actin in Pleural thickening in the carbon-black bleomycin mouse model. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.
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kif5a is responsible for collagen transport of myofibroblasts during Pleural Fibrosis
Biophysical Journal, 2017Co-Authors: Yoshikazu Tsukasaki, Reiko Ikebe, Ann Jeffers, Boren Jake, Shuzi Owens, Julia Wang, Hirotoshi Kamata, Masaaki Higashihara, Tsuyoshi Sakai, Steven IdellAbstract:Fibrosis is the production of extracellular matrix proteins in tissues and often proceeded by injuries. In Pleural Fibrosis excess collagen deposition occurs, which results in increased stiffness and thickening of pleura during tissue rearrangements. Myofibroblasts are responsible for oversecretion of collagen, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy (SIM) and DUO-Link technique, we found KIF5A notably colocalizes with collagen-1 containing vesicles. KIF5A knock-down (KD) by specific siRNA significantly reduced collagen-1 secretion but not plasminogen activator inhibitor 1 (PAI-1). KIF5A KD notably attenuated TGF-β induced increase in collagen-1 localization at cell peripheries. Live cell imaging with GFP-KIF5A and mCherry-collagen-1 showed that KIF5A and collagen-1 containing vesicles moved together. Kymograph showed that these molecules continuously move with mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion process. Moreover, KIF5A was notably upregulated along with collagen-1 and α-smooth muscle actin (α-SMA) (MesoMT marker) in thickening pleura of carbon-black bleomycin mouse model. All the results support that KIF5A is responsible for collagen transportation and secretion from HPMCs.
Yoshikazu Tsukasaki - One of the best experts on this subject based on the ideXlab platform.
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kif5a transports collagen vesicles of myofibroblasts during Pleural Fibrosis
Scientific Reports, 2017Co-Authors: Reiko Ikebe, Ann Jeffers, Shuzi Owens, Julia Wang, Jake Boren, Hirotoshi Kamata, Tsuyoshi Sakai, Yoshikazu Tsukasaki, Takahiro SuzukiAbstract:Fibrosis involves the production of extracellular matrix proteins in tissues and is often preceded by injury or trauma. In Pleural Fibrosis excess collagen deposition results in Pleural thickening, increased stiffness and impaired lung function. Myofibroblasts are responsible for increased collagen deposition, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 (Col-1) containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy and the DUO-Link technique, we found that KIF5A colocalized with Col-1 containing vesicles. KIF5A knock-down significantly reduced Col-1 secretion and attenuated TGF-β induced increment in Col-1 localization at cell peripheries. Live cell imaging revealed that GFP-KIF5A and mCherry-Col-1 containing vesicles moved together. Kymography showed that these molecules continuously move with a mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion limited process. Moreover, KIF5A was notably upregulated along with Col-1 and α-smooth muscle actin in Pleural thickening in the carbon-black bleomycin mouse model. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.
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kif5a is responsible for collagen transport of myofibroblasts during Pleural Fibrosis
Biophysical Journal, 2017Co-Authors: Yoshikazu Tsukasaki, Reiko Ikebe, Ann Jeffers, Boren Jake, Shuzi Owens, Julia Wang, Hirotoshi Kamata, Masaaki Higashihara, Tsuyoshi Sakai, Steven IdellAbstract:Fibrosis is the production of extracellular matrix proteins in tissues and often proceeded by injuries. In Pleural Fibrosis excess collagen deposition occurs, which results in increased stiffness and thickening of pleura during tissue rearrangements. Myofibroblasts are responsible for oversecretion of collagen, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy (SIM) and DUO-Link technique, we found KIF5A notably colocalizes with collagen-1 containing vesicles. KIF5A knock-down (KD) by specific siRNA significantly reduced collagen-1 secretion but not plasminogen activator inhibitor 1 (PAI-1). KIF5A KD notably attenuated TGF-β induced increase in collagen-1 localization at cell peripheries. Live cell imaging with GFP-KIF5A and mCherry-collagen-1 showed that KIF5A and collagen-1 containing vesicles moved together. Kymograph showed that these molecules continuously move with mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion process. Moreover, KIF5A was notably upregulated along with collagen-1 and α-smooth muscle actin (α-SMA) (MesoMT marker) in thickening pleura of carbon-black bleomycin mouse model. All the results support that KIF5A is responsible for collagen transportation and secretion from HPMCs.
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Mesomesenchymal transition of Pleural mesothelial cells is PI3K and NF-κB dependent.
American Journal of Physiology-Lung Cellular and Molecular Physiology, 2015Co-Authors: Shuzi Owens, Ann Jeffers, Jake Boren, Steven Idell, Yoshikazu Tsukasaki, Kathleen Koenig, Mitsuo Ikebe, Torry A. TuckerAbstract:Pleural organization follows acute injury and is characterized by Pleural Fibrosis, which may involve the visceral and parietal Pleural surfaces. This process affects patients with complicated parapneumonic Pleural effusions, empyema, and other Pleural diseases prone to Pleural Fibrosis and loculation. Pleural mesothelial cells (PMCs) undergo a process called mesothelial mesenchymal transition (MesoMT), by which PMCs acquire a profibrotic phenotype characterized by cellular enlargement and elongation, increased expression of α-smooth muscle actin (α-SMA), and matrix proteins including collagen-1. Although MesoMT contributes to Pleural Fibrosis and lung restriction in mice with carbon black/bleomycin-induced Pleural injury and procoagulants and fibrinolytic proteases strongly induce MesoMT in vitro, the mechanism by which this transition occurs remains unclear. We found that thrombin and plasmin potently induce MesoMT in vitro as does TGF-β. Furthermore, these mediators of MesoMT activate phosphatidylinositol-3-kinase (PI3K)/Akt and NF-κB signaling pathways. Inhibition of PI3K/Akt signaling prevented TGF-β-, thrombin-, and plasmin-mediated induction of the MesoMT phenotype exhibited by primary human PMCs. Similar effects were demonstrated through blockade of the NF-κB signaling cascade using two distinctly different NF-κB inhibitors, SN50 and Bay-11 7085. Conversely, expression of constitutively active Akt-induced mesenchymal transition in human PMCs whereas the process was blocked by PX866 and AKT8. Furthermore, thrombin-mediated MesoMT is dependent on PAR-1 expression, which is linked to PI3K/Akt signaling downstream. These are the first studies to demonstrate that PI3K/Akt and/or NF-κB signaling is critical for induction of MesoMT.
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Mesomesenchymal transition of Pleural mesothelial cells is PI3K and NF-κB dependent.
American Journal of Physiology-lung Cellular and Molecular Physiology, 2015Co-Authors: Shuzi Owens, Ann Jeffers, Jake Boren, Steven Idell, Yoshikazu Tsukasaki, Kathleen Koenig, Mitsuo Ikebe, Torry A. TuckerAbstract:Pleural organization follows acute injury and is characterized by Pleural Fibrosis, which may involve the visceral and parietal Pleural surfaces. This process affects patients with complicated para...
Takahiro Suzuki - One of the best experts on this subject based on the ideXlab platform.
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kif5a transports collagen vesicles of myofibroblasts during Pleural Fibrosis
Scientific Reports, 2017Co-Authors: Reiko Ikebe, Ann Jeffers, Shuzi Owens, Julia Wang, Jake Boren, Hirotoshi Kamata, Tsuyoshi Sakai, Yoshikazu Tsukasaki, Takahiro SuzukiAbstract:Fibrosis involves the production of extracellular matrix proteins in tissues and is often preceded by injury or trauma. In Pleural Fibrosis excess collagen deposition results in Pleural thickening, increased stiffness and impaired lung function. Myofibroblasts are responsible for increased collagen deposition, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 (Col-1) containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy and the DUO-Link technique, we found that KIF5A colocalized with Col-1 containing vesicles. KIF5A knock-down significantly reduced Col-1 secretion and attenuated TGF-β induced increment in Col-1 localization at cell peripheries. Live cell imaging revealed that GFP-KIF5A and mCherry-Col-1 containing vesicles moved together. Kymography showed that these molecules continuously move with a mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion limited process. Moreover, KIF5A was notably upregulated along with Col-1 and α-smooth muscle actin in Pleural thickening in the carbon-black bleomycin mouse model. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.
Tsuyoshi Sakai - One of the best experts on this subject based on the ideXlab platform.
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kif5a transports collagen vesicles of myofibroblasts during Pleural Fibrosis
Scientific Reports, 2017Co-Authors: Reiko Ikebe, Ann Jeffers, Shuzi Owens, Julia Wang, Jake Boren, Hirotoshi Kamata, Tsuyoshi Sakai, Yoshikazu Tsukasaki, Takahiro SuzukiAbstract:Fibrosis involves the production of extracellular matrix proteins in tissues and is often preceded by injury or trauma. In Pleural Fibrosis excess collagen deposition results in Pleural thickening, increased stiffness and impaired lung function. Myofibroblasts are responsible for increased collagen deposition, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 (Col-1) containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy and the DUO-Link technique, we found that KIF5A colocalized with Col-1 containing vesicles. KIF5A knock-down significantly reduced Col-1 secretion and attenuated TGF-β induced increment in Col-1 localization at cell peripheries. Live cell imaging revealed that GFP-KIF5A and mCherry-Col-1 containing vesicles moved together. Kymography showed that these molecules continuously move with a mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion limited process. Moreover, KIF5A was notably upregulated along with Col-1 and α-smooth muscle actin in Pleural thickening in the carbon-black bleomycin mouse model. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.
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kif5a is responsible for collagen transport of myofibroblasts during Pleural Fibrosis
Biophysical Journal, 2017Co-Authors: Yoshikazu Tsukasaki, Reiko Ikebe, Ann Jeffers, Boren Jake, Shuzi Owens, Julia Wang, Hirotoshi Kamata, Masaaki Higashihara, Tsuyoshi Sakai, Steven IdellAbstract:Fibrosis is the production of extracellular matrix proteins in tissues and often proceeded by injuries. In Pleural Fibrosis excess collagen deposition occurs, which results in increased stiffness and thickening of pleura during tissue rearrangements. Myofibroblasts are responsible for oversecretion of collagen, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy (SIM) and DUO-Link technique, we found KIF5A notably colocalizes with collagen-1 containing vesicles. KIF5A knock-down (KD) by specific siRNA significantly reduced collagen-1 secretion but not plasminogen activator inhibitor 1 (PAI-1). KIF5A KD notably attenuated TGF-β induced increase in collagen-1 localization at cell peripheries. Live cell imaging with GFP-KIF5A and mCherry-collagen-1 showed that KIF5A and collagen-1 containing vesicles moved together. Kymograph showed that these molecules continuously move with mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion process. Moreover, KIF5A was notably upregulated along with collagen-1 and α-smooth muscle actin (α-SMA) (MesoMT marker) in thickening pleura of carbon-black bleomycin mouse model. All the results support that KIF5A is responsible for collagen transportation and secretion from HPMCs.
Julia Wang - One of the best experts on this subject based on the ideXlab platform.
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kif5a transports collagen vesicles of myofibroblasts during Pleural Fibrosis
Scientific Reports, 2017Co-Authors: Reiko Ikebe, Ann Jeffers, Shuzi Owens, Julia Wang, Jake Boren, Hirotoshi Kamata, Tsuyoshi Sakai, Yoshikazu Tsukasaki, Takahiro SuzukiAbstract:Fibrosis involves the production of extracellular matrix proteins in tissues and is often preceded by injury or trauma. In Pleural Fibrosis excess collagen deposition results in Pleural thickening, increased stiffness and impaired lung function. Myofibroblasts are responsible for increased collagen deposition, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 (Col-1) containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy and the DUO-Link technique, we found that KIF5A colocalized with Col-1 containing vesicles. KIF5A knock-down significantly reduced Col-1 secretion and attenuated TGF-β induced increment in Col-1 localization at cell peripheries. Live cell imaging revealed that GFP-KIF5A and mCherry-Col-1 containing vesicles moved together. Kymography showed that these molecules continuously move with a mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion limited process. Moreover, KIF5A was notably upregulated along with Col-1 and α-smooth muscle actin in Pleural thickening in the carbon-black bleomycin mouse model. These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.
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kif5a is responsible for collagen transport of myofibroblasts during Pleural Fibrosis
Biophysical Journal, 2017Co-Authors: Yoshikazu Tsukasaki, Reiko Ikebe, Ann Jeffers, Boren Jake, Shuzi Owens, Julia Wang, Hirotoshi Kamata, Masaaki Higashihara, Tsuyoshi Sakai, Steven IdellAbstract:Fibrosis is the production of extracellular matrix proteins in tissues and often proceeded by injuries. In Pleural Fibrosis excess collagen deposition occurs, which results in increased stiffness and thickening of pleura during tissue rearrangements. Myofibroblasts are responsible for oversecretion of collagen, however the molecular mechanism of transportation of procollagen containing vesicles for secretion is unknown. Here, we studied the role of kinesin on collagen-1 containing vesicle transportation in human Pleural mesothelial cells (HPMCs). Among a number of cargo transporting kinesins, KIF5A was notably upregulated during TGF-β induced mesothelial-mesenchymal transition (MesoMT). Using superresolution structured illumination microscopy (SIM) and DUO-Link technique, we found KIF5A notably colocalizes with collagen-1 containing vesicles. KIF5A knock-down (KD) by specific siRNA significantly reduced collagen-1 secretion but not plasminogen activator inhibitor 1 (PAI-1). KIF5A KD notably attenuated TGF-β induced increase in collagen-1 localization at cell peripheries. Live cell imaging with GFP-KIF5A and mCherry-collagen-1 showed that KIF5A and collagen-1 containing vesicles moved together. Kymograph showed that these molecules continuously move with mean velocity of 0.56 μm/sec, suggesting that the movement is directional but not diffusion process. Moreover, KIF5A was notably upregulated along with collagen-1 and α-smooth muscle actin (α-SMA) (MesoMT marker) in thickening pleura of carbon-black bleomycin mouse model. All the results support that KIF5A is responsible for collagen transportation and secretion from HPMCs.