Hypergravity-induced enrichment of β1 integrin on the cell membranes of osteoblast-like cells via caveolae-dependent endocytosis

Zhou, Shuai; Zhang, Yan; Zhuang, Fengyuan; Yang, Chun

doi:10.1016/j.bbrc.2015.06.037

Cited by 14 publications

(11 citation statements)

References 29 publications

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“…It is important that only those integrin–RGD complexes were found to be involved in supporting growth-factor-induced cell-cycle progression. , For screening peptides for the potential to stimulate or inhibit osteoblast proliferation, the active sites of integrins against RGD were set as the binding site for peptides from P2. Integrin β1 plays a crucial role in that peptide RVYFFKGKQYWE promotes the response of osteoblast proliferation. − Integrin α5β1 stimulates cellular processes that promote osteoblast adhesion, proliferation, and differentiation , whereas the peptides that disturb integrin αvβ3, which suppresses cytoskeletal organizers in osteoclasts, thereby inhibit osteoclast proliferation. , As a result, RGD may play a critical role in integrin α5β1 or αvβ3 interaction with the extracellular matrix. Peptides with the potential activity of RGD are considered indicators for promoting bone formation or inhibiting osteoclast proliferation.…”

Section: Resultsmentioning

confidence: 99%

Isolation and Characterization of Peptides from Mytilus edulis with Osteogenic Activity in Mouse MC3T3-E1 Preosteoblast Cells

Chen

Wang

et al. 2019

J. Agric. Food Chem.

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Seafood provides a range of health benefits because of its high protein levels. In this study, a novel peptide, YPRKDETGAERT, was identified from NHA-2 of Mytilus edulis by capillary-electrophoresis electrospray ionization− quadrupole−time of flight (CESI-Q-TOF). Peptide YPRKDETGAERT showed the highest affinity among all the peptides, with -CDOCKER energy values of 204.482 kcal/mol on one integrin (PDB: 3VI4) and 210.16 kcal/mol on another integrin (PDB: 1L5G). The secondary mass spectrogram at the m/z of peptide YPRKDETGAERT was 1422.53 Da, which was determined by CESI-Q-TOF. Peptide YPRKDETGAERT induced an increase of 28.27 ± 3.66% in mouse-MC3T3-E1-preosteoblast-cell growth. The alkaline-phosphatase activity of peptide YPRKDETGAERT was 2.79 ± 0.07 mU, which was an increase of 21.25% compared with that of the control. These results provide theoretical and practical insights for the preparation and application of osteogenic peptides in the functional-foods industry.

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Section: Resultsmentioning

confidence: 99%

Isolation and Characterization of Peptides from Mytilus edulis with Osteogenic Activity in Mouse MC3T3-E1 Preosteoblast Cells

Chen

Wang

et al. 2019

J. Agric. Food Chem.

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“…Since the cytosol and intracellular micro-organelles such as the nucleus, mitochondria, the cytoskeletons including actin fibers, intermediate filaments, and microtubules have different densities, changes in their relative position could result from altered gravity. Several reports have shown that altered gravity exerts various effects on mammalian cell models[ 6 – 9 ]. Generally, it is known that microgravity strongly suppresses bone mass after a long period of exposure[ 10 ].…”

Section: Introductionmentioning

confidence: 99%

Hypergravity down-regulates c-fos gene expression via ROCK/Rho-GTP and the PI3K signaling pathway in murine ATDC5 chondroprogenitor cells

Kim¹,

Montagne²,

Nemoto³

et al. 2017

PLoS ONE

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Chondrocytes are known to be physiologically loaded with diverse physical factors such as compressive stress, shear stress and hydrostatic pressure. Although the effects of those mechanical stimuli onto various cell models have been widely studied, those of hypergravity have not yet been revealed clearly. Hereby, we hypothesized that the hypergravity affects relative positions of intracellular elements including nucleus and cytoskeletons due to their density differences, triggering mechanotransduction in the cell. The aim of this study was to investigate the effect of hypergravity on c-fos expression in the murine ATDC5 chondroprogenitor cells, as c-fos is a well known key regulator of cell proliferation and differentiation, including in chondrocytes. We first found that hypergravity down-regulated c-fos expression transiently via ROCK/Rho-GTP and PI3K signaling, and the down-regulation was suppressed by inhibition of actin polymerization.

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“…We reported that EGF-F9 treatment decreased focal adhesion at the filopodia and inhibited adhesion to extracellular matrix proteins (Kitano et al, 2015). Furthermore, it has been reported that caveolin-dependent endocytosis is associated with the levels of integrin b1 at the cell surface (Zhou et al, 2015). Furthermore, it is suggested that integrin and paxilin are incorporated into cells by endocytosis, along with the complex of PS, lipid rafts and caveolae.…”

Section: Discussionmentioning

confidence: 91%

“…Numerous studies are currently examining the role of integrin in endocytosis. Furthermore, it has been reported that caveolin-dependent endocytosis is associated with the levels of integrin b1 at the cell surface (Zhou et al, 2015). Thus, it is thought that the complex of PS, lipid rafts and caveolae is closely related to cell migration.…”

Section: Discussionmentioning

confidence: 99%

EGF domain of coagulation factor IX is conducive to exposure of phosphatidylserine

Hidai

Fujiwara

Kokubun

et al. 2017

Cell Biology International

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Lipid rafts are an initiation site for many different signals. Recently, we reported that an EGF domain in activated coagulation factor IX (EGF-F9) increases lipid raft formation and accelerates cell migration. However, the detailed mechanism is not well understood. This study aimed to evaluate the effects of EGF-F9 on the cell membrane. A431 cells (derived from human squamous cell carcinoma) were treated with recombinant EGF-F9. Cells were immunocytochemically stained with probes for lipid rafts or phosphatidylserine (PS). After 3 min of treatment with EGF-F9, cholera toxin subunit B (CTxB) binding domains emerged at the adhesive tips of filopodia. Subsequently, CTxB staining was observed on the filopodial shaft. Finally, large clusters of CTxB domains were observed at the edge of cell bodies. Markers for lipid rafts, such as caveolin-1 and a GPI anchored protein, co-localized with CTxB. Staining with annexin V and XII revealed that PS was exposed at the tips of filopodia, translocated on filopodial shafts, and co-localized with CTxB at the rafts. Immunocytochemistry showed that scramblase-1 protein was present at the filopodial tips. Our data indicates that EGF-F9 accelerates PS exposure around the filopodial adhesion complex and induces clustering of lipid rafts in the cell body. PS exposure is thought to occur on cells undergoing apoptosis. Further study of the function of the EGF-F9 motif in mediating signal transduction is necessary because it is shared by a number of proteins.

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Hypergravity-induced enrichment of β1 integrin on the cell membranes of osteoblast-like cells via caveolae-dependent endocytosis

Cited by 14 publications

References 29 publications

Isolation and Characterization of Peptides from Mytilus edulis with Osteogenic Activity in Mouse MC3T3-E1 Preosteoblast Cells

Isolation and Characterization of Peptides from Mytilus edulis with Osteogenic Activity in Mouse MC3T3-E1 Preosteoblast Cells

Hypergravity down-regulates c-fos gene expression via ROCK/Rho-GTP and the PI3K signaling pathway in murine ATDC5 chondroprogenitor cells

EGF domain of coagulation factor IX is conducive to exposure of phosphatidylserine

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