scholarly journals Groundnut (Apios americana Medik) Extract Enhances the Osteoblast Differentiation of MC3T3-E1 Cells

2021 ◽  
Vol 16 (4) ◽  
pp. 1934578X2110105
Author(s):  
Masanori Horie ◽  
Sakiko Sugino ◽  
Atsumi Tada ◽  
Kazuhiro Nara
Keyword(s):  
Osteoblast Differentiation ◽  
Type I Collagen ◽  
Type I ◽  
Methanol Fraction ◽  
Aqueous Fraction ◽  
Collagen Expression ◽  
Alp Activity ◽  
Apios Americana ◽  
Differentiation Medium ◽  
Cells Cultured

The effects of groundnut ( Apios americana Medik) extract on osteoblast differentiation were examined using MC3T3-E1 cells. MC3T3-E1 cells were treated with the crude extract along with other differentiating reagents. The alkaline phosphatase (ALP) activity of cells cultured in a differentiation medium supplemented with 0.01% crude groundnut extract was 1.5‐1.6 times higher than that of cells cultured in a differentiation medium without the extract. Crude groundnut extract was further separated into aqueous and methanol fractions. The methanol fraction enhanced ALP activity, osteocalcin, integrin-binding sialoprotein, and type I collagen expression, and calcium mineralization. Conversely, the aqueous fraction did not show such effects. Groundnut extract may enhance osteoblast differentiation, and this effect is likely conferred by water insoluble substance(s).

Intrinsic mechanical properties of the extracellular matrix affect the behavior of pre-osteoblastic MC3T3-E1 cells

2006 ◽  
Vol 290 (6) ◽  
pp. C1640-C1650 ◽  
Author(s):  
Chirag B. Khatiwala ◽  
Shelly R. Peyton ◽  
Andrew J. Putnam
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Focal Adhesions ◽  
Microscopic Analysis ◽  
Maximal Activity ◽  
Type I ◽  
Cell Functions ◽  
Collagen Density ◽  
Cells Cultured ◽  
In Cells

Mechanical cues present in the ECM have been hypothesized to provide instructive signals that dictate cell behavior. We probed this hypothesis in osteoblastic cells by culturing MC3T3-E1 cells on the surface of type I collagen-modified hydrogels with tunable mechanical properties and assessed their proliferation, migration, and differentiation. On gels functionalized with a low type I collagen density, MC3T3-E1 cells cultured on polystyrene proliferated twice as fast as those cultured on the softest substrate. Quantitative time-lapse video microscopic analysis revealed random motility speeds were significantly retarded on the softest substrate (0.25 ± 0.01 μm/min), in contrast to maximum speeds on polystyrene substrates (0.42 ± 0.04 μm/min). On gels functionalized with a high type I collagen density, migration speed exhibited a biphasic dependence on ECM compliance, with maximum speeds (0.34 ± 0.02 μm/min) observed on gels of intermediate stiffness, whereas minimum speeds (0.24 ± 0.03 μm/min) occurred on both the softest and most rigid (i.e., polystyrene) substrates. Immature focal contacts and a poorly organized actin cytoskeleton were observed in cells cultured on the softest substrates, whereas those on more rigid substrates assembled mature focal adhesions and robust actin stress fibers. In parallel, focal adhesion kinase (FAK) activity (assessed by detecting pY397-FAK) was influenced by compliance, with maximal activity occurring in cells cultured on polystyrene. Finally, mineral deposition by the MC3T3-E1 cells was also affected by ECM compliance, leading to the conclusion that altering ECM mechanical properties may influence a variety of MC3T3-E1 cell functions, and perhaps ultimately, their differentiated phenotype.

Type VI collagen expression is upregulated in the early events of chondrocyte differentiation

Development ◽  
1993 ◽  
Vol 117 (1) ◽  
pp. 245-251
Author(s):  
R. Quarto ◽  
B. Dozin ◽  
P. Bonaldo ◽  
R. Cancedda ◽  
A. Colombatti
Keyword(s):  
Suspension Culture ◽  
Type I Collagen ◽  
Type Ii Collagen ◽  
Type I ◽  
Type Ii ◽  
Type Vi Collagen ◽  
Full Spectrum ◽  
Collagen Expression ◽  
Hypertrophic Chondrocyte

Dedifferentiated chondrocytes cultured adherent to the substratum proliferate and synthesize large amounts of type I collagen but when transferred to suspension culture they decrease proliferation, resume the chondrogenic phenotype and the synthesis of type II collagen, and continue their maturation to hypertrophic chondrocyte (Castagnola et al., 1986, J. Cell Biol. 102, 2310–2317). In this report, we describe the developmentally regulated expression of type VI collagen in vitro in differentiating avian chondrocytes. Type VI collagen mRNA is barely detectable in dedifferentiated chondrocytes as long as the attachment to the substratum is maintained, but increases very rapidly upon passage of the cells into suspension culture reaching a peak after 48 hours and declining after 5–6 days of suspension culture. The first evidence of a rise in the mRNA steady-state levels is obtained already at 6 hours for the alpha 3(VI) chain. Immunoprecipitation of metabolically labeled cells with type VI collagen antibodies reveals that the early mRNA rise is paralleled by an increased secretion of type VI collagen in cell media. Induction of type VI collagen is not the consequence of trypsin treatment of dedifferentiated cells since exposure to the actin-disrupting drug cytochalasin or detachment of the cells by mechanical procedures has similar effects. In 13-day-old chicken embryo tibiae, where the full spectrum of the chondrogenic differentiation process is represented, expression of type VI collagen is restricted to the articular cartilage where chondrocytes developmental stage is comparable to stage I (high levels of type II collagen expression).(ABSTRACT TRUNCATED AT 250 WORDS)

Tissue inhibitor of metalloproteinases (TIMP) regulates extracellular type I collagen degradation by chondrocytes and endothelial cells

1987 ◽  
Vol 87 (2) ◽  
pp. 357-362
Author(s):  
J. Gavrilovic ◽  
R.M. Hembry ◽  
J.J. Reynolds ◽  
G. Murphy
Keyword(s):  
Endothelial Cells ◽  
Type I Collagen ◽  
Model System ◽  
Collagen Degradation ◽  
Type I ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Regulatory Factor ◽  
Tissue Inhibitor ◽  
Cells Cultured

A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.

Smad4-dependent regulation of type I collagen expression in the muscle of grass carp fed with faba bean

Gene ◽  
2019 ◽  
Vol 685 ◽  
pp. 32-41 ◽  
Author(s):  
Er-meng Yu ◽  
Ling-ling Ma ◽  
Hong Ji ◽  
Zhi-fei Li ◽  
Guang-jun Wang ◽  
...  
Keyword(s):  
Faba Bean ◽  
Grass Carp ◽  
Type I Collagen ◽  
Type I ◽  
Collagen Expression

scholarly journals Effects of different aperture-sized type I collagen/silk fibroin scaffolds on the proliferation and differentiation of human dental pulp cells

2021 ◽  
Vol 8 (4) ◽  
Author(s):  
Shihui Jiang ◽  
Zhaoxia Yu ◽  
Lanrui Zhang ◽  
Guanhua Wang ◽  
Xiaohua Dai ◽  
...  
Keyword(s):  
Silk Fibroin ◽  
Dental Pulp ◽  
Type I Collagen ◽  
Type I ◽  
Dental Pulp Cells ◽  
Human Dental Pulp Cells ◽  
Alp Activity ◽  
Proliferation And Differentiation ◽  
Human Dental Pulp ◽  
Pulp Cells

Abstract This study aimed at evaluate the effects of different aperture-sized type I collagen/silk fibroin (CSF) scaffolds on the proliferation and differentiation of human dental pulp cells (HDPCs). The CSF scaffolds were designed with 3D mapping software Solidworks. Three different aperture-sized scaffolds (CSF1–CSF3) were prepared by low-temperature deposition 3D printing technology. The morphology was observed by scanning electron microscope (SEM) and optical coherence tomography. The porosity, hydrophilicity and mechanical capacity of the scaffold were detected, respectively. HDPCs (third passage, 1 × 105 cells) were seeded into each scaffold and investigated by SEM, CCK-8, alkaline phosphatase (ALP) activity and HE staining. The CSF scaffolds had porous structures with macropores and micropores. The macropore size of CSF1 to CSF3 was 421 ± 27 μm, 579 ± 36 μm and 707 ± 43 μm, respectively. The porosity was 69.8 ± 2.2%, 80.1 ± 2.8% and 86.5 ± 3.3%, respectively. All these scaffolds enhanced the adhesion and proliferation of HDPCs. The ALP activity in the CSF1 group was higher than that in the CSF3 groups (P < 0.01). HE staining showed HDPCs grew in multilayer within the scaffolds. CSF scaffolds significantly improved the adhesion and ALP activity of HDPCs. CSF scaffolds were promising candidates in dentine-pulp complex regeneration.

scholarly journals Adhesion to type I collagen fibrous gels induces E- to N-cadherin switching without other EMT-related phenotypes in lung carcinoma cell A549

2020 ◽  
Author(s):  
Hitomi Fujisaki ◽  
Sugiko Futaki ◽  
Masashi Yamada ◽  
Kiyotoshi Sekiguchi ◽  
Toshihiko Hayashi ◽  
...  
Keyword(s):  
Single Cell ◽  
Type I Collagen ◽  
Transforming Growth Factor ◽  
A549 Cells ◽  
Type I ◽  
Mesenchymal Transition ◽  
Cell Behaviors ◽  
Tgf Β1 ◽  
Cells Cultured ◽  
Cell Cell

AbstractIn culture system, environmental factors, such as increasing exogenous growth factors and adhesion to type I collagen (Col-I) induce epithelial-to-mesenchymal transition (EMT) in cells. Col-I molecules maintain a non-fibril form under acidic conditions, and they reassemble into fibrils under physiological conditions. Col-I fibrils often assemble to form three-dimensional gels. The gels and non-gel-form of Col-I can be utilized as culture substrates and different gel-forming state often elicit different cell behaviors. However, gel-form dependent effects on cell behaviors, including EMT induction, remain unclear. EMT induction in lung cancer cell line A549 has been reported via adhesion to Col-I but the effects of gel form dependency are unelucidated. This study investigated the changes in EMT-related behaviors in A549 cells cultured on Col-I gels.We examined cell morphology, proliferation, single-cell migration and expression of EMT-related features in A549 cells cultured on gels or non-gel form of Col-I and non-treated dish with or without transforming growth factor (TGF)-β1. On Col-I gels, some cells kept cell–cell contacts and formed clusters, others maintained single-cell form. In cell–cell contact regions, E-cadherin expression was downregulated, whereas that of N-cadherin was upregulated. Vimentin and integrins α2 and β1 expression were not increased. In TGF-β1-treated A549 cells, cadherin switched from E- to N-cadherin. Their morphology changed to a mesenchymal form and cells scattered with no cluster formation. Vimentin, integrins α2 and β1 expression were upregulated. Thus, we concluded that culture on Col-I fibrous gels induced E- to N-cadherin switching without other EMT-related phenotypes in A549 cells.

scholarly journals The Effect of the Combination of Vitamin K2 and Genistein, Coumestrol and Daidzein on the Osteoblast Differentiation and Bone Matrix Formation

2016 ◽  
Vol 10 (2) ◽  
pp. 12-19
Author(s):  
Sahar S. Karieb ◽  
Mohammed M. Jawad ◽  
Hanady S. Al-Shmgani ◽  
Zahraa H.M. Kadri
Keyword(s):  
Bone Formation ◽  
Osteoblast Differentiation ◽  
Nuclear Factor Kappa B ◽  
Type I Collagen ◽  
Bone Mineralization ◽  
Bone Matrix ◽  
Vitamin K2 ◽  
Type I ◽  
Nuclear Factor ◽  
Effective Factor

Multiple studies have been reported the stimulatory effect of the combinations of nutrients factors on bone formation. One such factor is vitamin K2 which can be associated with bone protective activities. The effect of vitamin K2 alone and in combination with genistein, coumestrol and daidzein on osteoblast differentiation and mineralization were tested. Significantly, vitamin K2 increased bone mineralization in combination with genistein (10-5M), coumestrol (10-7M) and daidzein (10-5M). However, there is no additive effect of this vitamin on alkaline phosphatase (ALP) levels in osteoblasts. By contrast, vitamin K2 enhanced the stimulatory effect of type I collagen and osteocalcin expression. Vitamin K2 alone increased RUNX and OSX expression while there is no synergistic effect with tested compound; this vitamin also did not modulate nuclear factor kappa B ligand (RANKL)/ osteoprotegerin (OPG) ratio expression. These results suggested that vitamin K2 can be more effective factor in the presence of phytoestrogens on the improvement of bone formation after menopause.

Activation of human keratinocyte migration on type I collagen and fibronectin

1990 ◽  
Vol 96 (2) ◽  
pp. 197-205
Author(s):  
M. Guo ◽  
K. Toda ◽  
F. Grinnell
Keyword(s):  
Type I Collagen ◽  
Cultured Cells ◽  
Focal Adhesions ◽  
Human Keratinocytes ◽  
Type I ◽  
Integrin Subunit ◽  
Basal Cells ◽  
Keratinocyte Migration ◽  
Beta 1 Integrin ◽  
Cells Cultured

The purpose of our studies was to learn more about the regulation of keratinocyte migration. Human keratinocytes freshly harvested from skin were relatively immotile cells, whereas keratinocytes harvested from cell culture migrated on type I collagen or fibronectin as measured in a phagokinesis assay. Development of migratory competence by keratinocytes varied depending on the culture substratum. Cells cultured on plastic were activated more quickly and to a greater extent than cells cultured on dermis. The effect of the culture substratum on migratory competence was reversible. That is, cells cultured on plastic showed reduced activity after subculture on dermis. Cells cultured on dermis showed increased activity after subculture on plastic. Freshly isolated as well as cultured keratinocytes contained beta 1 integrin subunits, but only cultured cells were able to organize the subunits into focal adhesions. These adhesion sites also contained vinculin. In epidermal explants, beta 1 integrin subunits were mostly in basal cells, often more prominent between lateral cell borders than at the epidermal-dermal interface. In keratinocytes that migrated out of skin explants, there appeared to be an increase in the intensity of beta 1 integrin subunit immunostaining, possibly because of the change in shape of migrating cells. Also, beta 1 integrin subunits were found around and beneath migrating keratinocytes. These results show that changes in the distribution of beta 1 integrin subunits accompany development of migratory competence.

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