359 research outputs found

    Dust ring and gap formation by gas flow induced by low-mass planets embedded in protoplanetary disks I\rm I. Steady-state model

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    Recent high-spatial-resolution observations have revealed dust substructures in protoplanetary disks such as rings and gaps, which do not always correlate with gas. Because radial gas flow induced by low-mass, non-gas-gap-opening planets could affect the radial drift of dust, it potentially forms these dust substructures in disks. We investigate the potential of gas flow induced by low-mass planets to sculpt the rings and gaps in the dust profiles. We first perform three-dimensional hydrodynamical simulations, which resolve the local gas flow past a planet. We then calculate the trajectories of dust influenced by the planet-induced gas flow. Finally, we compute the steady-state dust surface density by incorporating the influences of the planet-induced gas flow into a one-dimensional dust advection-diffusion model. The outflow of the gas toward the outside of the planetary orbit inhibits the radial drift of dust, leading to dust accumulation (the dust ring). The outflow toward the inside of the planetary orbit enhances the inward drift of dust, causing dust depletion around the planetary orbit (the dust gap). Under weak turbulence (αdiff104\alpha_{\rm diff}\lesssim10^{-4}, where αdiff\alpha_{\rm diff} is the turbulence strength parameter), the gas flow induced by the planet with 1M\gtrsim1\,M_{\oplus} (Earth mass) generates the dust ring and gap in the distribution of small dust grains (1\lesssim1 cm) with the radial extent of 110\sim1\text{--}10 times gas scale height around the planetary orbit without creating a gas gap and pressure bump. The gas flow induced by low-mass, non-gas-gap-opening planets can be considered a possible origin of the observed dust substructures in disks. Our results may be helpful to explain the disks whose dust substructures were found not to correlate with those of the gas.Comment: 25 pages, 20 figures, Accepted for publication in Astronomy and Astrophysics (A&A

    Statistical Mechanics of Self--Gravitating System : Cluster Expansion Method

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    We study statistical mechanics of the self--gravitating system applying the cluster expansion method developed in solid state physics. By summing infinite series of diagrams, we derive a complex free energy whose imaginary part is related to the relaxation time of the system. Summation of another series yields two--point correlation function whose correlation length is essentially given by the Jeans wavelength of the system.Comment: 4 pages including 2 eps figures, RevTe

    Effects of culture on PAMPS/PDMAAm double-network gel on chondrogenic differentiation of mouse C3H10T1/2 cells: in vitro experimental study

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    BACKGROUND: Recently, several animal studies have found that spontaneous hyaline cartilage regeneration can be induced in vivo within a large osteochondral defect by implanting a synthetic double-network (DN) hydrogel, which is composed of poly-(2-acrylamido-2-methylpropanesulfonic acid) (PAMPS) and poly-(N,N’-dimethyl acrylamide) (PDMAAm), at the bottom of the defect. However, the effect of hydrogel on hyaline cartilage regeneration remains unexplained. The purpose of this study was to investigate the chondrogenic differentiation of C3H10T1/2 cells on PAMPS/PDMAAm DN gel. METHODS: C3H10T1/2 cells of 1.0 × 10(5) were cultured on PAMPS/PDMAAm DN gel in polystyrene tissue culture dishes or directly on polystyrene tissue culture dishes. We compared cultured cells on PAMPS/PDMAAm DN gel with those on polystyrene dishes by morphology using phase-contrast microscopy, mRNA expression of aggrecan, type I collagen, type II collagen, Sox 9 and osteocalcin using real-time RT-PCR, and local expression of type II collagen using immunocytochemistry. RESULTS: C3H10T1/2 cells cultured on the PAMPS/PDMAAm DN gels formed focal adhesions, aggregated rapidly and developed into large nodules within 7 days, while the cells cultured on the polystyrene surface did not. The mRNA levels of aggrecan, type I collagen, type II collagen, Sox 9 and osteocalcin were significantly greater in cells cultured on the PAMPS/PDMAAm DN gel than in those cultured on polystyrene dishes. In addition, C3H10T1/2 cells cultured on PAMPS/PDMAAm DN gel expressed more type II collagen at the protein level when compared with cells cultured on polystyrene dishes. CONCLUSIONS: The present study showed that PAMPS/PDMAAm DN gel enhanced chondrogenesis of C3H10T1/2 cells, which are functionally similar to mesenchymal stem cells. This suggests that mesenchymal stem cells from the bone marrow contribute to spontaneous hyaline cartilage regeneration in vivo in large osteochondral defects after implantation of PAMPS/PDMAAm DN gels. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/1471-2474-15-320) contains supplementary material, which is available to authorized users

    Double-Network Hydrogels Strongly Bondable to Bones by Spontaneous Osteogenesis Penetration

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    Implanting hydroxyapatite-mineralized tough hydrogel into osteochondral defects of rabbits, osteogenesis spontaneously penetrates into the gel matrix owing to the semi-permeablility of the hydrogel. The gradient layer (around 40 μm thick) contributes quite strong bonding of the gel to bone. This is the first success in realizing the robust osteointegration of tough hydrogels, and the method is simple and feasible for practical use

    The nucleotide and deduced amino acid sequences of porcine liver proline-β-naphthylamidase swEvidence for the identity with carboxylesterase

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    AbstractA cDNA clone for porcine liver proline-β-naphthylamidase was isolated and sequenced. The deduced amino acid sequence of 567 residues was highly homologous with those of carboxylesterases (EC 3.1.1.1) previously reported for other species. In addition, proline-β-naphthylamidase purified from porcine liver was shown to have strong activity towards p-nitrophenylacetate, a representative substrate for carboxylesterases. These results suggest that proline-β-naphthylamidase is identical with carboxylesterase
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