Osteoconductive TiO2 Coating on Titanium Using Anodizing in High Content Phosphoric Acid

2012 ◽  
Vol 706-709 ◽  
pp. 538-542
Author(s):  
Kensuke Kuroda ◽  
Ryoichi Ichino ◽  
Masazumi Okido

In this study, anodizing of Ti in the various concentration of H3PO4 aqueous solutions gave TiO2 films, and the osteoconductivity was examined using in vivo testing. In the anodizing treatment, anodizing potential of < 200 V was applied to the Ti substrate in H3PO4 aqueous solutions with the concentration of 0.1 to 14 M at 298 K. The coatings were evaluated using SEM, XRD, FT-IR and XPS. In in vivo testing, the coated samples were implanted in the rats’ tibia for 14 d to evaluate the osteoconductivity. In H3PO4 aqueous solutions with any concentration, anatase-type TiO2 films were obtained on the Ti substrate by anodizing. The crystallinity of anodized TiO2 films depended on the concentration of H3PO4 and sparking. In less than 2 M H3PO4, anatase with high crystallinity was formed. On the other hand, anodizing with sparking in more than 4 M H3PO4, gave low crystallinity anatase film. In in vivo testing, osteoconductivity of the coatings with low crystallinity anatase was much higher than that with high crystallinity.

1987 ◽  
Vol 52 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Jan Hlaváček ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Walter Y. Chan ◽  
Victor J. Hruby

[8-Neopentylglycine]oxytocin (II) and [8-cycloleucine]oxytocin (III) were prepared by a combination of solid-phase synthesis and fragment condensation. Both analogues exhibited decreased uterotonic potency in vitro, each being about 15-30% that of oxytocin. Analogue II also displayed similarly decreased uterotonic potency in vivo and galactogogic potency. On the other hand, analogue III exhibited almost the same potency as oxytocin in the uterotonic assay in vivo and in the galactogogic assay.


2012 ◽  
Vol 16 (01) ◽  
pp. 114-121 ◽  
Author(s):  
Tapan K. Saha ◽  
Yutaka Yoshikawa ◽  
Hirouki Yasui ◽  
Hiromu Sakurai

We prepared [meso-tetrakis(4-carboxylatophenyl)porphyrinato]oxovanadium(IV) tetrasodium, ([VO(tcpp)]Na4), and investigated its in vitro insulin-mimetic activity and in vivo metallokinetic feature in healthy rats. The results were compared with those of previously proposed insulin-mimetic oxovanadium(IV)porphyrin complexes and oxovanadium(IV) sulphate. The in vitro insulin-mimetic activity and bioavailability of [VO(tcpp)]Na4 were considerably better than those of [meso-tetrakis (1-methylpyridinium-4-yl)porphyrinato]oxovanadium(IV)(4+) tetraperchlorate ([VO(tmpyp)](ClO4)4) and oxovanadium(IV) sulphate. On the other hand, [VO(tcpp)]Na4 and [meso-tetrakis(4-sulfonatophenyl) porphyrinato]oxidovanadate(IV)(4-)([VO(tpps)]) showed very similar in vitro insulin-mimetic activity and in vivo metallokinetic feature in healthy rats. In particular, the order of in vitro insulin-mimetic activity of the complexes was determined to be: [VO(tcpp)]Na4 ≈ [VO(tpps)] > ([VO(tmpyp)](ClO4)4 > oxovanadium(IV) sulphate.


Reproduction ◽  
2016 ◽  
Vol 152 (4) ◽  
pp. 313-321 ◽  
Author(s):  
Naoya Araki ◽  
Natsuko Kawano ◽  
Woojin Kang ◽  
Kenji Miyado ◽  
Kaoru Yoshida ◽  
...  

Mammalian spermatozoa acquire their fertilizing ability in the female reproductive tract (sperm capacitation). On the other hand, seminal vesicle secretion, which is a major component of seminal plasma, inhibits the initiation of sperm capacitation (capacitation inhibition) and reduces the fertility of the capacitated spermatozoa (decapacitation). There are seven major proteins involved in murine seminal vesicle secretion (SVS1-7), and we have previously shown that SVS2 acts as both a capacitation inhibitor and a decapacitation factor, and is indispensable forin vivofertilization. However, the effects of SVSs other than SVS2 on the sperm have not been elucidated. Since mouseSvs2–Svs6genes evolved by gene duplication belong to the same gene family, it is possible that SVSs other than SVS2 also have some effects on sperm capacitation. In this study, we examined the effects of SVS3 and SVS4 on sperm capacitation. Our results showed that both SVS3 and SVS4 are able to bind to spermatozoa, but SVS3 alone showed no effects on sperm capacitation. On the other hand, SVS4 acted as a capacitation inhibitor, although it did not show decapacitation abilities. Interestingly, SVS3 showed an affinity for SVS2 and it facilitated the effects of SVS2. Interaction of SVS2 and spermatozoa is mediated by the ganglioside GM1 in the sperm membrane; however, both SVS3 and SVS4 had weaker affinities for GM1 than SVS2. Therefore, we suggest that separate processes may cause capacitation inhibition and decapacitation, and SVS3 and SVS4 act on sperm capacitation cooperatively with SVS2.


2006 ◽  
Vol 71 (4) ◽  
pp. 532-542 ◽  
Author(s):  
Suzana Jovanović-Šanta ◽  
Julijana Petrović ◽  
Marija Sakač ◽  
Zorica Žakula ◽  
Esma Isenović ◽  
...  

Since many of newly synthesised D-secoestratriene derivatives showed antiestrogenic effect, with almost a total loss of estrogenic activity, we studied the effects of some of these compounds on estrogen receptors (ER), the translocation of the estrogen-ER complexes formed in presence of competing substances into the nucleus, as well as the binding of these complexes to DNA. The results of uterotrophic effects of analysed derivatives are in agreement with the influence of these compounds on activity and binding parameters of estrogen receptors. Namely, compounds that show relatively high antiestrogenic activity predominantly increase Kd and inhibit translocation to nuclei of radioactive complexes formed in their presence. On the other hand, compounds that do not significantly change binding parameters of estrogen receptors do not show antiestrogenic effect in in vivo experiments.


2013 ◽  
Vol 300-301 ◽  
pp. 1352-1355 ◽  
Author(s):  
Futo Tsumuji ◽  
Daiki Hoshino ◽  
Shou Ogihara ◽  
Zong Fan Duan ◽  
Yutaro Suzuki ◽  
...  

In this work, a PPy actuator was fabricated by galvanostatic electropolymerization. The electrochemical deformation behaviors of the PPy actuator were investigated in aqueous solutions of an electrolyte, lithium bis(trifluoromethanesulphonyl)imide (LiTFSI), containing different concentrations of methanol. Marked improvement of the actuating strain of approximately 9% was achieved when the actuator was driven by a potential between –1 and 1 V in the LiTFSI electrolyte containing 40 to 50% of methanol under a load stress of 0. 3 MPa. On the other hand, the actuator functioned in the electrolyte solutions containing more than 60% of methanol showed rapid decrease of the actuating strain and the electrochemical creep after repeated actuations. Possible mechanisms for these behaviors were discussed.


1987 ◽  
Vol 65 (11) ◽  
pp. 2656-2660 ◽  
Author(s):  
Alfredo Maestre Alvarez ◽  
Nicole Morel-Desrosiers ◽  
Jean-Pierre Morel

The standard enthalpies of transfer of ribose and arabinose from water to aqueous solutions of electrolytes (CaCl2, SrCl2, BaCl2, LaCl3, and GdCl3) have been measured at 25 °C. A method is described to calculate from these data the equilibrium constant and the enthalpy for the association between the cations and the complexing isomers of ribose. Mean values relative to these isomers are given: the constants vary from 2.0 to 4.3 and the enthalpies from −5.9 to −17.9 kJ mol−1 for the different cations studied. The thermodynamic properties of association are not related to the size nor to the charge of the complexed cation in a simple way. On the other hand, the enthalpies of reaction are linearly correlated to the entropies of reaction.


2005 ◽  
Vol 60 (8-9) ◽  
pp. 633-636 ◽  
Author(s):  
Nuri Öztürk ◽  
Çağrı Çırak ◽  
Semiha Bahçeli

The adsorption of 1,5-pentanedithiol (1,5-PDT) and 1,6-hexanedithiol (1,6-HDT) in liquid phases on NaA (or 4A-type), CaA (or 5A-type) and NaY zeolites has been studied by using infrared spectroscopy. From the IR spectra it is found that the peak positions of the symmetric as well as the antisymmetric modes of the methylene (CH2) groups are observed at almost the same band values for the title dithiolates adsorbed on the A-type and NaY zeolites. On the other hand, the weak SH stretching vibration, observed for all samples, can be attributed to the sulphure atoms of 1,5-PDT and 1,6-HDT coordinatively adsorbed on cationic sites of the zeolites.


1968 ◽  
Vol 46 (4) ◽  
pp. 662-663 ◽  
Author(s):  
Robert H. McCorkell ◽  
John W. Irvine Jr.

The presence of an extracting strong acid greatly enhances the extraction of phosphoric acid from aqueous solutions into organic solvents, but no type of compound forms between the phosphoric acid and the other extracted species. Only the alteration of the solvent properties when an ionic species and water are added to it can account for the increase in [Formula: see text]


2021 ◽  
Vol 5 (1) ◽  
pp. e202101162
Author(s):  
Yuta Endo ◽  
Yuko Shimizu ◽  
Hanako Nishikawa ◽  
Katsuhiro Sawasato ◽  
Ken-ichi Nishiyama

Integral membrane proteins with the N-out topology are inserted into membranes usually in YidC- and PMF-dependent manners. The molecular basis of the various dependencies on insertion factors is not fully understood. A model protein, Pf3-Lep, is inserted independently of both YidC and PMF, whereas the V15D mutant requires both YidC and PMF in vivo. We analyzed the mechanisms that determine the insertion factor dependency in vitro. Glycolipid MPIase was required for insertion of both proteins because MPIase depletion caused a significant defect in insertion. On the other hand, YidC depletion and PMF dissipation had no effects on Pf3-Lep insertion, whereas V15D insertion was reduced. We reconstituted (proteo)liposomes containing MPIase, YidC, and/or F0F1-ATPase. MPIase was essential for insertion of both proteins. YidC and PMF stimulated Pf3-Lep insertion as the synthesis level increased. V15D insertion was stimulated by both YidC and PMF irrespective of the synthesis level. These results indicate that charges in the N-terminal region and the synthesis level are the determinants of YidC and PMF dependencies with the interplay between MPIase, YidC, and PMF.


1994 ◽  
Vol 124 (1) ◽  
pp. 129-137 ◽  
Author(s):  
Y Yamakita ◽  
S Yamashiro ◽  
F Matsumura

Phosphorylation of the regulatory light chain of myosin II (MLC) controls the contractility of actomyosin in nonmuscle and muscle cells. It has been reported that cdc2 phosphorylates MLC in vitro at Ser-1 or Ser-2 and Thr-9 which protein kinase C phosphorylates (Satterwhite, L. L., M. J. Lohka, K. L. Wilson, T. Y. Scherson, L. K. Cisek, J. L. Corden, and T. D. Pollard. 1992 J. Cell Biol. 118:595-605). We have examined in vivo phosphorylation of MLC during mitosis and after the release of mitotic arrest. Phosphate incorporation of MLC in mitotic cells is found to be 6-12 times greater than that in nonmitotic cells. Phosphopeptide maps have revealed that the MLC from mitotic cells is phosphorylated at Ser-1 and/or Ser-2 (Ser-1/2), but not at Thr-9. MLC is also phosphorylated to a much lesser extent at Ser-19 which myosin light chain kinase phosphorylates. On the other hand, MLC of nonmitotic cells is phosphorylated at Ser-19 but not at Ser-1/2. The extent of phosphate incorporation is doubled at 30 min after the release of mitotic arrest when some cells start cytokinesis. Phosphopeptide analyses have revealed that the phosphorylation at Ser-19 is increased 20 times, while the phosphorylation at Ser-1/2 is decreased by half. This high extent of MLC phosphorylation at Ser-19 is maintained for another 30 min and gradually decreased to near the level of interphase cells as cells complete spreading at 180 min. On the other hand, phosphorylation at Ser-1/2 is decreased to 18% at 60 min, and is practically undetectable at 180 min after the release of mitotic arrest. The stoichiometry of MLC phosphorylation has been determined by quantitation of phosphorylated and unphosphorylated forms of MLC separated on 2D gels. The molar ratio of phosphorylated MLC to total MLC is found to be 0.16 +/- 0.06 and 0.31 +/- 0.05 in interphase and mitotic cells, respectively. The ratio is increased to 0.49 +/- 0.05 at 30 min after the release of mitotic arrest. These results suggest that the change in the phosphorylation site from Ser-1/2 to Ser-19 plays an important role in signaling cytokinesis.


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