Bicontinuous Cyclosporin a Loaded Water-AOT/Tween 85-Isopropylmyristate Microemulsion: Structural Characterization and Dermal Pharmacokinetics In Vivo

2009 ◽  
Vol 98 (3) ◽  
pp. 1167-1176 ◽  
Author(s):  
Hongzhuo Liu ◽  
Yongjun Wang ◽  
Yiyong Lang ◽  
Huimin Yao ◽  
Yang Dong ◽  
...  
Keyword(s):  
Cyclosporin A ◽  
Structural Characterization ◽  
Dermal Pharmacokinetics

Inhibition of Cyclosporin A-Induced Gingival Overgrowth by Azithromycin Through Phagocytosis: An In Vivo and In Vitro Study

2004 ◽  
Vol 75 (3) ◽  
pp. 380-387 ◽  
Author(s):  
Jeong-Won Paik ◽  
Chang-Sung Kim ◽  
Kyoo-Sung Cho ◽  
Jung-Kiu Chai ◽  
Chong-Kwan Kim ◽  
...  
Keyword(s):  
Cyclosporin A ◽  
In Vitro Study ◽  
Vitro Study ◽  
Gingival Overgrowth

Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location

1993 ◽  
Vol 13 (8) ◽  
pp. 4760-4769
Author(s):  
R J Bram ◽  
D T Hung ◽  
P K Martin ◽  
S L Schreiber ◽  
G R Crabtree
Keyword(s):  
Signal Transduction ◽  
T Cell ◽  
Cyclosporin A ◽  
Cell Function ◽  
Inhibitory Effects ◽  
Gene Deletions ◽  
Cyclophilin B ◽  
Intracellular Vesicles

The immunosuppressants cyclosporin A (CsA) and FK506 appear to block T-cell function by inhibiting the calcium-regulated phosphatase calcineurin. While multiple distinct intracellular receptors for these drugs (cyclophilins and FKBPs, collectively immunophilins) have been characterized, the functionally active ones have not been discerned. We found that overexpression of cyclophilin A or B or FKBP12 increased T-cell sensitivity to CsA or FK506, respectively, demonstrating that they are able to mediate the inhibitory effects of their respective immunosuppressants in vivo. In contrast, cyclophilin C, FKBP13, and FKBP25 had no effect. Direct comparison of the Ki of each drug-immunophilin complex for calcineurin in vitro revealed that although calcineurin binding was clearly necessary, it was not sufficient to explain the in vivo activity of the immunophilin. Subcellular localization was shown also to play a role, since gene deletions of cyclophilins B and C which changed their intracellular locations altered their activities significantly. Cyclophilin B has been shown previously to be located within calcium-containing intracellular vesicles; its ability to mediate CsA inhibition implies that certain components of the signal transduction machinery are also spatially restricted within the cell.

scholarly journals In vivo degradation of banana starch: Structural characterization of the degradation process

2010 ◽  
Vol 81 (2) ◽  
pp. 291-299 ◽  
Author(s):  
Fernanda H.G. Peroni-Okita ◽  
Renata A. Simão ◽  
Mateus B. Cardoso ◽  
Claudinéia A. Soares ◽  
Franco M. Lajolo ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Degradation Process ◽  
In Vivo Degradation

scholarly journals Partial inhibition by cyclosporin A of the swelling of liver mitochondria in vivo and in vitro induced by sub-micromolar [Ca2+], but not by butyrate. Evidence for two distinct swelling mechanisms

1990 ◽  
Vol 268 (1) ◽  
pp. 147-152 ◽  
Author(s):  
A M Davidson ◽  
A P Halestrap
Keyword(s):  
Light Scattering ◽  
Cyclosporin A ◽  
Binding Sites ◽  
Mitochondrial Protein ◽  
Liver Mitochondria ◽  
Partial Inhibition ◽  
Mitochondrial Volume ◽  
Bongkrekic Acid

1. The effects of cyclosporin A on the increase in matrix PPi and consequent swelling of energized liver mitochondria incubated with 1 mM-butyrate, 30 microM-bongkrekic acid or 0.1-35 microM-Ca2+ [Halestrap (1989) Biochim. Biophys. Acta 973, 355-382] were studied. 2. Cyclosporin (1 microM) had no significant effect on the swelling induced by butyrate, bongkrekic acid or Ca2+ at concentrations of less than 0.3 microM. 3. At higher [Ca2+] (greater than 0.3 microM), swelling became progressively inhibited by cyclosporin, although the increase in matrix PPi was slightly greater in the presence than in the absence of cyclosporin. 4. Titration with cyclosporin indicated that there are 128 pmol of relevant cyclosporin-binding sites per mg of mitochondrial protein, with a Ki of about 5 nM. 5. The decrease in light-scattering by hepatocytes induced by butyrate [Davidson & Halestrap (1988) Biochem. J. 254, 379-384] was unaffected by cyclosporin, whereas that induced by vasopressin was inhibited by 20-30% without a significant change in cellular PPi content. 6. It is suggested that there are two mechanisms for the increase in mitochondrial volume induced by Ca2+: a PPi-mediated mechanism that is insensitive to cyclosporin and an additional Ca2(+)-mediated effect that is inhibited by cyclosporin. The nature of these pathways and their inter-relationship is discussed in the following paper [Halestrap & Davidson (1990) Biochem. J. 268, 153-160].

scholarly journals Strontium-releasing fluorapatite glass-ceramic scaffolds: Structural characterization and in vivo performance

2018 ◽  
Vol 75 ◽  
pp. 463-471 ◽  
Author(s):  
Isabelle Denry ◽  
Ourania-Menti Goudouri ◽  
Douglas C. Fredericks ◽  
Adil Akkouch ◽  
Michael R. Acevedo ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Glass Ceramic

Structural characterization and in vitro–in vivo evaluation of effect of a polysaccharide from Sanguisorba officinalis on acute kidney injury

2019 ◽  
Vol 10 (11) ◽  
pp. 7142-7151
Author(s):  
Wenwen Zhao ◽  
Xi Zeng ◽  
Fancheng Meng ◽  
Xiaolin Bi ◽  
Dahai Xu ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Structural Characterization ◽  
Kidney Injury ◽  
In Vivo Evaluation ◽  
Acidic Polysaccharide ◽  
Sanguisorba Officinalis

We report here an acidic polysaccharide, namely RSP-3, which ameliorates acute kidney injury and is obtained from Sanguisorba officinalis.

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