scholarly journals In Vivo Quantitative Evaluation of the Transport Kinetics of Gold Nanocages in a Lymphatic System by Noninvasive Photoacoustic Tomography

ACS Nano ◽  
2011 ◽  
Vol 5 (12) ◽  
pp. 9658-9667 ◽  
Author(s):  
Xin Cai ◽  
Weiyang Li ◽  
Chul-Hong Kim ◽  
Yuchen Yuan ◽  
Lihong V. Wang ◽  
...  
2018 ◽  
Vol 14 (5) ◽  
pp. 1796-1797
Author(s):  
Huanjie Li ◽  
Yanzhi Wang ◽  
Huili Li ◽  
Shengnan Huang ◽  
Ying Liu ◽  
...  

1995 ◽  
Vol 198 (10) ◽  
pp. 2237-2244 ◽  
Author(s):  
F Jensen ◽  
J Brahm

The continuous flow tube method was used to investigate the kinetics of chloride transport, and its potential oxygenation-dependency, in red blood cells (RBCs) from four teleost fish species and man. A significant interspecific variation in Cl- transport kinetics was found. At 15 °C, the rate constant k for unidirectional 36Cl- efflux was significantly lower in RBCs from eel and carp than in RBCs from rainbow trout and Atlantic cod. The values of k of cod RBCs at 15 °C and of human RBCs at 37 °C were not significantly different. The volume and surface area of the RBCs were evaluated and used to calculate the apparent membrane permeability to Cl- (PCl). The magnitude of PCl followed the sequence: eel<carp<trout¾cod. PCl values in trout and cod at 15 °C were similar to human values at 37 °C. An extrapolation of human values to 15 °C revealed that the Cl- shift at this temperature was considerable faster in all four teleosts than in man. This illustrates appropriate adaption of band-3-mediated anion transport to the different temperature regimes encountered by fish and mammals. The Cl- transport kinetics did not differ significantly between oxygenated and deoxygenated RBCs in any of the species examined. The apparent absence of any effect of a change in haemoglobin oxygen-saturation may be related to the presence of a flexible link which results in minimal interaction between the membrane domain (mediating Cl- transport) and the cytoplasmic domain (to which oxygenation-dependent haemoglobin binding occurs) of band 3. In carp, Cl- transport kinetics were not influenced by pH over the extracellular pH (pHe) range 7.6­8.36, which spans the in vivo pHe range. The data are discussed in relation to the rate-limiting role of red blood cell HCO3-/Cl- exchange for CO2 excretion.


ACS Nano ◽  
2010 ◽  
Vol 4 (8) ◽  
pp. 4559-4564 ◽  
Author(s):  
Chulhong Kim ◽  
Eun Chul Cho ◽  
Jingyi Chen ◽  
Kwang Hyun Song ◽  
Leslie Au ◽  
...  

2014 ◽  
Vol 86 (2) ◽  
pp. 219-226 ◽  
Author(s):  
Taís Gratieri ◽  
Ester Pujol-Bello ◽  
Guilherme M. Gelfuso ◽  
Joel G. de Souza ◽  
Renata F.V. Lopez ◽  
...  

Author(s):  
Lieselotte Veryser ◽  
Lien Taevernier ◽  
Tanmayee Joshi ◽  
Pratima Tatke ◽  
Evelien Wynendaele ◽  
...  

Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel

Alzheimer's disease is characterized post-mortem in part by abnormal extracellular neuritic plaques found in brain tissue. There appears to be a correlation between the severity of Alzheimer's dementia in vivo and the number of plaques found in particular areas of the brain. These plaques are known to be the deposition sites of fibrils of the protein β-amyloid. It is thought that if the assembly of these plaques could be inhibited, the severity of the disease would be decreased. The peptide fragment Aβ, a precursor of the p-amyloid protein, has a 40 amino acid sequence, and has been shown to be toxic to neuronal cells in culture after an aging process of several days. This toxicity corresponds to the kinetics of in vitro amyloid fibril formation. In this study, we report the biochemical and ultrastructural effects of pH and the inhibitory agent hexadecyl-N-methylpiperidinium (HMP) bromide, one of a class of ionic micellar detergents known to be capable of solubilizing hydrophobic peptides, on the in vitro assembly of the peptide fragment Aβ.


1977 ◽  
Vol 16 (04) ◽  
pp. 157-162 ◽  
Author(s):  
C. Schümichen ◽  
B. Mackenbrock ◽  
G. Hoffmann

SummaryThe bone-seeking 99mTc-Sn-pyrophosphate compound (compound A) was diluted both in vitro and in vivo and proved to be unstable both in vitro and in vivo. However, stability was much better in vivo than in vitro and thus the in vitro stability of compound A after dilution in various mediums could be followed up by a consecutive evaluation of the in vivo distribution in the rat. After dilution in neutral normal saline compound A is metastable and after a short half-life it is transformed into the other 99mTc-Sn-pyrophosphate compound A is metastable and after a short half-life in bone but in the kidneys. After dilution in normal saline of low pH and in buffering solutions the stability of compound A is increased. In human plasma compound A is relatively stable but not in plasma water. When compound B is formed in a buffering solution, uptake in the kidneys and excretion in urine is lowered and blood concentration increased.It is assumed that the association of protons to compound A will increase its stability at low concentrations while that to compound B will lead to a strong protein bond in plasma. It is concluded that compound A will not be stable in vivo because of a lack of stability in the extravascular space, and that the protein bond in plasma will be a measure of its in vivo stability.


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