Cell Kinetics of Human Nasal Septal Chondrocytes In Vitro: Importance for Cartilage Grafting in Otolaryngology

2002 ◽  
Vol 31 (06) ◽  
pp. 366 ◽  
Author(s):  
Anna Lavezzi ◽  
Mario Mantovani ◽  
Lorenzo Grillo della Berta ◽  
Luigi Matturri
Keyword(s):  
Cell Kinetics ◽  
Cartilage Grafting ◽  
Kinetics Of

Cell kinetics of the in vitro metaphase arrest technique and the clinical applications

1993 ◽  
Vol 2 (5) ◽  
pp. 387-392 ◽  
Author(s):  
P S Rooney ◽  
P A Clarke ◽  
K-A Gifford ◽  
M H Robinson ◽  
J D Hardcastle ◽  
...  
Keyword(s):  
Cell Kinetics ◽  
Clinical Applications ◽  
Metaphase Arrest ◽  
Kinetics Of

Growth and cell kinetics of human hair papilla cells in vitro. An autoradiographic and flow cytometric study

1991 ◽  
Vol 24 (4) ◽  
pp. 367-374 ◽  
Author(s):  
I. D. Bassukas ◽  
A. Arai ◽  
H. Schell ◽  
O. P. Hornstein
Keyword(s):  
Human Hair ◽  
Cell Kinetics ◽  
Flow Cytometric ◽  
Flow Cytometric Study ◽  
Kinetics Of

Effect of pH and inhibitors on beta-amyloid fibril assembly

1996 ◽  
Vol 54 ◽  
pp. 752-753
Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel
Keyword(s):  
Amyloid Fibril ◽  
Peptide Fragment ◽  
Hydrophobic Peptides ◽  
Amyloid Fibril Formation ◽  
Effects Of Ph ◽  
Severity Of The Disease ◽  
Kinetics Of ◽  
The Brain

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.

Kinetics of Various 99mTc-Sn-Pyrophosphate Compounds in the Rat

1977 ◽  
Vol 16 (04) ◽  
pp. 157-162 ◽  
Author(s):  
C. Schümichen ◽  
B. Mackenbrock ◽  
G. Hoffmann
Keyword(s):  
Normal Saline ◽  
Half Life ◽  
Compound A ◽  
Short Half Life ◽  
Low Concentrations ◽  
The Stability ◽  
Kinetics Of ◽  
In Vitro Stability

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.

Sign in / Sign up

Export Citation Format

Share Document