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1.
Neuro Endocrinol Lett ; 33(2): 207-11, 2012.
Article in English | MEDLINE | ID: mdl-22592203

ABSTRACT

OBJECTIVES: The S100B protein subgroup is a thermolabile acidic calcium-binding protein, which was first described in association with the central nervous system. Destruction of nerve tissue results in S100B protein release from astrocytes and elevation of its levels in cerebrospinal fluid. If the blood-brain barrier is also damaged, S100B can pass into the systemic circulation and elevated blood levels of S100B can be detected. High S100B serum levels in patients with head injuries are predictive of possible development of secondary brain injury and may be related to the extent of permanent injury to the CNS . MATERIAL AND METHODS: The authors present results obtained from a group of 39 children aged 0 (newborns) to 17 years with an isolated craniocerebral injury. RESULTS: In our group of 39 children (aged 0-17 years) we observed excellent GOS group (GOS - Glasgow Outcome Scale 4 or 5) in 33 patients at the time of transfer from our intensive care unit to the neurological department. There were no deaths and only 6 children were in the poor GOS group (GOS 2 or 3). A second GOS evaluation was performed 6 months later: at this time 36 children were in the excellent GOS group and only 3 children remained in the poor GOS group. CONCLUSIONS: Due to high variability in S100B protein serum levels in children (dependent on age and gender) no correlation between initial S100B levels and GOS was observed for our group of patients. Our results indicate that the rate of decrease of S100B protein levels back to normal values is more meaningful than its absolute value.


Subject(s)
Craniocerebral Trauma/blood , Craniocerebral Trauma/diagnosis , Glasgow Outcome Scale/statistics & numerical data , Nerve Growth Factors/blood , S100 Proteins/blood , Adolescent , Child , Child, Preschool , Female , Glasgow Coma Scale/statistics & numerical data , Humans , Infant , Infant, Newborn , Male , S100 Calcium Binding Protein beta Subunit
2.
Acta Medica (Hradec Kralove) ; 47(4): 309-11, 2004.
Article in English | MEDLINE | ID: mdl-15841917

ABSTRACT

The objective of our work was to describe the photophysical properties (absorption and fluorescence) of the sensitizers TPPS4, ZnTPPS4 a PdTPPS4 and above all the complexes of these sensitizers with cyclodextrin carriers HP-alpha-CD, HP-beta-CD and HP-gamma-CD (2-hydroxypropyl-alpha, beta, gamma-cyclodextrin) in a suitable environment for the cultivation of cancerous cell lines, and to determine the optimal radioactive conditions for maximizing photodynamic effects in cancerous cells.


Subject(s)
Cyclodextrins/chemistry , Drug Carriers/chemistry , Photochemotherapy , Radiation-Sensitizing Agents/chemistry , Neoplasms/drug therapy , Photochemistry , Polymers/chemistry , Porphyrins/chemistry , Pyrroles/chemistry , Spectrometry, Fluorescence , Spectrophotometry
3.
J Biochem Biophys Methods ; 51(3): 273-81, 2002 May 31.
Article in English | MEDLINE | ID: mdl-12088887

ABSTRACT

In this work, we present a home-made two-dimensional (2-D) CCD imaging system for the monochromatic densitometry of plane gels and its application to the imaging and densitometry of chlorophyll (Chl)-containing proteins separated by non-denaturing polyacrylamide gel electrophoresis. The monochromatic imaging of separated green bands at the wavelengths corresponding to their absorption band increases their contrast. This allows a better visualization of the faint-green bands in the gel and using of samples with lower Chl content for the electrophoresis. By the comparison of 2-D densitograms of the same gel illuminated with 670 and 650 nm lights, that is, at the red absorption maximum of Chl a and b, respectively, we achieved a selective imaging of the complexes with different Chl a/b ratio. This approach was used to specify an unknown band that appeared in the gel of the sample prepared from the thylakoid membranes of preheated barley leaves.


Subject(s)
Chlorophyll/analysis , Photosynthetic Reaction Center Complex Proteins/isolation & purification , Electrophoresis, Gel, Two-Dimensional/methods , Electrophoresis, Polyacrylamide Gel/methods , Hordeum/growth & development , Light-Harvesting Protein Complexes
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