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Coomassie Brilliant Blue G-250 can be used to quantitatively determine proteins in cerebrospinal fluid. When the dye combines with protein, the absorption maximum of the dye shifts. The dye-protein color forms almost instantaneously and is stable for at least 1 h. The procedure is also insensitive to changes in temperature in the range of 20--30 degrees C. The absorptivities of the dye complexes with human albumin or globulin differ, thus a pure albumin or pure globulin standard is unsuitable; a standard containing 70% albumin and 30% globulins is the most appropriate for this application. A bichromatic approach to standardization increases the range of linearity of a calibration curve. The method gives values that are about 9% higher than a sodium sulfate-sulfosalicylic turbidimetric procedure for cerbrospinal fluid proteins.
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Case report on a 33 year old multiple sclerosis patient showing recurrent meningitis with an episode of rhinorrhea. The emphasis was put on the protein electrophoresis patterns.
The cerebrospinal fluid (CSF) is a specific ultrafiltrate of plasma, which surrounds the brain and spinal cord. The study of its proteins and their alteration may yield useful information on several neurological diseases. By using various electrophoretic separation techniques, several CSF proteins have been identified derived from plasma or from brain. Different one-dimensional methods, such as agarose gel electrophoresis and isoelectric focusing, are of similar value in identifying the non-specific oligoclonal bands, which are mainly helpful in the diagnosis of multiple sclerosis and other inflammatory diseases. Isoelectric focusing has a greater resolution than other one-dimensional methods, and it yields additional data about disease-associated proteins occurring in Alzheimer's disease, Huntington's chorea and amyotrophic lateral sclerosis. Silver-stained two-dimensional gels provide more information about the complex protein composition of CSF, particularly about proteins produced in the brain, such as apolipoprotein E and neuron-specific enolase. For the detection of oligoclonal antibodies, the investigation of protein changes revealed by Parkinson's disease, schizophrenia and Creutzfeldt-Jakob disease, and the analysis of CSF immune complexes, two-dimensional electrophoresis has a greater sensitivity.
A prospective study was performed to determine whether the popular opinion that a high CSF protein concentration increases the risk of shunt complications is true. Ninety-five patients were enrolled into the study and they had 116 shunt operations over 15 months. It was considered that the CSF protein content might influence the development of complications that occurred within 2 months of surgery. Shunt complications occurred following 24.6% of operations within this period. This included 12 infections, 13 obstructions and three cases of overdrainage. The distribution of complications, compared to CSF protein content, was non-significant on a chi 2-test (p > 0.5). The total protein content of each of the complication groups was also analysed using the Mann-Whitney U-test and the differences were non-significant for the infection (0.1 > p > 0.05) and obstruction groups (0.5 > p > 0.1). It is concluded that an elevated CSF protein content does not increase the risk of shunt complications, and that there is no reason why shunting should be delayed in patients with a high CSF protein content.
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BACKGROUND: Prosthetic infections are a major problem, requiring complex and lengthy management. The role of blood proteins in the pathogenesis of implant infection has been investigated, but research into the role of CSF protein in shunt infections has not been undertaken, even though a high CSF protein has been assumed to increase the risk of such infections. METHODS: New shunt catheters were exposed to either CSF or individual protein solutions, and the numbers of radiolabelled staphylococci that adhered to them were compared with controls that had been exposed to saline only. RESULTS: A significant reduction in bacteria adhering to the test catheter was found in each instance. Furthermore, the CSF with the highest protein content, from a patient with intraventricular haemorrhage, had the greatest inhibitory effect on bacterial adhesion. The effect of the solutions on the hydrophobicity of the silicone rubber was also investigated. The silicone rubber was more hydrophilic, and bacterial adhesion was less, with solutions containing a higher protein content, and these findings were in keeping with the current theories on the mechanism of bacterial adhesion to polymers. CONCLUSIONS: A high CSF protein content does not predispose to the development of shunt infections.
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Physiologic alterations in cerebrospinal fluid proteins occur inter alia with aging. Agarose gel electrophoresis discriminates many cerebrospinal fluid proteins and in addition quantifies concentration alterations. This study aimed to investigate the time course of these alterations in children and to establish normative values for cerebrospinal fluid protein properties. In 202 children without diseases known to alter cerebrospinal fluid, normative protein properties were quantified using nephelometry, ultrafiltration, high-resolution electrophoresis, and Gaussian curve fit densitometry. Total protein and protein concentrations (albumin and gamma-globulins) decreased from birth until 7 months age, and, from then on, increased slightly (transthyretin, albumin, and alpha2-proteins) or strongly (gamma-globulins). Protein proportions (transthyretin and transferrin) increased until about 3 years of age and decreased from then on. These normative values for children as quantified by high-resolution agarose gel electrophoresis are presented in a significance-structured percentile table. The time courses of these cerebrospinal fluid properties reflect physiologic alterations of the blood-brain barrier function during childhood.
A new silver stain for electrophoretically separated polypeptides can be rapidly and easily used and can detect as little as 0.01 nanogram of protein per square millimeter. When employed with two-dimensional electrophoresis, it should permit qualitative and quantitative characterization of protein distributions in body fluids and tissues. It has been used to demonstrate regional variations in cerebrospinal fluid proteins.
Two-dimensional electrophoresis, with isoelectric focusing in the first dimension and sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the second, has been adapted for the high-resolution analysis of cerebrospinal fluid proteins. Proteins were detected with a new, highly sensitive silver stain that made visible more than 300 polypeptides from 60 microL of spinal fluid, in highly reproducible patterns. We have mapped these patterns, noting difference between the proteins observed in spinal fluid and plasma, and have prepared a partial map of cerebrospinal fluid proteins.
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