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PubMed1980

Isoelectric focusing of cerebrospinal fluid proteins in ischemic cerebrovascular disease.

The cerebrospinal fluid (CSF) protein patterns, in ischemic cerebrovascular disease (ICD), of varying extension were studied by isoelectric focusing (IEF) in 100 patients at different intervals after the onset of symptoms. The diagnoses were based on conventional clinical examinations and CSF spectrophotometry in all cases. Computed tomography was performed on 52 cases. One or more CSF protein aberrations were noted in 94 patients. Some of these findings were most common with small lesions including TIA. Other aberrations were most frequent with the more extensive infarctions. A regional increase in the gammaglobulin range was found in six cases. The findings were most frequent in the first days after the stroke except for barrier damage which reached a maximum during the second week. The IEF findings of CSF seem to be of diagnostic value. Taken together with the clinical signs and CT findings, they could conceivably give prognostic information.

Adult↗
PubMedDate not supplied

Interpretation of cerebrospinal fluid proteins by gel electrophoresis.

The use of polyacrylamide gel electrophoresis (PAGE) for the separation of proteins in cerebrospinal fluid (CSF) results in greater definition than does a "routine" method such as cellulose acetate electrophoresis. Unconcentrated CSF is easily separated into as many as 18 bands by the use of PAGE. By means of a modified PAGE method described in this paper, unconcentrated and untreated CSF is quickly and conveniently analyzed for protein constituents. This modification involves a continuous buffer environment, a pore-size concentration gradient and CSF in amounts of 0.1 to 0.4 ml. Sucrose addition is not necessary in this procedure. Whereas most central nervous system (CNS) disease states do not yield consistently distinctive protein patterns, some diseases, such as vascular disease, infectious meningitis and some metastatic tumors, yield significantly altered patterns. It is suggested that the chief value of CSF protein electrophoresis at the present time is to follow the course of a CNS disease.

Buffers↗
PubMed1975

[Behavior of cerebrospinal fluid proteins in degenerative diseases].

132 cerebrospinals fluids from patients with degenerative diseases of the central nervous system have been analyzed for protein distribution in agar gel electrophoresis. After subdivision into diagnostically well defined groups these patients were compared with 48 with metabolic and psychiatric diseases and with 79 normal controls. The majority of diagnostic groups showed a tendency to permeability impairment. Other outstanding deviations were not found, except for single cases which were not statistically typical of the groups as a whole. However, the "degenerative type" of proteinogram emphasized in the literature predominated not only in the degenerative groups but also in certain other diseases with destruction of central nervous tissue which do not belong to the degenerative diseases in the strict sense. On the other hand, there are some degenerative subgroups without this "typical" electrophoretic pattern. There would thus appear to be grounds for amending the term "degenerative" into "tissue destroying" or "atrophic type", to avoid misinterpretation.

Alpha-Globulins↗
PubMed1976

Electrophoresis of normal lumbar cerebrospinal fluid proteins in the African.

Lumbar cerebrospinal fluid obtained from Zambian patients suspected of suffering from central nervous system conditions was concentrated over a hundred-fold and subjected to small-scale cellulose acetate electrophoresis (Millipore). The percentage of each protein fraction was determined by scanning. Only twenty samples were considered normal out of a total of 150 studies. These normal values were not statistically different from those of published data on Europeans and North American Caucasians. The high serum gamma globulin in African subjects is not reflected in the cerebrospinal fluid.

Adolescent↗
PubMed1995

Separation of cerebrospinal fluid proteins using capillary electrophoresis: a potential method for the diagnosis of neurological disorders.

A method for the analysis of proteins in cerebrospinal fluid (CSF) using free solution capillary electrophoresis (FSCE) was developed, in which the adsorption of proteins to the fused silica capillary wall was virtually eliminated. FSCE was carried out on 30 randomly selected CSF samples. Good sensitivity and resolution was obtained with minimal baseline noise. These preliminary results clearly demonstrated the potential of FSCE to analyse proteins in CSF, both qualitatively and quantitatively more rapidly than has been possible hitherto. A total run time of approximately 30 min allowed between 20 to 25 peaks to be separated. Many peaks with long migration times were detected in CSF that appeared to be specific since they were not detectable in corresponding serum samples. The separation patterns for most of the CSF samples selected showed relatively similar patterns but there were often minor qualitative and quantitative differences. Four CSF samples showed patterns that were significantly different from the others, primarily in the peaks with long migration times. A larger clinical study is now being undertaken.

Adsorption↗
PubMed1986

Electrophoresis and immunoblot of cerebrospinal fluid proteins in spasmodic torticollis.

Protein patterns of cerebrospinal fluid (CSF) from patients with spasmodic torticollis (ST) were investigated to determine whether abnormalities previously reported could be detected and further identified. CSF was collected from 12 patients with ST and 6 normal controls. The CSF proteins were analyzed using sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis and silver staining. In 11 of the 12 patients with ST, a CSF protein pattern was observed which differed from that in the controls. The identity of the abnormal proteins was ascertained by blotting and immunostaining with specific antisera to IgG and ceruloplasmin (Cp). CSF from 2 of 12 patients had distinct bands staining for IgG and 7 had abnormal immunostaining for Cp.

Adult↗
PubMed1987

Cerebrospinal fluid proteins studied by two-dimensional gel electrophoresis and immunoblotting technique.

The proteins of lumbar CSF have been investigated by two-dimensional gel electrophoresis, and their patterns have been compared with the corresponding serum protein patterns. Serum proteins in CSF have been identified by electroblotting and immunoreaction with antiserum against total human serum proteins. Proteins derived from brain have been identified with antiserum against human brain proteins. The most prominent CSF protein group has been identified as a multiple form of apolipoprotein E. The correct position of the glial fibrillary acidic protein has also been determined. The prefractionation of CSF proteins by size exclusion chromatography or by affinity chromatography followed by two-dimensional electrophoresis has facilitated the detection of trace components in CSF and the corresponding serum.

Blood Proteins↗
PubMed1980

Serum and cerebrospinal fluid proteins in tuberculous meningitis.

Serum and CSF protein electrophoresis was performed on cellulose acetate in 8 controls and 30 cases of tuberculous meningitis before treatment and during a hospitalization period of 5 months. The analysis of the CSF electrophoretic pattern showed that abnormalities in the prealbumin, beta and gamma fractions may still exist as late as 5 months after initiation of treatment. An increase in alpha 2 and decrease in the albumin fractions in the serum also persisted. Treatment for 20 weeks improved the clinical condition of the patients and resulted in a significant improvement in the CSF prealbumin and alpha 1 fractions. These findings indicate that changes in these fractions may be considered a good prognostic aid.

Adolescent↗
PubMed1983

[Cerebrospinal fluid proteins: II. Normal values of protein fractions obtained by electrophoresis (variations related to race, sex and age)].

The total protein content and protein fractions, obtained by electrophoresis on cellulose acetate strips, of CSF collected from the cisterna magna of 213 patients (with no neurological diseases) were determined in order to verify variations related to race, sex and age, as well as to establish the proteinogram normal limits. No differences between caucasians and coloured persons were observed with respect to CSF total protein and protein fractions. Children (5 months to 11 years old) do not present differences related to sex or age, on their proteinogram. Children's CSF total protein, relative values of pre-albumin, alpha 1--and beta-globulins, absolute values of albumin, alfa 2--, beta--, tau --and gamma-globulins, differ from those found in adults. Differences between males and females in the normal CSF proteinogram were found in adults. As a consequence of these findings, the CSF proteinogram normal limits for children, males and females were separately established. In adults, statistically significant positive correlation between age and the 7 protein fractions when expressed in mg/100 ml were observed, as well as between age and total protein. Comparison of the results obtained in this research with those found in some publications was carried out and is briefly discussed.

Adolescent↗
PubMedDate not supplied

Two-dimensional polyacrylamide gel electrophoresis of serum and cerebrospinal fluid proteins in multiple sclerosis and subacute sclerosing panencephalitis.

Serum and cerebrospinal fluid (CSF) proteins in multiple sclerosis (MS) and subacute sclerosing panencephalitis (SSPE) were fractionated by means of two dimensional polyacrylamide gel electrophoresis. At the same time, separations of serum and CSF proteins of control cases were made. Some major differences were observed between the patterns obtained for MS serum and those obtained for normal and SSPE serum: for MS serum one extra specific group of proteins was located in the more acidic area of the gel. In the case of CSF protein separations, MS and SSPE showed common features remarkably different from normal: the disappearance of a specific CSF 38,000 dalton group of proteins and the fractionation of proteins into many discrete spots in the chi and lambda light chain region after two dimensional electrophoresis. The latter correlates with the presence of oligoclonal immunoglobulins in the CSF. In addition, in SSPE CSF, there appear 4 to 5 proteins which cannot be detected elsewhere (nor in normal CSF nor in CSF from various neurological diseases). Identification of these proteins has not yet been made.

Blood Proteins↗
PubMed1992

Human cerebrospinal fluid protein database: edition 1992.

Two-dimensional electrophoresis maps of human cerebrospinal fluid proteins are presented in the form of labeled images. 931 protein spots are identified in spinal fluid from a normal volunteer. Distinct spots that represent variants of the same protein, especially posttranslational modifications, are estimated to reduce the 931 different spots to < 200 different proteins. 248 spots of 29 protein groups have been identified and are indicated on enlargements of specific gel regions. The distribution of protein abundance, mass, charge and shape characteristics of these normal 931 spinal fluid spots are graphically profiled. Analysis of the shape parameter "vertical height: width ratio" reveals that a ratio > 3.5 correlates with glycoproteins, enabling their identification simply by image analysis. Proteins that are not present on the normal map, but appear in spinal fluid in patients with schizophrenia and Creutzfeldt-Jakob disease are illustrated on additional maps.

Cerebrospinal Fluid Proteins↗
PubMed1998

[Cerebrospinal fluid proteins in the diagnosis of disorders of the blood-cerebrospinal fluid barrier in central nervous system diseases].

BACKGROUND: Many neurological diseases are connected with the dysfunction of blood-CSF barrier. The quantitative determination of CSF proteins has already been used in the diagnosis of barrier impairments and inflammatory diseases of the central nervous system. PATIENTS: Serum and CSF, totaling 264 samples, were obtained from 15 controls and 117 patients with various diseases of the nervous system. Laurell's electroimmunoassay was used for estimation of albumin and IgG levels in serum and CSF. CSF-protein profile was evaluated according to Reiber's graph for the evaluation of the CSF-protein profile. RESULTS: The graph for the protein profile can be divided into 5 functionally different parts (1--normal range, 2, 3, 4--different types of barrier dysfunctions and 5--local humoral response in CNS without any barrier impairment). There was a good correlation of CSF-protein profiles and neurological diseases in our group of patients. CONCLUSIONS: According to our results, Reiber's graph was helpful for the diagnosis of blood-CSF-barrier dysfunctions. The graph has the following advantages: a) possibility of simultaneous assessment of the functional state of blood-CSF-barrier and the inflammatory response of the CNS, b)sensitivity for the determination of pathological local IgG-production in CNS and c) minimal number of protein assays necessary.

Blood-Brain Barrier↗