CHOLINESTERASES OF CEREBROSPINAL FLUID: DATA FOR NORMAL FLUIDS AND FLUIDS FROM PATIENTS WITH SYPHILIS, MENINGITIS, OR POLIOMYELITIS

1949 ◽  
Vol 27e (6) ◽  
pp. 327-340 ◽  
Author(s):  
K. G. Colling ◽  
R. J. Rossiter

In confirmation of the work of others it has been shown that the principal enzyme in human cerebrospinal fluid that can hydrolyze acetylcholine is true cholinesterase. There is in addition a lesser quantity of pseudocholinesterase. The true cholinesterase, but not the pseudocholinesterase, was found to be significantly increased in the spinal fluids of patients with syphilis, while the pseudocholinesterase, and not the true cholinesterase, was increased in the fluids of patients with either meningitis or poliomyelitis. The true cholinesterase activity was correlated neither with the protein concentration nor with the cell count, while the pseudocholinesterase was correlated with the protein concentration and less significantly with the cell count. When correction was made for the correlation between cell count and protein concentration, the correlation between pseudocholinesterase activity and protein concentration remained statistically significant, but that between pseudocholinesterase and cell count became of dubious significance. In pathological conditions it appears unlikely that either true cholinesterase or pseudocholinesterase is derived from the white cells in the fluid. It is possible that the increased pseudocholinesterase comes from the blood plasma as a result of an increase in the permeability of the "plasma–spinal fluid barrier" and that the increased true cholinesterase comes from the substance of the brain or spinal cord. For the pathological conditions studied, the determination of true and pseudocholinesterase activity of the spinal fluid would be of little value as a diagnostic aid.

1972 ◽  
Vol 18 (12) ◽  
pp. 1475-1477 ◽  
Author(s):  
G T Vatassery ◽  
G A Mortenson

Abstract Methods are reported for the manual spectrophotometric or fluorometric estimation of tocopherol in human cerebrospinal fluid. The fluid is centrifuged, an equal volume of ethanol is added, and the tocopherol is extracted with hexane, which is then used for the direct estimation by fluorometry. The fluorescence of tocopherol is significantly affected by the proportion of ethanol in the hexane solvent. The standards used for comparison should therefore be dissolved in hexane that had been previously equilibrated with twice its volume of ethanol:water (1:1 by vol). For spectrophotometry, the original hexane extract is dried at 40°C under reduced pressure, the residue dissolved in hexane, and color developed by adding bathophenanthroline, ferric chloride, and orthophosphoric acid. The color is measured at 536 nm. Concentrations of tocopherol in the spinal fluid samples analyzed so far ranged from 40 to 210 µg/ liter.


2010 ◽  
Vol 6 ◽  
pp. S500-S500
Author(s):  
Liang Ye ◽  
Tina Li ◽  
Daniel Lee ◽  
Curtis Huang ◽  
Chenbing Guan ◽  
...  

2019 ◽  
Vol 20 (12) ◽  
pp. 2982 ◽  
Author(s):  
Gil Yong Park ◽  
Angelo Jamerlan ◽  
Kyu Hwan Shim ◽  
Seong Soo A. An

Transthyretin (TTR) is a thyroid hormone-binding protein which transports thyroxine from the bloodstream to the brain. The structural stability of TTR in tetrameric form is crucial for maintaining its original functions in blood or cerebrospinal fluid (CSF). The altered structure of TTR due to genetic mutations or its deposits due to aggregation could cause several deadly diseases such as cardiomyopathy and neuropathy in autonomic, motor, and sensory systems. The early diagnoses for hereditary amyloid TTR with cardiomyopathy (ATTR-CM) and wild-type amyloid TTR (ATTRwt) amyloidosis, which result from amyloid TTR (ATTR) deposition, are difficult to distinguish due to the close similarities of symptoms. Thus, many researchers investigated the role of ATTR as a biomarker, especially its potential for differential diagnosis due to its varying pathogenic involvement in hereditary ATTR-CM and ATTRwt amyloidosis. As a result, the detection of ATTR became valuable in the diagnosis and determination of the best course of treatment for ATTR amyloidoses. Assessing the extent of ATTR deposition and genetic analysis could help in determining disease progression, and thus survival rate could be improved following the determination of the appropriate course of treatment for the patient. Here, the perspectives of ATTR in various diseases were presented.


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