Lysosomal hydrolases in cerebrospinal fluid of multiple sclerosis patients. A follow-up study. 1987

T Halonen, and H Kilpeläinen, and A Pitkänen, and P J Riekkinen

The change in activity of lysosomal hydrolases in the brain tissue of patients with demyelinating disease has been suggested to reflect the demyelination process. In this study we measured neutral proteinase (NP), acid proteinase (AP), and beta-glucuronidase (BG) activities in CSF of 32 patients with multiple sclerosis (MS) (remitting, remitting and relapsing, or chronic progressive course of the disease), 62 controls, and 4 patients with chronic inflammatory disease of central nervous system (ID). Samples from MS patients were taken at different clinical conditions of the disease during the 22-month follow-up. Elevated NP activity was found in patients with relapsing course of MS and also in patients with ID (P less than 0.05). NP activity correlated with the number of leucocytes in CSF of both MS (P less than 0.005, r = 0.50) and control (P less than 0.05, r = 0.21) patients. AP activity decreased in the MS group, especially in patients with remitting or remitting and relapsing courses of the disease (P less than 0.05), but even more in patients with ID (P less than 0.01). During the follow-up the increase in NP activity seemed to be associated with the clinical relapses of MS patients. Other enzymes did not fluctuate with the disease. This study suggests that the change in activity of lysosomal hydrolases is not specific for MS. The increase in NP activity in CSF is associated with clinical relapse of individual MS patients during the follow-up and may indicate immunological activation of the demyelination process in the brain. The large intra- and interindividual variation in enzyme activities in the CSF, however, makes the use of these enzymes difficult for diagnosis of MS and follow-up of MS activity.

UI MeSH Term Description Entries
D009103 Multiple Sclerosis An autoimmune disorder mainly affecting young adults and characterized by destruction of myelin in the central nervous system. Pathologic findings include multiple sharply demarcated areas of demyelination throughout the white matter of the central nervous system. Clinical manifestations include visual loss, extra-ocular movement disorders, paresthesias, loss of sensation, weakness, dysarthria, spasticity, ataxia, and bladder dysfunction. The usual pattern is one of recurrent attacks followed by partial recovery (see MULTIPLE SCLEROSIS, RELAPSING-REMITTING), but acute fulminating and chronic progressive forms (see MULTIPLE SCLEROSIS, CHRONIC PROGRESSIVE) also occur. (Adams et al., Principles of Neurology, 6th ed, p903) MS (Multiple Sclerosis),Multiple Sclerosis, Acute Fulminating,Sclerosis, Disseminated,Disseminated Sclerosis,Sclerosis, Multiple
D010450 Endopeptidases A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. Endopeptidase,Peptide Peptidohydrolases
D005500 Follow-Up Studies Studies in which individuals or populations are followed to assess the outcome of exposures, procedures, or effects of a characteristic, e.g., occurrence of disease. Followup Studies,Follow Up Studies,Follow-Up Study,Followup Study,Studies, Follow-Up,Studies, Followup,Study, Follow-Up,Study, Followup
D005966 Glucuronidase Endo-beta-D-Glucuronidase,Endoglucuronidase,Exo-beta-D-Glucuronidase,beta-Glucuronidase,Endo beta D Glucuronidase,Exo beta D Glucuronidase,beta Glucuronidase
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D015260 Neprilysin Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT. Antigens, CD10,Antigens, Leukemia, Common Acute Lymphoblastic,CALLA Antigen,CD10 Antigens,Common Acute Lymphoblastic Leukemia Antigens,Endopeptidase-24.11,Enkephalin Dipeptidyl Carboxypeptidase,Enkephalinase,Kidney-Brush-Border Neutral Proteinase,Membrane Metallo-Endopeptidase,Atriopeptidase,CD10 Antigen,Enkephalinase-24.11,Neutral Endopeptidase,Neutral Endopeptidase 24.11,Thermolysin-Like Metalloendopeptidase,YGG-Forming Enzyme,Antigen, CD10,Carboxypeptidase, Enkephalin Dipeptidyl,Dipeptidyl Carboxypeptidase, Enkephalin,Endopeptidase 24.11,Endopeptidase 24.11, Neutral,Endopeptidase, Neutral,Enkephalinase 24.11,Enzyme, YGG-Forming,Kidney Brush Border Neutral Proteinase,Membrane Metallo Endopeptidase,Metallo-Endopeptidase, Membrane,Metalloendopeptidase, Thermolysin-Like,Neutral Proteinase, Kidney-Brush-Border,Thermolysin Like Metalloendopeptidase,YGG Forming Enzyme
D016282 Aspartic Acid Endopeptidases A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity. Aspartic Endopeptidases,Aspartyl Endopeptidases,Acid Endopeptidases, Aspartic,Endopeptidases, Aspartic Acid,Endopeptidases, Aspartyl

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