sclerosis/protease

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Prevention of acute autoimmune encephalomyelitis and abrogation of relapses in murine models of multiple sclerosis by the protease inhibitor D-penicillamine.

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The in vitro activity of gelatinase B, an enzyme whose appearance in the cerebrospinal fluid is associated with inflammatory diseases of the central nervous system, was dose-dependently inhibited by the antirheumatic D-penicillamine. Inhibition of gelatinase B in electrophoretically pure

Influence of ACTH on activity of some granulocytic proteases in patients with multiple sclerosis.

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The effect of treatment with ACTH on activity of granulocytic acid and neutral proteases in patients suffering from multiple sclerosis was studied. Protease activity was distinctly higher in granulocytes from patients. ACTH normalized the activities investigated in patients with exacerbating course

Neutral protease in cerebrospinal fluid from patients with multiple sclerosis and other neurological diseases.

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Neutral protease activity was significantly elevated in the cerebro-spinal fluid of patients with multiple sclerosis (MS) in exacerbation and in the acute phase of acute viral meningoencephalitis (AME) compared with that of MS in remission, amyotrophic lateral sclerosis or psychosomatic disease.

Von Willebrand factor cleaving protease (ADAMTS-13) in 123 patients with connective tissue diseases (systemic lupus erythematosus and systemic sclerosis).

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OBJECTIVE Autoantibodies inactivating the von Willebrand factor (VWF) cleaving protease, ADAMTS-13, are among the most frequent causes of thrombotic thrombocytopenic purpura (TTP). We evaluated whether or not ADAMTS-13 deficiency and autoantibodies inactivating the protease prevalent in patients

[Changes in the protease inhibitor activity of the blood serum in patients with disseminated sclerosis].

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Changes in the blood serum protease inhibitors activity alpha 1-antitrypsin and antithrombin III were studied in 60 patients with multiple sclerosis. The activity of the inhibitors under study was found to be dependent upon the severity of the pathological process as well as on the age of the

[Diagnostic and pathogenetic implications of the site specificity of antibody proteases in multiple sclerosis].

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Disseminated sclerosis is currently regarded as a CNS autoimmune disease. One of the mechanisms behind this pathology is antibody (AB) formation. In this context, recent data on AB with proteolytic activity are of importance because they participate in selective proteolysis of myelin proteins in

Polymorphonuclear neutral protease activity in multiple sclerosis and other diseases.

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Polymorphonuclear neutral protease activity (PMN-NPA) was examined in 87 patients with definite multiple sclerosis (MS) (48 active, 39 inactive), 49 patients with other neurological diseases (OND), 24 patients with immune-mediated non-neurological diseases (INND), and 32 normal subjects. PMN-NPA was

Differential expression of protease M/neurosin in oligodendrocytes and their progenitors in an animal model of multiple sclerosis.

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To determine the possible involvement of protease M/neurosin in demyelinating diseases of the CNS, we examined its expression in myelin oligodendrocyte glycoprotein (MOG)-induced experimental autoimmune encephalomyelitis (EAE), a recognized animal model of multiple sclerosis (MS). In situ

Serine proteases purified from sera of patients with amyotrophic lateral sclerosis (ALS) induce contrasting cytopathology in murine motoneurones to IgG.

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Affinity purified IgG from sera of patients with amyotrophic lateral sclerosis (ALS) is claimed to enhance transmitter release, induce apoptotic death of cultured motoneurones, and elicit a distinctive cytopathology with raised Ca(2+) in mouse motoneurones. An alternative hypothesis attributes these

Clinical significance of serum levels of secretory leukocyte protease inhibitor in patients with systemic sclerosis.

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We aimed to investigate the clinical significance of serum levels of secretory leukocyte protease inhibitor (SLPI), which is widely expressed in lung tissues and serves as a useful marker reflecting the activity of various lung diseases, in patients with systemic sclerosis (SSc). Serum SLPI levels

Autoantibody against a protease domain of caspase-8 in patients with systemic sclerosis.

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BACKGROUND Systemic sclerosis (SSc) is characterized by autoantibodies against various cellular components. OBJECTIVE To determine the presence or levels of antibodies (Abs) against a protease domain (PD) of caspase-8 and their clinical relevance in SSc. METHODS Anti-caspase-8 PD Ab was examined by

Occurrence of reduced alpha 2-macroglobulin and lowered protease inhibiting capacity in plasma of amyotrophic lateral sclerosis patients.

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Lowered levels of plasma alpha 2-macroglobulin were found in 13 patients with amyotrophic lateral sclerosis using anti-alpha 2-macroglobulin-embedded agar plates. Levels of this major protease inhibitor in ALS patients were contrasted with those in disease controls, consisting of patients with a

Elevated neutral protease activity in myelin from brains of patients with multiple sclerosis.

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Incubation of human myelin at neutral pH resulted in the proteolytic conversion of the myelin-associated glycoprotein to a lower molecular weight derivative (dMAG) and the degradation of basic protein. The formation of dMAG occurred much more rapidly than the degradation of basic protein. The

Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot.

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OBJECTIVE The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse

Cytoplasmic, lysosomal and matrix protease activities in spinal cord tissue from amyotrophic lateral sclerosis (ALS) and control patients.

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The histological identification of ubiquitin-conjugated protein deposits in spinal motor neurones of patients with amyotrophic lateral sclerosis (ALS) has suggested that an underlying abnormality of intracellular protein metabolism may be responsible for the pathogenesis of the disease. In an

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