ABSTRACT
A 45-year-old man with multiple symmetric lipomatosis suffered recurrent syncope attributed to carotid sinus syndrome caused by extrinsic compression of the carotid body by the lipomatous masses. Surgical removal reduced but did not stop syncope, which was then controlled by implantation of a DDD pacemaker.
Subject(s)
Carotid Sinus/physiopathology , Lipomatosis, Multiple Symmetrical/complications , Reflex, Abnormal/physiology , Syncope/etiology , Constriction, Pathologic/diagnosis , Constriction, Pathologic/etiology , Humans , Male , Middle Aged , Pacemaker, Artificial , Recurrence , Syncope/prevention & control , SyndromeABSTRACT
The optimal assay conditions and the stability of the following enzymes of lysosomal origin in human cerebrospinal fluid (CSF) were studied: acid phosphatase, beta-D-N-acetylglucosaminidase, alpha-D-galactosidase, beta-D-galactosidase, alpha-D-glucosidase, beta-D-glucosidase, alpha-L-fucosidase, alpha-D-mannosidase, beta-D-glucuronidase. The microsomal alpha-D-mannosidase, pH 5.7, was used as a reference non-lysosomal glycohydrolase. All the examined enzymes, with the only exception of beta-D-glucuronidase, underwent a more or less rapid loss of activity upon CSF storage in the temperature range from 37 degrees C to -80 degrees C. Storage in liquid nitrogen (-196 degrees C) was the only condition in which full activity for all tested enzymes was maintained for at least 15 days. Addition of human serum albumin to CSF, immediately after withdrawal, had a double effect in favouring enzyme stabilization and causing enzyme activation in some cases, and enzyme inhibition in others. Using conditions warranting enzyme stability the fluorimetric methods for lysosomal enzymes determination in cerebrospinal fluid appear to be highly reproducible (CV less than 5%) and simple enough for routine use.
Subject(s)
Hydrolases/cerebrospinal fluid , Lysosomes/enzymology , Adult , Enzyme Stability , Humans , Middle Aged , Reference Values , Specimen Handling , Spectrometry, Fluorescence , TemperatureABSTRACT
The specific activities of five glycohydrolases of lysosomal origin (beta-N-acetylglucosaminidase, beta-glucuronidase, beta-galactosidase, alpha-mannosidase and alpha-fucosidase) were measured in different types of primary and metastatic tumors of the human nervous system. The activities of these hydrolytic enzymes in samples of tumor tissue were compared with those in the white matter of 'control' tissue. The specific activities of beta-glucuronidase and beta-N-acetylglucosaminidase were significantly higher (P less than 0.001) in each group of tumors than in normal cerebral matter. The activities of the other hydrolases were sometimes significantly increased in primary tumors, but not always. In metastatic tumors, they were also significantly higher (P less than 0.01).
Subject(s)
Brain Neoplasms/enzymology , Glycoside Hydrolases/analysis , Lysosomes/enzymology , Acetylglucosaminidase/analysis , Adolescent , Adult , Child , Female , Glucuronidase/analysis , Glycosphingolipids/analysis , Humans , Male , Middle AgedABSTRACT
Myopatic changes observed in muscle of rats after abdominal aorta ligation and/or serotonin injection have been regarded as a suitable model to explore the possibility that vasoactive treatments induce muscular damage similar to human myopathies. In the present study, we investigated the effect of serotonin administration to normal and aorta-ligated rats on cAMP-dependent protein-kinase (PK) and hydrolytic enzymes in skeletal muscle.
