Ribonuclease activities in various classes of nuclei from bovine cerebrum.
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Biomedical subjects
Publications and source records attributed to P Mandel.
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Arylsulfatases A, B, and C, beta-galactosidase, and acid phosphatase were assayed in neuronal, astroglial, and oligodendroglial fractions isolated from adult rabbit and beef brains. The specific activities of all acid hydrolases were lower in beef cells compared to rabbit cells. The lysosomal enzymes of the rabbit neuronal fraction showed 10--25 time higher activities than the oligodendroglial fraction and 5-fold higher activities than the astroglial fraction. In beef brain, the specific activities of these enzymes were similar in oligodendroglia and astrocytes but 4--10 times lower than in neurons. The low activity of arylsulfatase A and beta-galactosidase in oligodendroglial cells may suggest that the low turnover of cerebroside and sulfatide in myelin may be regulated in part by the enzymes that catalyze their degradation.
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A stereospecific saturable high affinity binding of 3H-naloxone has been found in 3 glial and 2 neuronal cell lines. Kinetic study of binding seems to indicate only one class of receptor sites in the 5 cell lines. Acute exposure to morphine (1 X 10(-5)M) concurrent with PGE1-induced stimulation of adenylate cyclase did not result in a decrease of the cAMP level in any cell line tested.
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Important amounts of nicotinic acid appear in the growth medium of neuroblastoma cell cultures. It is shown that an enzyme released by the cells into the growth medium deamidates the nicotinamide supplied by the growth medium to nicotinic acid.
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