Modulation of ATPase activities in the central nervous system by the S-100 proteins.
The isomeric forms of bovine S-100a and S-100b have been shown to stimulate ATPase activities in fractions enriched in myelin and mitochondria isolated from the Gerbil brain and for S-100b more effectively than for calmodulin in erythrocytes or skeletal muscle. In the presence of Ca2+, S-100a produced a slight increase of ATPase activity in the mitochondrial fraction. However, S-100b in the presence of Zn2+ almost doubled the ATPase activity in brain myelin. S-100a, or S-100b, with or without Ca2+ and Zn2+ respectively, had no effect on the ATPase activity in mitochondria of the Gerbil liver. The observations may indicate a "second messenger" role for S-100b in the presence of Zn2+ in the Schwann cell.
Simonian
A
A
Institute of Biochemistry, Academy of Sciences of Armenian SSR, Yerevan.
Baudier
J
J
Haglid
K G
KG
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D015415:Biomarkers; D001921:Brain / Q000201:enzymology*; D002135:Calcium-Binding Proteins / Q000502:physiology*; D005849:Gerbillinae; D008099:Liver / Q000201:enzymology; D008297:Male; D009414:Nerve Growth Factors; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins / Q000502:physiology*; D013347:Subcellular Fractions / Q000201:enzymology
D015415:Biomarkers; D002135:Calcium-Binding Proteins; D009414:Nerve Growth Factors; C030564:S-100 calcium-binding protein alpha subunit; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins; D000251:Adenosine Triphosphatases