Regional Cyclic Nucleotide Phosphodiesterase Activity in Cat Central Nervous System: Effects of Benzodiazepines

1974 ◽  
Vol 145 (2) ◽  
pp. 407-410 ◽  
Author(s):  
C. Dalton ◽  
H. J. Crowley ◽  
H. Sheppard ◽  
W. Schallek
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Cyclic Nucleotide ◽  
Cyclic Nucleotide Phosphodiesterase ◽  
Phosphodiesterase Activity

scholarly journals Photoaffinity labelling of central-nervous-system myelin. Evidence for an endogenous type I cyclic AMP-dependent kinase phosphorylating the larger subunit of 2′,3′-cyclic nucleotide 3′-phosphodiesterase

1984 ◽  
Vol 221 (2) ◽  
pp. 361-368 ◽  
Author(s):  
J M Bradbury ◽  
R J Thompson
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Cyclic Nucleotide ◽  
Type I ◽  
Phosphodiesterase Activity ◽  
Dependent Protein Kinase ◽  
Photoaffinity Labelling ◽  
Dependent Protein

Endogenous cyclic AMP-stimulated phosphorylation of a 49700-Mr Wolfgram protein component in rabbit central nervous system was investigated by using photoaffinity labelling and 2′,3′-cyclic nucleotide 3′-phosphodiesterase activity staining after electroblotting on to nitrocellulose paper. Photoaffinity labelling with 8′-azidoadenosine 3′,5′-cyclic monophosphate showed a cyclic AMP-binding protein that appeared to be intrinsic to the myelin membrane and appeared to represent the R-subunit of a type I cyclic AMP-dependent protein kinase. This photoaffinity-labelled protein was of larger apparent Mr than the protein showing cyclic AMP-stimulated phosphorylation. Blotting of one-dimensional sodium dodecyl sulphate/polyacrylamide-gel electrophoretograms followed by staining for 2′,3′-cyclic nucleotide 3′-phosphodiesterase activity showed two activity bands corresponding to the two components of the Wolfgram protein doublet. Cyclic AMP-stimulated protein phosphorylation corresponded to the upper component of this doublet. Electroblotting of two-dimensional non-equilibrium pH-gradient electrophoretograms also showed co-migration of cyclic AMP-stimulated protein phosphorylation with enzyme activity. It is proposed that central-nervous-system myelin contains an endogenous type I cyclic-AMP dependent protein kinase that phosphorylates the larger subunit of 2′,3′-cyclic nucleotide 3′-phosphodiesterase.

Calmodulin-binding peptides isolated from α-casein peptone

1995 ◽  
Vol 62 (4) ◽  
pp. 587-592 ◽  
Author(s):  
Kenji Kizavva ◽  
Keiko Naganuma ◽  
Umeji Murakami
Keyword(s):  
Enzyme Activity ◽  
Cyclic Nucleotide ◽  
Cyclic Nucleotide Phosphodiesterase ◽  
Phosphodiesterase Activity ◽  
Calmodulin Binding ◽  
C Terminus ◽  
Binding Peptides

SUMMARYPeptides that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase were isolated from a pepsin digest of α-casein. Analysis of these peptides showed that they corresponded to the αs2-casein sequences 164–179 (Leu–Lys–Lys–Ile–Ser–Gln–Arg–Tyr–Gln–Lys–Phe–Ala–Leu–Pro–Gln–Tyr), 183–206 (Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr) and 183–207 (C-terminus, Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr–Leu). These peptides inhibited calmodulin-induced cyclic nucleotide phosphodiesterase activity over the range 1–50 μM without affecting the basal enzyme activity. These results demonstrated that the affinities of these peptides for calmodulin are comparable to the affinities of certain endogenous neurohormones and proteins that interact with calmodulin.

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