Activity of cyclic AMP phosphodiesterases and adenylyl cyclase in peripheral nerve after crush and permanent transection injuries. 1998

R S Walikonis, and J F Poduslo
Department of Neurology, Mayo Clinic and Mayo Foundation, Rochester, Minnesota 55905, USA.

Recent studies demonstrate that cAMP levels are tightly controlled during demyelination and remyelination in Schwann cells as cAMP decreases to 8-10% of normal following both sciatic nerve crush or permanent transection injury and only begins to increase in the crushed nerve after remyelination (Poduslo, J. F., Walikonis, R. S., Domec, M., Berg, C. T., and Holtz-Heppelmann, C. J. (1995) J. Neurochem. 65, 149-159). To investigate the mechanisms responsible for this change in cAMP levels, cAMP phosphodiesterase (PDE) and adenylyl cyclase activities were determined before and after sciatic nerve injury. Basal cAMP PDE activity in soluble endoneurial homogenates of normal nerve was 34.9 +/- 1.9 pmol/mg of protein/min (chi +/- S.E.; n = 10). This activity increased about 3-fold within 6 days following both injuries. Basal PDE activity remained elevated in the transected nerve, but declined to 70 pmol/mg of protein/min in the crushed nerve at 21 and 35 days following injury. Isozyme-specific inhibitors and stimulators were used to identify the PDE families in the sciatic nerve. The low Km cAMP-specific (PDE4) and the Ca2+/calmodulin-stimulated (PDE1) families were found to predominate in assays using endoneurial homogenates. The PDE4 inhibitor rolipram also increased cAMP levels significantly after incubation of endoneurial tissue with various isozyme-specific inhibitors, indicating that PDE4 plays a major role in determining cAMP levels. PDE4 mRNA was localized by in situ hybridization to cells identified as Schwann cells by colabeling of S100, a Schwann cell specific protein. Adenylyl cyclase activity declined following injury, from 3.7 pmol/mg of protein/min in normal nerve to 0.70 pmol/mg/min by 7 days following injury. Both decreased synthesis and increased degradation contribute, therefore, to the reduced levels of cAMP following peripheral nerve injury and are likely critical to the process of Wallerian degeneration.

UI MeSH Term Description Entries
D008297 Male Males
D009186 Myelin Sheath The lipid-rich sheath surrounding AXONS in both the CENTRAL NERVOUS SYSTEMS and PERIPHERAL NERVOUS SYSTEM. The myelin sheath is an electrical insulator and allows faster and more energetically efficient conduction of impulses. The sheath is formed by the cell membranes of glial cells (SCHWANN CELLS in the peripheral and OLIGODENDROGLIA in the central nervous system). Deterioration of the sheath in DEMYELINATING DISEASES is a serious clinical problem. Myelin,Myelin Sheaths,Sheath, Myelin,Sheaths, Myelin
D009409 Nerve Crush Treatment of muscles and nerves under pressure as a result of crush injuries. Crush, Nerve
D009416 Nerve Regeneration Renewal or physiological repair of damaged nerve tissue. Nerve Tissue Regeneration,Nervous Tissue Regeneration,Neural Tissue Regeneration,Nerve Tissue Regenerations,Nervous Tissue Regenerations,Neural Tissue Regenerations,Regeneration, Nerve,Regeneration, Nerve Tissue,Regeneration, Nervous Tissue,Regeneration, Neural Tissue,Tissue Regeneration, Nerve,Tissue Regeneration, Nervous,Tissue Regeneration, Neural
D009418 S100 Proteins A family of highly acidic calcium-binding proteins found in large concentration in the brain and believed to be glial in origin. They are also found in other organs in the body. They have in common the EF-hand motif (EF HAND MOTIFS) found on a number of calcium binding proteins. The name of this family derives from the property of being soluble in a 100% saturated ammonium sulfate solution. Antigen S 100,Nerve Tissue Protein S 100,S100 Protein,S-100 Protein,S100 Protein Family,Protein, S100,S 100 Protein
D010727 Phosphoric Diester Hydrolases A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4. Phosphodiesterase,Phosphodiesterases,Hydrolases, Phosphoric Diester
D011760 Pyrrolidinones A group of compounds that are derivatives of oxo-pyrrolidines. A member of this group is 2-oxo pyrrolidine, which is an intermediate in the manufacture of polyvinylpyrrolidone. (From Merck Index, 11th ed) Pyrrolidinone,Pyrrolidone,Pyrrolidones
D012016 Reference Values The range or frequency distribution of a measurement in a population (of organisms, organs or things) that has not been selected for the presence of disease or abnormality. Normal Range,Normal Values,Reference Ranges,Normal Ranges,Normal Value,Range, Normal,Range, Reference,Ranges, Normal,Ranges, Reference,Reference Range,Reference Value,Value, Normal,Value, Reference,Values, Normal,Values, Reference
D000242 Cyclic AMP An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH. Adenosine Cyclic 3',5'-Monophosphate,Adenosine Cyclic 3,5 Monophosphate,Adenosine Cyclic Monophosphate,Adenosine Cyclic-3',5'-Monophosphate,Cyclic AMP, (R)-Isomer,Cyclic AMP, Disodium Salt,Cyclic AMP, Monoammonium Salt,Cyclic AMP, Monopotassium Salt,Cyclic AMP, Monosodium Salt,Cyclic AMP, Sodium Salt,3',5'-Monophosphate, Adenosine Cyclic,AMP, Cyclic,Adenosine Cyclic 3',5' Monophosphate,Cyclic 3',5'-Monophosphate, Adenosine,Cyclic Monophosphate, Adenosine,Cyclic-3',5'-Monophosphate, Adenosine,Monophosphate, Adenosine Cyclic
D000262 Adenylyl Cyclases Enzymes of the lyase class that catalyze the formation of CYCLIC AMP and pyrophosphate from ATP. Adenyl Cyclase,Adenylate Cyclase,3',5'-cyclic AMP Synthetase,Adenylyl Cyclase,3',5' cyclic AMP Synthetase,AMP Synthetase, 3',5'-cyclic,Cyclase, Adenyl,Cyclase, Adenylate,Cyclase, Adenylyl,Cyclases, Adenylyl,Synthetase, 3',5'-cyclic AMP

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