Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1966 Jun 1;29(3):525–545. doi: 10.1083/jcb.29.3.525

NUCLEOSIDE PHOSPHATASE AND CHOLINESTERASE ACTIVITIES IN DORSAL ROOT GANGLIA AND PERIPHERAL NERVE

Alex B Novikoff 1, Nelson Quintana 1, Humberto Villaverde 1, Regina Forschirm 1
PMCID: PMC2106968  PMID: 4225492

Abstract

In dorsal root ganglia and peripheral nerve of the rat and other species, nucleoside phosphatase and unspecific cholinesterase reaction products are found in the plasma membranes and spaces between them at two sites: (1) Schwann cell-axon interfaces and mesaxons of unmyelinated fibers, and (2) sheath cell-perikaryon interfaces and interfaces between adjacent sheath cells. Acetylcholinesterase reaction product is found in the perikaryon (within the endoplasmic reticulum) and the axon (axoplasmic surface). Nucleoside phosphatase reaction product is also found in the numerous vacuoles at the surface of perineurium cells, ganglion sheath cells, and cells surrounding some ganglion blood vessels. Nucleoside phosphatase activities in the sections fail to respond, in the manner described for "transport ATPase," to diisopropylphosphofluoridate, sodium and potassium ions, and ouabain. Nucleoside diphosphates are hydrolyzed more slowly than triphosphates in unmyelinated fibers, and are not hydrolyzed at the perikaryon surface. Nucleoside monophosphates are either not hydrolyzed or hydrolyzed very slowly. In contrast to these localizations, which are believed to demonstrate sites of enzyme activity, it is considered likely that diffusion artifacts account for the nucleoside phosphatase reaction product frequently found along the outer surfaces of myelinated fibers and within vacuoles at the Schwann cell surfaces of these fibers. The diffuse reaction product seen in basement membranes of ganglion and nerve may also be artifact.

Full Text

The Full Text of this article is available as a PDF (2.4 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BONTING S. L., SIMON K. A., HAWKINS N. M. Studies on sodium-potassium-activated adenosine triphosphatase. I. Quantitative distribution in several tissues of the cat. Arch Biochem Biophys. 1961 Dec;95:416–423. doi: 10.1016/0003-9861(61)90170-9. [DOI] [PubMed] [Google Scholar]
  2. COLE D. F. LOCATION OF OUABAIN-SENSITIVE ADENOSINE TRIPHOSPHATASE IN CILIARY EPITHELIUM. Exp Eye Res. 1964 Mar;3:72–75. doi: 10.1016/s0014-4835(64)80009-9. [DOI] [PubMed] [Google Scholar]
  3. DUNHAM E. T., GLYNN I. M. Adenosinetriphosphatase activity and the active movements of alkali metal ions. J Physiol. 1961 Apr;156:274–293. doi: 10.1113/jphysiol.1961.sp006675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. EVANS D. H., MURRAY J. G. Histological and functional studies on the fibre composition of the vagus nerve of the rabbit. J Anat. 1954 Jul;88(3):320–337. [PMC free article] [PubMed] [Google Scholar]
  5. FUKUDA T., KOELLE G. B. The cytological localization of intracellular neuronal acetylcholinesterase. J Biophys Biochem Cytol. 1959 May 25;5(3):433–440. doi: 10.1083/jcb.5.3.433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. GLAUERT A. M., GLAUERT R. H. Araldite as an embedding medium for electron microscopy. J Biophys Biochem Cytol. 1958 Mar 25;4(2):191–194. doi: 10.1083/jcb.4.2.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. GOLDFISCHER S., ESSNER E., NOVIKOFF A. B. THE LOCALIZATION OF PHOSPHATASE ACTIVITIES AT THE LEVEL OF ULTRASTRUCTURE. J Histochem Cytochem. 1964 Feb;12:72–95. doi: 10.1177/12.2.72. [DOI] [PubMed] [Google Scholar]
  8. Goldfischer S. The cytochemical demonstration of lysosomal aryl sulfatase activity by light and electron microscopy. J Histochem Cytochem. 1965 Jul-Aug;13(6):520–523. doi: 10.1177/13.6.520. [DOI] [PubMed] [Google Scholar]
  9. HOKIN L. E., YODA A. INHIBITION BY DIISOPROPYLFLUOROPHOSPHATE OF A KIDNEY TRANSPORT ADENOSINE TRIPHOSPHATASE BY PHOSPHORYLATION OF A SERINE RESIDUE. Proc Natl Acad Sci U S A. 1964 Aug;52:454–461. doi: 10.1073/pnas.52.2.454. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Holtzman E., Novikoff A. B. Lysomes in the rat sciatic nerve following crush. J Cell Biol. 1965 Dec;27(3):651–669. doi: 10.1083/jcb.27.3.651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. KARNOVSKY M. J., ROOTS L. A "DIRECT-COLORING" THIOCHOLINE METHOD FOR CHOLINESTERASES. J Histochem Cytochem. 1964 Mar;12:219–221. doi: 10.1177/12.3.219. [DOI] [PubMed] [Google Scholar]
  12. KARNOVSKY M. J. THE LOCALIZATION OF CHOLINESTERASE ACTIVITY IN RAT CARDIAC MUSCLE BY ELECTRON MICROSCOPY. J Cell Biol. 1964 Nov;23:217–232. doi: 10.1083/jcb.23.2.217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. NOVIKOFF A. B., DRUCKER J., SHIN W. Y., GOLDFISCHER S. Further studies of the apparent adenosinetriphosphatase activity of cell membranes in formol-calcium-fixed tissues. J Histochem Cytochem. 1961 Jul;9:434–451. doi: 10.1177/9.4.434. [DOI] [PubMed] [Google Scholar]
  14. NOVIKOFF A. B., GOLDFISCHER S., ESSNER E. The importance of fixation in a cytochemical method for the Golgi apparatus. J Histochem Cytochem. 1961 Jul;9:459–460. doi: 10.1177/9.4.459. [DOI] [PubMed] [Google Scholar]
  15. NOVIKOFF A. B., GOLDFISCHER S. Nucleosidediphosphatase activity in the Golgi apparatus and its usefulness for cytological studies. Proc Natl Acad Sci U S A. 1961 Jun 15;47:802–810. doi: 10.1073/pnas.47.6.802. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. NOVIKOFF A. B., MASEK B. Survival of lactic dehydrogenase and DPNH-diaphorase activities after formol-calcium fixation. J Histochem Cytochem. 1958 May;6(3):217–217. doi: 10.1177/6.3.217. [DOI] [PubMed] [Google Scholar]
  17. OSTROWSKI K., BARNARD E. A. Application of isotopically labelled specific inhibitors as a method in enzyme cytochemistry. Exp Cell Res. 1961 Nov;25:465–468. doi: 10.1016/0014-4827(61)90298-1. [DOI] [PubMed] [Google Scholar]
  18. POST R. L., MERRITT C. R., KINSOLVING C. R., ALBRIGHT C. D. Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte. J Biol Chem. 1960 Jun;235:1796–1802. [PubMed] [Google Scholar]
  19. REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. ROSENBLUTH J. Subsurface cisterns and their relationship to the neuronal plasma membrane. J Cell Biol. 1962 Jun;13:405–421. doi: 10.1083/jcb.13.3.405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. ROSTGAARD J., BARRNETT R. J. FINE STRUCTURE LOCALIZATION OF NUCLEOSIDE PHOSPHATASES IN RELATION TO SMOOTH MUSCLE CELLS AND UNMYELINATED NERVES IN THE SMALL INTESTINE OF THE RAT. J Ultrastruct Res. 1964 Aug;11:193–207. doi: 10.1016/s0022-5320(64)80103-9. [DOI] [PubMed] [Google Scholar]
  22. SABATINI D. D., BENSCH K., BARRNETT R. J. Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J Cell Biol. 1963 Apr;17:19–58. doi: 10.1083/jcb.17.1.19. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. TORACK R. M., BARRNETT R. J. Fine structural localization of cholinesterase activity in the rat brain stem. Exp Neurol. 1962 Sep;6:224–244. doi: 10.1016/0014-4886(62)90004-3. [DOI] [PubMed] [Google Scholar]
  24. WACHSTEIN M., MEISEL E. Histochemistry of hepatic phosphatases of a physiologic pH; with special reference to the demonstration of bile canaliculi. Am J Clin Pathol. 1957 Jan;27(1):13–23. doi: 10.1093/ajcp/27.1.13. [DOI] [PubMed] [Google Scholar]
  25. WATSON M. L. Staining of tissue sections for electron microscopy with heavy metals. J Biophys Biochem Cytol. 1958 Jul 25;4(4):475–478. doi: 10.1083/jcb.4.4.475. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES