Endopeptidase-24.11 is suppressed in myelin-forming but not in non-myelin-forming Schwann cells during development of the rat sciatic nerve.
Endopeptidase-24.11, which is identical with the common acute lymphoblastic leukemia antigen (CALLA), is a cell surface zinc metalloprotease that has the ability to hydrolyse a variety of physiologically active peptides. Interest in this enzyme is based on the view that it may play a role in the regulation of peptide signals in different tissues, including the nervous and immune systems. We have previously shown that endopeptidase-24.11 is present in Schwann cells in the peripheral nervous system of newborn pigs [Kioussi C. and Matsas R. (1991) J. Neurochem. 57, 431-440]. In the present study we have investigated the developmental expression of the endopeptidase by Schwann cells in the rat sciatic nerve, from embryonic day 16 to maturity. Endopeptidase-24.11 was monitored enzymatically as well as by immunoblotting and immunocytochemistry using the monoclonal anti-endopeptidase antibody 23B11. We found an age-dependent decline in both the enzyme activity and the levels of immunoreactive protein. Endopeptidase-24.11 was first detected at embryonic day 18 and was present in all neonatal and early postnatal Schwann cells. However, as myelination proceeded the endopeptidase was gradually suppressed in the majority of cells that form myelin but retained in non-myelin-forming cells in the adult animal. At this stage, only very few large diameter myelinated fibers expressed weakly endopeptidase-24.11. Schwann cells dissociated from postnatal day 5 nerves and cultured up to one week in the absence of axons expressed endopeptidase-24.11. These results show that the endopeptidase has a distinct developmental profile in the rat sciatic nerve, similar to that of a group of other Schwann cell surface antigens, including the cell adhesion molecules N-CAM and L1 and the nerve growth factor receptor. We suggest that, as is the case with these antigens, endopeptidase-24.11 may play a role in nerve development and/or regeneration. In addition, persistence of endopeptidase-24.11 in a minority of adult myelin-forming Schwann cells suggests a possible role for the enzyme in axon-myelin apposition and maintenance, especially of larger diameter axons.
Kioussi
C
C
Department of Biochemistry, Hellenic Pasteur Institute, Athens, Greece.
Crine
P
P
Matsas
R
R
D000375:Aging / Q000502:physiology*; D000818:Animals; D000911:Antibodies, Monoclonal; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D007124:Immunoenzyme Techniques; D007668:Kidney / Q000201:enzymology / Q000254:growth & development; D007687:Kidney Tubules, Proximal / Q000201:enzymology; D009186:Myelin Sheath / Q000502:physiology*; D015260:Neprilysin / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D012583:Schwann Cells / Q000201:enzymology / Q000502:physiology*; D012584:Sciatic Nerve / Q000201:enzymology* / Q000254:growth & development
D000911:Antibodies, Monoclonal; D015260:Neprilysin