TY - JOUR
T1 - Diamine oxidase induces neurite outgrowth in chick dorsal root ganglia by a nonenzymatic mechanism
AU - Munis, James R.
AU - Steiner, Joseph T.
AU - Ruat, Martial
AU - Snyder, Solomon H.
PY - 1998/3
Y1 - 1998/3
N2 - The enzyme diamine oxidase (DAO) catalyzes the oxidative deamination of histamine, diamines, and polyamines. DAO has been localized to several tissues, including thymus, kidney, intestine, seminal vesicles, placenta, and pregnancy plasma. DAO is not constitutively expressed in the mammalian brain, but it becomes detectable following focal injury. Although the physlologic role of DAO remains unknown, the observation that it is present at the interface between rapidly dividing and quiescent cells in several tissues suggests that it might be involved in regulating cell division or differentiation at tissue boundaries. In addition, the observation that DAO is expressed in the brain following injury suggests that the protein might play a role in the CNS response to focal neuronal damage. To test that hypothesis, we assessed the ability of purified DAO to alter the pattern of neuronal differentiation and nerve growth in vitro. In chick dorsal root ganglion explant cultures, purified porcine DAO induced neurite outgrowth in the low nanomolar range. Addition of aminoguanidine, which inhibits DAO enzyme activity, did not inhibit the protein's neurotrophic activity. These findings suggest that DAO can function as a neurotrophic ligand independent of its enzymatic activity.
AB - The enzyme diamine oxidase (DAO) catalyzes the oxidative deamination of histamine, diamines, and polyamines. DAO has been localized to several tissues, including thymus, kidney, intestine, seminal vesicles, placenta, and pregnancy plasma. DAO is not constitutively expressed in the mammalian brain, but it becomes detectable following focal injury. Although the physlologic role of DAO remains unknown, the observation that it is present at the interface between rapidly dividing and quiescent cells in several tissues suggests that it might be involved in regulating cell division or differentiation at tissue boundaries. In addition, the observation that DAO is expressed in the brain following injury suggests that the protein might play a role in the CNS response to focal neuronal damage. To test that hypothesis, we assessed the ability of purified DAO to alter the pattern of neuronal differentiation and nerve growth in vitro. In chick dorsal root ganglion explant cultures, purified porcine DAO induced neurite outgrowth in the low nanomolar range. Addition of aminoguanidine, which inhibits DAO enzyme activity, did not inhibit the protein's neurotrophic activity. These findings suggest that DAO can function as a neurotrophic ligand independent of its enzymatic activity.
KW - Diamine oxidase
KW - Dorsal root ganglion
KW - Neurite outgrowth
UR - http://www.scopus.com/inward/record.url?scp=0031892515&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031892515&partnerID=8YFLogxK
U2 - 10.1046/j.1471-4159.1998.70031323.x
DO - 10.1046/j.1471-4159.1998.70031323.x
M3 - Article
C2 - 9489756
AN - SCOPUS:0031892515
SN - 0022-3042
VL - 70
SP - 1323
EP - 1326
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
IS - 3
ER -