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J Biol Chem, Vol. 274, Issue 17, 11736-11741, April 23, 1999
1-Syntrophin in Rat Brain
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From the Neuronal nitric-oxide synthase (nNOS) has a
PSD-95/Dlg/ZO-1 (PDZ) domain that can interact with multiple proteins.
nNOS has been known to interact with PSD-95 and a related protein,
PSD-93, in brain and with Division of Protein Metabolism, Institute
for Protein Research, Osaka University, 3-2 Yamada-Oka, Suita, Osaka
565-0871, Japan, Central Laboratories for Key Technology, Kirin
Brewery Company, Limited, 1-13-5 Fukuura, Kanazawa-Ku, Yokohama,
Kanagawa 236-0004, Japan, and the ** Netherlands Institute for Research,
Meibergdreef 33, 1105 AZ, Amsterdam Zuidoost, Netherlands
1-syntrophin in skeletal muscle in
mammals. In this study, we have purified an nNOS-interacting protein
from bovine brain using an affinity column made of Sepharose conjugated with glutathione S-transferase-rat nNOS fusion protein and
identified it as 1-syntrophin by microsequencing. Immunostaining of
primary cultures of rat embryonic brain neuronal cells with antibodies against these proteins showed that nNOS and 1-syntrophin were colocalized in neuronal cell bodies and neurites. Immunohistochemical analysis indicated that the nNOS- and 1-syntrophin-like
immunoreactive substances were highly expressed in the rat hypothalamic
suprachiasmatic nucleus (SCN) and paraventricular nucleus. In the SCN,
nNOS- and 1-syntrophin-like immunoreactive substances were
colocalized in the same neurons as detected by confocal microscopy.
These results indicate that nNOS in brain interacts with
1-syntrophin in specific neurons of the SCN and paraventricular
nucleus and that this interaction might play a physiological role in
functions of these neurons.
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