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Department of Internal Medicine II, Technical University of Munich, D-81675 Munich, Germany
The aim of this study was to
characterize neuronal nitric oxide synthase (nNOS) activity and
5'-end splice variants in rat small intestine. nNOS was
predominantly expressed in the longitudinal muscle layer, with attached
myenteric plexus (LM-MP). The biochemical properties of NOS activity in
enriched nerve terminals resemble those of nNOS isolated from the
brain. Western blot analysis of purified NOS protein with an nNOS
antibody showed a single band in the particulate fraction and three
bands in the soluble fraction. Rapid amplification of 5' cDNA
ends-PCR revealed the presence of three different 5'-end splice
variants of nNOS. Two variants encode for nNOS
, which has a specific
domain for membrane association. The third variant encodes for nNOS
,
which lacks the domain for membrane association and should therefore be
soluble. nNOS is predominantly expressed in LM-MP and can be enriched
in enteric nerve terminals. We present the first evidence that three
5'-end splice variants of nNOS encoding two different proteins
are expressed in rat small intestine. These two nNOS enzymes exhibit
different subcellular locations and might be implicated in different
biological functions.
nitric oxide synthase isoforms; endothelial nitric oxide synthase; inducible nitric oxide synthase; nerve terminals; myenteric plexus
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