| Literature DB >> 18213519 |
Kyungjin Lee1, Kiyoon Kang, Munyoung Park, Young-Min Woo, Kyoungwhan Back.
Abstract
Serotonin N-hydroxycinnamoyltransferase (SHT) is a key enzyme in the synthesis of feruloylserotonin (FS) and 4-coumaroylserotonin (CS). These serotonin derivatives show strong antioxidant activity, making them valuable for both nutritional and pharmacological use in humans. Ectopic expression of SHT under the control of the endosperm specific-glutelin and prolamin promoters from rice was produced via Agrobacterium-mediated transformation. SHT expression was confirmed by Southern blot analysis, followed by Northern blotting and SHT enzyme activity analyses using total RNA and protein, respectively, extracted from transgenic seeds. The glutelin A3 (GluA3) promoter produced low SHT mRNA expression in rice seeds, whereas the prolamin promoter expressed high levels of SHT mRNA. In spite of the ectopic expression of SHT in rice seeds, both transgenic genotypes accumulated levels of serotonin derivatives similar to those found in wild-type rice. Furthermore, our data suggest that serotonin, rather than phenylpropanid-CoAs, is the rate-limiting substrate in the biosynthesis of serotonin derivatives in SHT-overexpressing transgenic rice seeds.Entities:
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Year: 2008 PMID: 18213519 DOI: 10.1007/s11130-007-0069-1
Source DB: PubMed Journal: Plant Foods Hum Nutr ISSN: 0921-9668 Impact factor: 3.921