salvianolic-acid-B and 4-hydroxyphenyllactic-acid

Salvia miltiorrhiza Bunge is a traditional Chinese medicine, and its water-soluble phenolic acid active compounds have very important medicinal value; however, the synthesis pathways of the main active ingredients remain unknown. Here, we employed nuclear magnetic resonance (NMR)-based metabolomics and transcriptomics techniques to study the biosynthesis mechanism of salvianolic acids. High-performance liquid chromatography (HPLC) combined with NMR showed an improvement over traditional techniques, and 54 metabolites were detected. The results of the multivariate statistical analysis showed that salvianolic acid B (SAB), rosmarinic acid (RA), caffeic acid, succinate, and citrate were among the multiple compounds that were increased in the methyl jasmonate (MeJA)-elicited group; the levels of sucrose, fructose, glutamine, and tyrosine were decreased. Combined with the differentially expressed genes (DEGs) found by transcriptome sequencing, we speculate that the synthesis of RA after MeJA treatment mostly occurred through caffeic acid and bypassed 4-hydroxyphenyllactic acid. This provides useful information for the study of salvianolic acids synthesis.

Topics: Acetates; Benzofurans; Biosynthetic Pathways; Cells, Cultured; Chromatography, High Pressure Liquid; Cinnamates; Cyclopentanes; Depsides; Gene Expression Profiling; Metabolomics; Oxylipins; Phenylpropionates; Plant Roots; Proton Magnetic Resonance Spectroscopy; Rosmarinic Acid; Salvia miltiorrhiza

Salvia miltiorrhiza is a medicinal plant widely used in the treatment of cardiovascular and cerebrovascular diseases. Hydrophilic phenolic acids, including rosmarinic acid (RA) and lithospermic acid B (LAB), are its primary medicinal ingredients. However, the biosynthetic pathway of RA and LAB in S. miltiorrhiza is still poorly understood. In the present study, we accomplished the isolation and characterization of a novel S. miltiorrhiza Hydroxyphenylpyruvate reductase (HPPR) gene, SmHPPR, which plays an important role in the biosynthesis of RA. SmHPPR contained a putative catalytic domain and a NAD(P)H-binding motif. The recombinant SmHPPR enzyme exhibited high HPPR activity, converting 4-hydroxyphenylpyruvic acid (pHPP) to 4-hydroxyphenyllactic acid (pHPL), and exhibited the highest affinity for substrate 4-hydroxyphenylpyruvate. SmHPPR expression could be induced by various treatments, including SA, GA

Topics: Amino Acid Sequence; Benzofurans; Biosynthetic Pathways; Cinnamates; Depsides; Gene Expression Regulation, Plant; Oxidoreductases; Phenylpropionates; Phenylpyruvic Acids; Phylogeny; Plant Proteins; Plant Roots; Plants, Genetically Modified; Recombinant Proteins; Rosmarinic Acid; Salvia miltiorrhiza; Sequence Alignment