Context: Inflammatory disorders are common in modern life, and medicinal plants provide an interesting source for new compounds bearing anti-inflammatory properties. In this regard, Brazilian medicinal plants are considered to be a promising supply of such compounds due to their great biodiversity.Objectives: To undertake a review on Brazilian medicinal plants with corroborated anti-inflammatory activities by selecting data from the literature reporting the efficacy of plants used in folk medicine as anti-inflammatory, including the mechanisms of action of their extracts and isolated compounds.Methods: A search in the literature was undertaken by using the following Web tools: Web of Science, SciFinder, Pub-Med and Science Direct. The terms ‘anti-inflammatory’ and ‘Brazilian medicinal plants’ were used as keywords in search engine. Tropicos and Reflora websites were used to verify the origin of the plants, and only the native plants of Brazil were included in this review. The publications reporting the use of well-accepted scientific protocols to corroborate the anti-inflammatory activities of Brazilian medicinal plants with anti-inflammatory potential were considered.Results: We selected 70 Brazilian medicinal plants with anti-inflammatory activity. The plants were grouped according to their anti-inflammatory mechanisms of action. The main mechanisms involved inflammatory mediators, such as interleukins (ILs), nuclear factor kappa B (NF-κB), prostaglandin E2 (PGE2), cyclooxygenase (COX) and reactive oxygen species (ROS).Conclusions: The collected data on Brazilian medicinal plants, in the form of crude extract and/or isolated compounds, showed significant anti-inflammatory activities involving different mechanisms of action, indicating Brazilian plants as an important source of anti-inflammatory compounds.

The plant metabolite 3,4,5-tri-O-galloylquinic acid methyl ester (TGAME, compound 6) was synthesized, and its potential effect on calcium oxalate monohydrate (COM) crystal binding to the surface of Madin-Darby canine kidney cells type I (MDCKI) and crystal growth in a Drosophila melanogaster Malpighian tubule (MT) model were investigated. Membrane, cytosolic, and total annexin A1 (AxA1), α-enolase, and heat shock protein 90 (HSP90) amounts were examined by Western blot analysis after subcellular fractionation, then confirmed by immunofluorescence staining of cultured cells. Pretreatment of MDCKI cells with TGAME for up to 6 h significantly diminished COM crystal binding in a concentration-dependent manner. TGAME significantly inhibited AxA1 surface expression by immunofluorescence microscopy, whereas intracellular AxA1 increased. Western blot analysis confirmed AxA1 expression changes in the membrane and cytosolic fractions of compound-treated cells, whereas whole cell AxA1 remained unchanged. TGAME also significantly decreased the size, number, and growth of calcium oxalate (CaOx) crystals induced in a Drosophila melanogaster MT model and possessed a potent antioxidant activity in a DPPH assay.

No abstract

Copaifera lucens n-butanolic fraction (BF) was used as a source of galloylquinic acids, and aerobically incubated with Aspergillus alliaceus ATCC10060, Aspergillus brasiliensis ATCC 16404, and Cunninghamella elegans ATCC 10028b cultures for 60 and 120 h. Out of the three studied filamentous fungi, A. alliaceus ATCC10060 was able to degrade galloylquinic acids into one major metabolite, 3-O-methylgallic acid (M1). The product was identified by 1 H-NMR, UPLC-MS/MS and its potential effect on calcium oxalate monohydrate (COM) crystal binding to Madin-Darby canine kidney cells type I surface was studied. Renal cells pretreatment with BF and M1 for 3 h significantly decreased calcium oxalate monohydrate crystal-adherence at 50 μg/mL and 5 μM, respectively. Both M1 and BF significantly reduced surface expression of COM-binding proteins annexin A1 and heat shock protein 90, respectively as evidenced by Western blot analysis of membrane, cytosolic, and whole cell lysate fractions. The compounds also showed antioxidant activities in DPPH assay.