Effects of Phytochemicals on Type 2 Diabetes via MicroRNAs.

PURPOSE OF REVIEW: Type 2 diabetes, characterized by inadequate insulin secretion and resistance, is increasingly prevalent. To effectively manage type 2 diabetes, identifying new therapeutic targets is crucial. MicroRNAs, short noncoding RNA molecules, play a pivotal role in regulating ß-cell function, insulin production, and resistance, and show promise as biomarkers for predicting type 2 diabetes onset. Phytochemicals, known for their antioxidant activities, may influence microRNA expression, potentially improving insulin sensitivity and mitigating associated complications. This review aims to explore the significance of microRNA in type 2 diabetes, their potential as biomarkers, and how certain phytochemicals may modulate microRNA expressions to reduce or prevent diabetes and its complications. RECENT FINDINGS: Current research suggests that microRNAs show promise as novel therapeutic biomarkers for diagnosing type 2 diabetes and monitoring diabetic complications. Additionally, phytochemicals may regulate microRNAs to control type 2 diabetes, presenting a potential therapeutic strategy. The multifactorial effects of phytochemicals on type 2 diabetes and its complications through microRNAs warrant further research to elucidate their mechanisms. Comprehensive clinical trials are needed to assess the safety and efficacy of phytochemicals and their combinations. Given their ability to modulate microRNAs expression, incorporating phytochemical-rich foods into the diet may be beneficial.

Characterization of a glutenin-specific serine proteinase of Sunn bug Eurygaster integricepts Put.

Glutenin hydrolyzing proteinases (GHPs) have been purified, by affinity chromatography, from wheat seeds damaged by the Sunn bug Eurygaster integriceps (Hemiptera, Scutelleridae). A 28 kDa protein was partially sequenced by mass spectrometry and Edman degradation which showed homology to serine proteases from various insects. Three full length clones were obtained from cDNA isolated from Sunn bug salivary glands using degenerate PCR based on the sequences obtained. The cleavage site of the protease was determined using recombinant and synthetic peptides and shown to be between the consensus hexapeptide and nonapeptide repeat motifs present in the high molecular weight subunits of wheat glutenin (PGQGQQ∧GYYPTSLQQ). Homology models were generated for the three proteinases identified in this study using the high resolution X-ray structure of a crayfish (Pontastacus leptodactylus) trypsin complexed with a peptide inhibitor as template (PDB accession 2F91). The novel specificity of this protease may find applications in both fundamental and applied studies.