To improve the hydrophobicity and poor separability of hyper-cross-linked polymers (HCPs) in extraction, a porous magnetic adsorbent (Fe₃O₄@SHCP) was constructed by facile post-modification to introduce sulfonic acid groups and magnetic nanoparticles for the magnetic solid-phase extraction of heterocyclic aromatic amines (HAAs). Owing to the double extraction mechanism adopted by Fe₃O₄@SHCP, it has a high extraction efficiency for HAAs. Coupled with high-performance liquid chromatography (HPLC), 5 HAAs in baked cakes were detected at one time. Under optimal extraction conditions, the enrichment factor of HAAs was up to 952-986, with LODs at 0.05-0.3 ng·g^-1. Based on the HPLC method, novel digital imaging colorimetry (DIC) was developed to accurately and rapidly monitor HAAs in cakes. Additionally, the established DIC method has been used to successfully evaluate the effect of baking temperature and duration on HAAs in baked cakes.

JOURNAL/nrgr/04.03/01300535-202604000-00040/figure1/v/2026-04-21T135625Z/r/image-tiff α-Synuclein accumulation and transmission are vital to the pathogenesis of Parkinson’s disease, although the mechanisms underlying misfolded α-synuclein accumulation and propagation have not been conclusively determined. The expression of low-density lipoprotein receptor–related protein 1, which is abundantly expressed in neurons and considered to be a multifunctional endocytic receptor, is elevated in the neurons of patients with Parkinson’s disease. However, whether there is a direct link between low-density lipoprotein receptor–related protein 1 and α-synuclein aggregation and propagation in Parkinson’s disease remains unclear. Here, we established animal models of Parkinson’s disease by inoculating monkeys and mice with α-synuclein pre-formed fibrils and observed elevated low-density lipoprotein receptor–related protein 1 levels in the striatum and substantia nigra, accompanied by dopaminergic neuron loss and increased α-synuclein levels. However, low-density lipoprotein receptor–related protein 1 knockdown efficiently rescued dopaminergic neurodegeneration and inhibited the increase in α-synuclein levels in the nigrostriatal system. In HEK293A cells overexpressing α-synuclein fragments, low-density lipoprotein receptor–related protein 1 levels were upregulated only when the N-terminus of α-synuclein was present, whereas an α-synuclein fragment lacking the N-terminus did not lead to low-density lipoprotein receptor–related protein 1 upregulation. Furthermore, the N-terminus of α-synuclein was found to be rich in lysine residues, and blocking lysine residues in PC12 cells treated with α-synuclein pre-formed fibrils effectively reduced the elevated low-density lipoprotein receptor–related protein 1 and α-synuclein levels. These findings indicate that low-density lipoprotein receptor–related protein 1 regulates pathological transmission of α-synuclein from the striatum to the substantia nigra in the nigrostriatal system via lysine residues in the α-synuclein N-terminus.

Olfactory impairment is an initial non‐motor symptom of Parkinson's disease that causes the deposition of aggregated α‐synuclein (α‐syn) in olfactory neurons. Transient receptor potential canonical (TRPC) channels are a diverse group of non‐selective Ca²⁺ entry channels involved in the progression or pathogenesis of PD via Ca²⁺ homeostatic regulation. However, the relationship between TRPC and α‐syn pathology in an olfactory system remains unclear. To address this issue, we assessed the olfactory function in α‐syn transgenic mice. In contrast with control mice, the transgenic mice exhibited impaired olfaction, TRPC3 activation and apoptotic neuronal cell death in the olfactory system. Similar results were observed in primary cultures of olfactory neurons, that is TRPC3 activation, increasing intracellular Ca²⁺ concentration and apoptotic cell death in the α‐syn‐overexpressed neurons. These changes were significantly attenuated by TRPC3 knockdown. Therefore, our findings suggest that TRPC3 activation and calcium dyshomeostasis play a key role in α‐syn‐induced olfactory dysfunction in mice.