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Huh, Y.-M.

Publications and source records attributed to Huh, Y.-M..

2 recordsLinked to original sources

CellDF: Quality-controlled cell matching for whole-slide HE-IHC label transfer

A laboratory that stains immunohistochemistry (IHC) on a section adjacent to a hematoxylin and eosin (HE) section already holds the material to supervise HE models on its own cases. It goes unused because adjacent sections sample non-identical cells, and residual registration error prevents assigning IHC labels to individual HE cells. We present CellDF (Cell Displacement Field), which turns registered serial-section data into pairs of HE cells and the protein-expression labels measured on the adjacent section. CellDF estimates a locally adaptive residual displacement field through iterated kernel regression over each HE cell's K nearest IHC candidates; a sparse-kernel variant keeps it tractable at whole-slide cell counts, where pairwise matchers are not. The within-tile distribution of these displacements yields two ground-truth-free statistics, the directional scatter {sigma}{theta} and the between-tile angular deviation |{Delta}{theta}|, that localize matching quality more finely than landmark-based target registration error and drive a two-stage filter that withholds labels where matching is unreliable. On 54 same-section HyReCo pairs, {sigma}{theta} correlates only moderately with landmark error and flags localized restaining damage that global error misses; on 30 four-marker Acrobat serial-section cases, the same statistic identifies which IHC marker, if any, lies close enough to HE for cell-level transfer. As a proof of concept, transferred labels trained a cell classifier on HE embeddings that generalized to held-out cells within the sample (F1 0.85, AUROC 0.88). A laboratory can thereby generate cell-level protein-expression labels from its own sections and tune HE-only models on them, with each label set's reliability read from the data.

pathology↗

Darapladib, an inhibitor of Lp-PLA2, sensitizes cancer cells to ferroptosis by remodeling lipid metabolism

Arachidonic and adrenic acids in the membrane play key roles in ferroptosis, but how these fatty acids are manipulated in cells is largely unknown. Here, we reveal that lipoprotein-associated phospholipase A2 (Lp-PLA2) controls intracellular phospholipid metabolism and contributes to ferroptosis resistance. A metabolic drug screen identified that darapladib (SB-480848), an inhibitor of Lp-PLA2, synergistically induced ferroptosis with GPX4 inhibitors. Notably, darapladib was able to enhance ferroptosis under lipoprotein-deficient or serum-free conditions. Furthermore, Lp-PLA2 was located in the membrane and cytoplasm and suppressed ferroptosis, suggesting the critical role of intracellular Lp-PLA2. Lipidomic analysis showed that phosphatidylethanolamine (PE) species were generally enriched, while lysophosphatidylethanolamine (lysoPE) and free fatty acid levels were reduced, upon darapladib treatment. Finally, combination treatment with darapladib and PACMA31, a GPX4 inhibitor, efficiently inhibited tumor growth in a xenograft model. Our study suggests that inhibition of Lp-PLA2 is a potential therapeutic strategy to enhance ferroptosis in cancer treatment.

cancer biology↗