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Biology subjects

Chin, B.

Publications and source records attributed to Chin, B..

3 recordsLinked to original sources

Endothelial Cell Autophagy Suppresses Metastasis In Mouse Mammary and Pancreatic Neuroendocrine Tumor Models

Autophagy, a key lysosomal degradation pathway regulating metabolic adaptation in cancer, plays fundamental roles in both the tumor and host stromal compartments during cancer progression. An important unanswered question is whether and how autophagy in specific host stromal elements, such as endothelial cells, influences metastasis. Here, we scrutinize how the genetic loss of autophagy in endothelial cells impacts primary tumor progression and metastasis in the Polyoma Middle T (PyMT) model of luminal B breast cancer. In both autochthonous and orthotopic mammary transplant models, PyMT primary tumor growth is significantly delayed upon endothelial cell Atg12 or Atg5 genetic deletion (Atg12 or 5 ECKO), which correlates with increased tumor cell apoptosis and HIF1 activation. In contrast, PyMT-bearing Atg12 ECKO mice exhibit increased metastasis, as well as higher rates of primary tumor and lung metastatic recurrence following surgical resection of PyMT primary tumors. Experimental metastasis assays further corroborate that loss of endothelial cell autophagy in Atg12 ECKO host animals promotes PyMT metastatic colonization and outgrowth, resulting in increased lung metastases compared to controls. Similarly, in the Rat Insulin Promoter T antigen pancreatic neuroendocrine tumor (RT2-PNET) model, endothelial cell deletion of Atg12 promotes liver micro-metastases. Taken together, these results from distinct preclinical cancer models reveal that endothelial cell autophagy suppresses metastatic seeding and progression and broach that autophagy inhibition in host endothelial cells may adversely influence the efficacy of systemic autophagy-lysosomal pathway inhibition in the clinical oncology setting.

cancer biology↗

Multimodal non-ionizing quantitative characterization of enamel hypomineralization

Enamel hypomineralization is clinically graded but difficult to quantify with visual and radiographic assessment. We evaluated whether optical coherence tomography (OCT) and lock-in thermography imaging (LITI) provide non-ionizing, quantitative lesion localization and phenotyping, using clinical mDDE classification as a practical benchmark and micro-CT ({micro}CT) mineral density as an in vitro reference in a subset. Twenty-five extracted first permanent molars were classified as control, hypomineralized (Type 1 white-cream; Type 2 yellow-brown), or other enamel defects. Co-localized OCT A-scan decay slopes and LITI lock-in phase-contrast were measured in predefined ROIs; six teeth underwent {micro}CT with hydroxyapatite calibration. Clinical scoring showed substantial agreement (inter-rater {kappa}=0.61; intra-rater {kappa}=0.70). OCT decay slopes differed across clinical groups (Kruskal-Wallis p=0.00028), separating controls from defect groups, while separation between hypomineralization and other defects was limited. LITI detected thermophotonic "hot spots" at many clinically identified sites (sensitivity 80%) but showed low specificity (20%) at a single modulation frequency, consistent with high anomaly sensitivity but limited etiologic discrimination. In the {micro}CT subset, hypomineralized ROIs showed reduced mineral density relative to adjacent enamel and spatial concordance with OCT and LITI contrast. Together, OCT+LITI support objective lesion mapping and motivate multi-frequency thermophotonics and expanded reference sampling to improve specificity for chairside translation.

biophysics↗

Caspase inhibition mitigates tau cleavage and neurotoxicity in iPSC-induced neurons with the V337M MAPT mutation

Tau post-translational modifications (PTMs) are associated with progressive tau accumulation and neuronal loss in tauopathies, including forms of frontotemporal lobar degeneration (FTLD) and Alzheimers disease (AD). Proteolytic cleavage of tau by active caspases, including caspase-6, represents an underexplored tau PTM implicated in tau pathology. Caspase-cleaved tau is toxic and prone to self-aggregation in experimental models. To elucidate the presence and temporal course of caspase activation, tau cleavage, and neuronal death, we generated two neoepitope monoclonal antibodies (mAbs) against caspase-6 tau proteolytic sites and cortical neurons from induced pluripotent stem cells (iPSCs) with the frontotemporal dementia (FTD)-causing V337M MAPT mutation. FTLD V337M MAPT and AD postmortem brains showed positivity for both cleaved tau mAbs as well as active caspase-6. Relative to isogenic wild-type MAPT controls, V337M MAPT neurons showed a time-dependent increase in pathogenic tau in the form of tau oligomers, caspase-cleaved tau, and p-tau. Accumulation of toxic tau species in 3-month V337M MAPT neurons also increased vulnerability to stress, which was pharmacologically rescued by caspase inhibition. We propose a model in which time-dependent accumulation of caspase-cleaved tau in V337M MAPT neurons promotes neurotoxicity that is reversed by caspase-6 inhibition. Caspase-cleaved tau may be a biomarker of tauopathy, and caspases could be viable targets for therapeutic intervention against tau pathogenesis in FTLD and other tauopathies. SignificanceThe mechanisms leading to tau pathology in frontotemporal dementia (FTD) and Alzheimers disease (AD) remain elusive. Experimental studies in AD demonstrate that tau cleavage by active caspase-6 contributes to tau pathology since cleaved tau may be toxic and prone to self-aggregation. Yet, the role of caspase-cleaved tau in promoting toxicity and cell death is unclear. Here, we generated two neoepitope monoclonal antibodies against caspase-6 tau and evaluated tau cleavage in postmortem human brains, iPSC-induced cortical neurons with the FTD-causing V337M MAPT mutation, and isogenic wild-type MAPT controls. Our results demonstrate a time-dependent accumulation of caspase-cleaved tau and increased neurotoxicity in the mutant iNs that is reversed by caspase-6 inhibition. Caspases could be viable therapeutic targets against tau pathology in tauopathies.

neuroscience↗