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Joshi, O.

Publications and source records attributed to Joshi, O..

4 recordsLinked to original sources

Pancreatic cancer cells breach endothelial barriers through protrusion-driven invasion or endothelial retraction

Extravasation, the exit of circulating cancer cells from blood vessels, is a critical yet poorly understood step in metastatic dissemination. Here we show that pancreatic ductal adenocarcinoma (PDAC) cells can breach endothelial barriers through two mechanistically distinct modes of extravasation. MIA PaCa-2 cells breach endothelial junctions via filopodia-like protrusions, enabling access to and spread across the basal extracellular matrix (ECM). By contrast, AsPC-1 cells remain rounded atop the endothelium and cross the barrier by triggering rapid retraction of neighbouring endothelial cells. These distinct extravasation modes were also observed in zebrafish larvae. In the mouse lung, AsPC-1 cells arrest, survive, induce endothelial detachment from the basal lamina, and extravasate through this retraction mechanism before metastatic outgrowth. Mechanistically, AsPC-1-secreted factors are sufficient to destabilise endothelial monolayers, and AsPC-1 cells also induce endothelial apoptosis; however, blocking apoptosis does not prevent barrier disruption. By contrast, treatment with saracatinib, a Src-family kinase inhibitor, protects endothelial barriers, limits early vascular disruption in the lung, and delays metastatic outgrowth. Together, these findings reveal that PDAC cells can extravasate via mechanistically distinct routes, suggesting that effective anti-metastatic strategies may need to target multiple modes of endothelial barrier breach rather than a single pathway.

cell biology↗

MicroRNA-223 Enhances Microglia-Dependent Clearance of Amyloid Beta Plaques and Ameliorates Behavioral Deficits in a Mouse Model of Alzheimer's Disease

The Alzheimers disease (AD) brain is characterized by dysregulated expression of multiple microRNAs (miRNA), positioning them as promising diagnostic and therapeutic targets. The levels of glia-enriched miR-223 are abnormal in the brains and plasma of AD patients and miR-223 is neuroprotective in models of stroke. However, whether miR-223 can be beneficial in AD is not known. Here, we report that intracerebroventricular (ICV) injection of miR-223 oligonucleotide mimic alleviated cognitive impairment, reduced amyloid beta (A{beta}) pathology, and ameliorated the defects in synaptic marker expression in AppNL-G-F AD model mice. Mechanistically, miR-223 induced microglial clustering around A{beta} plaques with a concomitant upregulation of microglial phagocytic receptors AXL, TREM2 and CD11c, while pharmacological microglial depletion abolished the plaque-clearance phenotype. Moreover, in human iPSC-derived microglia miR-223 directly targeted multiple genes in the endo-lysosomal pathway, including AD risk gene SPPL2A, indicating that it acts as a major regulator of microglial phenotype. Lastly, long-term AAV-mediated overexpression of miR-223 recapitulates its beneficial effects on cognition, pathology, and synaptic marker expression. Our study demonstrates a novel approach for the treatment of AD using miR-223 and highlights the potential of RNAi-based therapeutics in neurodegenerative disease.

neuroscience↗

Filopodome proteomics identifies CCT8 as a MYO10 interactor critical for filopodia functions

Cancer cells utilize filopodia to explore, adhere to, and invade their surrounding microenvironment, yet the protein networks that organize these protrusions remain incompletely defined. To uncover the molecular machinery underlying MYO10-positive filopodia, we targeted the fast biotin ligase TurboID to the filopo-dia tip-localized motor protein MYO10. Proximity biotinylation in two cell types revealed hundreds of potential MYO10 interactors. Surprisingly, there was limited overlap between the cell lines, indicating a previously unknown level of cell-type specificity in filopodia composition. A targeted microscopy and siRNA screen identified MINK1, SCRIB, CSNK1A1, and CCT8 as new regulators of filopodia formation. Focusing on one common interactor between cell lines, CCT8, known as a subunit of the chaperonin TRiC (TCP1 Ring Complex), we found that CCT8 associates with the MYO10 motor domain and regulates MYO10 filopodia independently of TRiC. Depleting CCT8 affected filopodia dynamics and impaired cell spreading, migration, and invasion in breast cancer cells. These findings establish CCT8 as a TRiC-independent regulator of MYO10 filopodia across different cancer cell types, highlight the surprising cell-type-specificity of filopodia composition, and provide a strategy and resource for studying filopodia in various biological contexts.

cell biology↗

Localization of AP2α2, TRPV1 and PIEZO2 to the Large Dense Core Vesicles of Human Dorsal Root Ganglion Neurons

Dorsal Root Ganglia (DRG) consist of both peptidergic and non-peptidergic nociceptive neurons. CGRP, an inflammatory neuropeptide, is a classical marker of peptidergic nociceptors and CGRP is stored within the large dense core vesicles (LDCVs) of these neurons. In addition to storing large peptide neurotransmitters, LDCVs might also serve to transport key membrane proteins to the peripheral terminals. This immunohistochemical study investigated the localization of different membrane proteins to the LDCVs of human DRG neurons. Previously validated antibodies against the endocytotic subunit AP22, the heat-activated channel TRPV1 and the mechanosensitive channel PIEZO2 were used in conjunction with an antibody against CGRP on sections of intact human DRG isolated from de-identified human subjects. Immunohistochemical studies were also performed on human synovial tissue to examine peripheral terminals. High magnification confocal microscopy was used to determine the co-localization signal of these membrane proteins with CGRP. We observed a strong co-localization of AP22 with the CGRP containing LDCVs signifying its role in membrane recycling. Moreover, we also observed a strong colocalization of TRPV1 and PIEZO2 with CGRP suggesting that LDCV release controls the trafficking of these channels to the membrane. It is likely that during injury, bulk exocytosis of CGRP will concomitantly increase the surface expression of TRPV1 and PIEZO2 channels enhancing the responsiveness of these neurons to painful stimuli. This model suggests that neurons that co-localize TRPV1 and PIEZO2 to CGRP containing LDCVs are likely silent nociceptors.

neuroscience↗