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Here, it is found that caveolin\u20101 (CAV1), a primary component of membrane lipid rafts and caveolae, is highly expressed in MM cells and is associated with MM progression and drug resistance. CAV1 knockdown decreases MM cell adhesion to stromal cells and attenuates cell adhesion\u2010mediated drug resistance to bortezomib. CAV1 inhibition in MM cells enhances natural killer cell\u2010mediated cytotoxicity through increasing CXCL10, SLAMF7, and CD112. CAV1 suppression reduces mitochondrial membrane potential, increases reactive oxygen species, and inhibits autophagosome\u2010lysosome fusion, resulting in the disruption of redox homeostasis. Additionally, CAV1 knockdown enhances glutamine addiction by increasing ASCT2 and LAT1 and dysregulates glutathione metabolism. As a result of CAV1 inhibition, MM cells are more sensitive to starvation, glutamine depletion, and glutamine transporter inhibition, and grow more slowly in vivo in a mouse model treated with bortezomib. The observation that CAV1 inhibition modulated by 6\u2010mercaptopurine, daidzin, and statins enhances the efficacy of bortezomib in vitro and in vivo highlights the translational significance of these FDA\u2010approved drugs in improving MM outcomes. These data demonstrate that CAV1 serves as a potent therapeutic target for enhancing chemotherapy and immunotherapy for MM.<\/jats:p>","DOI":"10.1002\/advs.202408373","type":"journal-article","created":{"date-parts":[[2024,12,4]],"date-time":"2024-12-04T09:12:29Z","timestamp":1733303549000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Targeting Caveolin\u20101 in Multiple Myeloma Cells Enhances Chemotherapy and Natural Killer Cell\u2010Mediated Immunotherapy"],"prefix":"10.1002","volume":"12","author":[{"given":"Dewen","family":"Zhan","sequence":"first","affiliation":[{"name":"The Affiliated Traditional Chinese Medicine Hospital Guangzhou Medical University  Guangzhou 510130 China"},{"name":"Guangzhou Municipal and Guangdong Provincial Key Laboratory of Protein Modification and Degradation School of Basic Medical Sciences Guangzhou Medical University  Guangzhou 511436 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