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The Cardinal Edge

Abstract

The nucleus has long been simplified in the field of biology, despite being an important organelle. Until recently, it has been commonly depicted as a simple sphere located at the center of a cell, responsible mainly for regulating protein synthesis. However, current research indicates that the linkers of the nucleoskeleton and cytoskeleton (LINC) complexes, the pillars of nuclear architecture, play a critical role in maintaining nuclear integrity and function. These complexes interact with proteins, such as Lamins, that modulate responses to biomechanical stimuli through the regulation of gene expression. As such, when these structures are downregulated, they can contribute to specific pathologies, with one such being osteosarcoma, a malignant bone tumor with high metastasis rates and mortality. This literature review aims to provide insight into how a deficiency in nuclear architecture proteins contributes to the development of osteosarcoma. Four peer-reviewed articles that conducted comprehensive studies on LINC complexes, Lamins A/C, and supporting proteins, and their effects on nuclear morphology, migration potential, and aggressiveness within established human osteosarcoma cell lines, were investigated. Overall, researchers found that lower Lamin A/C levels correlate with properties characteristic of aggressive osteosarcoma, demonstrating abnormal nuclear patterns and increased migration from reduced biomechanical properties within human osteosarcoma cells. However, one of the articles highlighted a unique perspective on how SUN proteins could play a more significant role than Lamins A/C in this pathology. These conclusions underscore that low expression levels of nuclear architecture are crucial to the pathophysiology of osteosarcoma. Further research into LINC complexes and Lamins could guide the development of therapeutic treatments to halt osteosarcoma progression and reduce tumor aggressiveness.

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