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The 37/67 kDa laminin receptor (RPSA), also known as oncofetal antigen/immature laminin receptor protein (OFA/iLRP), is a multifunctional protein that plays a critical role in both protein synthesis and cell-extracellular matrix interactions [5]. In normal cells, it is primarily located in the cytoplasm as a component of the 40S ribosomal subunit, but in malignant cells, it is significantly overexpressed and translocated to the cell surface [6, 9]. This surface-expressed "immature" form acts as a high-affinity receptor for laminin, facilitating tumor cell adhesion, invasion, and metastasis [1, 4]. Because of its high expression in a wide variety of cancers and its relative absence on the surface of normal adult cells, it is considered a promising target for cancer immunotherapy, including vaccines and monoclonal antibodies [1, 3]. Additionally, it serves as a receptor for various pathogens, including prions and several viruses, making it a target for infectious disease research [5, 9]. Therapeutic strategies targeting this protein aim to block its interaction with the extracellular matrix or to leverage its tumor-specific surface expression for targeted killing [1, 10].
Inhibition of laminin binding to prevent tumor cell invasion and metastasis; induction of T-cell mediated immune responses against tumor cells; blocking of viral and prion entry into cells [1, 3, 9].
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