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Laminin receptor (67 kDa), commonly referred to as **67LR**, is a multifunctional, non-integrin cell-surface receptor derived from a 37 kDa precursor (37LRP). It binds **laminin** in the extracellular matrix with high affinity, playing a pivotal role in mediating **cell adhesion, migration, invasion, angiogenesis, and extracellular matrix remodeling**. Overexpression of 67LR in tumor cells is correlated with enhanced *invasive and metastatic potential*, making it an important marker and possible therapeutic target in oncology. Beyond interactions with laminin, 67LR serves as a receptor for specific viruses (Sindbis, dengue) and prion proteins, thus mediating pathogen entry and prion internalization. The precursor, 37LRP, is a highly conserved ribosomal protein involved in translational processes and nuclear structure maintenance, and evolutionary studies confirm its essential role in basic cell viability and protein synthesis. Given its dual role in ribosomal function and cell surface signaling, drug targeting poses challenges regarding specificity and safety, especially with respect to normal cellular metabolism.
Inhibition of laminin binding to 67LR (blocking cell adhesion, migration, invasion)[4][5]; Inhibition of receptor-prion interaction[5]; Interference with receptor-mediated signaling affecting proliferation and metastasis[4]
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