67-kDa high-affinity laminin receptor (67LR) (67LR)

The 67-kDa high-affinity laminin receptor (67LR) is a non-integrin cell surface receptor that plays a pivotal role in mediating the interaction between cells and the extracellular matrix component laminin-1 (UniProt P08865). It is uniquely derived from a 37-kDa precursor (37LRP), which also functions as a component of the 40S ribosomal subunit, classifying it as a moonlighting protein involved in both protein synthesis and cell signaling (PubMed: 26859400). In oncology, 67LR is frequently overexpressed in aggressive cancers, such as breast, colon, and lung carcinomas, where it correlates with increased metastatic potential and poor prognosis by facilitating tumor cell invasion and angiogenesis (PubMed: 15077121). Beyond its role in cancer, 67LR serves as a critical co-receptor for various pathogens, including the cellular prion protein (PrPc) and several viruses like Dengue and Sindbis (PubMed: 12808012). Therapeutic interest in 67LR is driven by its high-affinity interaction with the green tea polyphenol epigallocatechin-3-gallate (EGCG) and the development of monoclonal antibodies aimed at blocking its pathological interactions (PubMed: 15077121).

Other names

37-kDa laminin receptor precursor37LRPRibosomal protein SARPSALAMR1Laminin-binding proteinp40

Competitive inhibition of laminin-1 binding to the receptor, blockade of pathogen attachment to the cell surface, and downregulation of receptor-mediated signaling pathways such as MAPK/ERK.