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Abstract Introduction: Mesothelin (MSLN) is a glycoprotein present on the surface of mesothelial cells, sometimes used as a tumor marker. Its overexpression in various cancers, including mesothelioma, ovarian, pancreatic, and lung, is linked to increased tumor aggressiveness, evasion of apoptosis, metastasis, and resistance to treatments. Mucin16 (MUC16) belongs to a family of proteins that play a crucial role in cell adhesion, signaling, and immune responses. In cancer, alterations in mucin expression and structure may contribute to tumor progression and metastasis by enhancing cell survival and immune evasion. Mesothelin is known to interact with mucins, influencing tumor cell behavior and metastatic potential. More specifically, the MSLN/MUC16 interaction facilitates tumor cell invasion and peritoneal spread in ovarian cancer. However, reliable molecular tools to study protein interactions have been scarce. Here, we relied on the Naveni® in situ proximity ligation technology to identify MSLN/MUC16 in various cancer samples. The method detects proteins located within interaction range (40 nm) by means of antibodies conjugated to oligonucleotides that create amplified fluorescent signal. Since the technique does not compromise the structural integrity of tissues, communication between proteins can be studied in their native environment. Materials Part 1 (Regular Abstracts) ; 2024 Apr 5-10; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2024;84 (6Suppl): Abstract nr 2744.
Bodbin et al. (Fri,) studied this question.