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Cell communication network factor 1 (CCN1), formerly known as Cysteine-rich angiogenic inducer 61 (CYR61), is a secreted matricellular protein that plays a vital role in regulating the cellular microenvironment (UniProt P23276). It functions by interacting with various cell surface receptors, including integrins (such as αvβ3, αvβ5, and α6β1) and heparan sulfate proteoglycans, to modulate signaling pathways involved in cell adhesion, migration, and proliferation (NCBI Gene 3491). In physiological conditions, CCN1 is essential for vascular development, placental formation, and wound healing. However, its overexpression is associated with several diseases, most notably cancer, where it promotes tumor growth, angiogenesis, and metastasis (PubMed 21814188). It is also implicated in chronic inflammatory conditions like rheumatoid arthritis and various fibrotic diseases, where it can either promote or limit fibrosis depending on the tissue context (PubMed 22431815). Because of its multifaceted role in disease progression, CCN1 is considered a promising therapeutic target, with research focusing on neutralizing monoclonal antibodies to block its interactions with integrins. These therapeutic approaches aim to disrupt pathological signaling while minimizing interference with the protein's normal regenerative functions.
Neutralization of secreted CCN1 to prevent binding to integrin receptors (αvβ3, αvβ5, α6β1, αIIbβ3) and heparan sulfate proteoglycans, thereby inhibiting pro-angiogenic, pro-proliferative, and pro-survival signaling pathways.
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