Cldn34c2, a member of the claudin family, holds a critical role in cellular function by participating in bicellular tight junction assembly and cell adhesion. The protein is primarily localized to the plasma membrane, where it contributes to the formation of tight junctions between adjacent cells. Tight junctions are crucial components of epithelial tissues, serving as barriers that regulate the passage of ions, molecules, and cells through the intercellular space. In particular, Cldn34c2's involvement in bicellular tight junction assembly underscores its significance in maintaining the integrity of these cellular barriers. The proper functioning of tight junctions is essential for diverse physiological processes, including the establishment of tissue boundaries, prevention of paracellular leakage, and regulation of cell polarity. Through its predicted role in cell adhesion, Cldn34c2 plays a crucial part in cellular interactions, influencing overall tissue architecture and function.
Inhibition of Cldn34c2 involves the modulation of various cellular processes and signaling pathways that contribute to tight junction assembly and cell adhesion. These mechanisms of inhibition target specific cellular components and pathways associated with Cldn34c2 function. For instance, compounds influencing actomyosin contractility, such as Rho kinase (ROCK) inhibitors, indirectly impact Cldn34c2-associated tight junction dynamics. Modulators of protein phosphorylation, including protein kinase C (PKC) inhibitors and broad-spectrum kinase inhibitors, alter the phosphorylation status of tight junction proteins, thereby affecting Cldn34c2 function in cell adhesion. Additionally, inhibitors of key signaling pathways, such as the PI3K-Akt pathway and the TGF-β receptor, disrupt downstream cascades linked to Cldn34c2, influencing its participation in bicellular tight junction assembly. The diverse array of inhibitors reflects the multifaceted nature of Cldn34c2's involvement in cellular processes, highlighting the intricate regulatory networks that govern tight junction formation and cell adhesion. Understanding these mechanisms of inhibition contributes to a comprehensive appreciation of Cldn34c2's role in cellular physiology and provides insights into potential strategies for modulating its function for various research purposes.
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