Integrin-linked kinase (ILK) is a multifunctional protein involved in cell-matrix interactions, cell adhesion, and anchorage-dependent cell growth. It functions as a signal transducer and a scaffold protein within the ILK-PINCH-Parvin complex, and is associated with integrin and growth factor receptor signalling pathways. ILK is crucial for cellular processes like proliferation, survival, differentiation, migration, invasion, and angiogenesis, and its dysfunction is linked to various diseases including cancer [1,3,4].

In endothelial cell-specific ILK conditional knock-out (ecILK cKO) mice, endothelial ILK deletion significantly impaired cardiac function, leading to systolic and diastolic dysfunction, extensive extracellular matrix remodelling, perivascular fibrosis, and early ischaemic-like events. The mice also exhibited features of coronary microvascular disease, and endothelial cells underwent endothelial-to-mesenchymal transition (endMT), indicating that endothelial ILK is a crucial regulator of microvascular endothelial homeostasis [2]. In cisplatin-resistant ovarian cancer cells, targeting ILK by small-interfering RNA reduced cell growth and invasion, and increased apoptosis. Phosphorylated ILK levels were higher in cisplatin-resistant ovarian cancer cells and tumor tissue compared to sensitive cells and normal ovarian epithelium [5].

In conclusion, ILK is essential for maintaining normal physiological functions in various tissues, especially in microvascular endothelial homeostasis. Studies using ILK KO/CKO mouse models have revealed its significant role in cardiac function and microvascular diseases, as well as in cancer development. Understanding ILK's functions can potentially provide new therapeutic strategies for related diseases.