Integrin-linked kinase (ILK) is a multifunctional molecule involved in cell-matrix interactions, cell adhesion, and anchorage-dependent cell growth. It functions as both a signal transducer and a scaffold protein within the ILK-PINCH-Parvin complex, regulating crucial cellular processes such as proliferation, survival, differentiation, migration, invasion, and angiogenesis. These processes impact systemic changes in multiple organs including the kidney, heart, muscle, skin, and vascular system, and are also vital during embryonal development [1].

In endothelial cell-specific ILK conditional knock-out (ecILK cKO) mice, deletion of coronary endothelial ILK significantly impaired cardiac function, leading to systolic and diastolic dysfunction, extensive extracellular matrix remodelling, perivascular fibrosis, and features of coronary microvascular disease. Endothelial cells in these mice underwent endothelial-to-mesenchymal transition (endMT), indicating that ILK is a crucial regulator of microvascular endothelial homeostasis [2].

In conclusion, ILK is essential for maintaining normal physiological functions through its role in multiple cellular processes. The use of ecILK cKO mouse models has revealed its significance in preventing microvascular dysfunction and cardiac remodelling, contributing to the understanding of its role in cardiovascular diseases.