ILK Research and renal disease.docVIP

 PAGE \* MERGEFORMAT 17 ILK Research and renal disease [Keywords:] ILK; foot cell; mesangial cells; renal interstitial fibrosis; Literature Review ILK (integrin linked kinase, ILK) is a multifunctional protein involved in various signal transduction pathways in the regulation of cell cycle, cell adhesion, matrix accumulation, tumorigenesis, embryonic development, plays an important role in such processes. Recent research found, ILK and kidney regulation of normal development and function is closely related to kidney disease in many of the occurrence and development. of ILK and kidney disease is on the research reviewed in the paper. 1 ILK molecular structure and biological effects 1.1 ILK and its binding protein structure ILK as a serine threonine protein kinase, in 1996 by Hannigan et al [1] the first time. It is evolutionarily conserved in Drosophila, C. elegans, mice and humans have homologous analogues. People the ILK gene located on chromosome 11p15.5-p15.4 [2]. ILK in the cDNA full-length 1.8kb, encoding 452 amino acids, relative molecular mass 59000.Northern hybridization showed that the vast majority of ILK in mammalian cells and tissues expression, especially in cardiac and skeletal muscle expression of high [1]. ILK molecule contains three domains: N terminal (33 164 amino acids) with four ankyrin repeats (ANK). By ANK, ILK binding energy and the adapter protein PINCH. PINCH LIM domain containing 5, the LIM1 and ILK binding. PINCH localization and function of ILK has an important regulatory role [3 4]. ANK also mediated by ILK and ILK associated phosphatase (ILKAP) interaction [5]. middle phosphatidylinositol binding domain ( also known as PH domain), located in the ILK 180 amino acid residues between 212 [1]. C-terminal domain with some overlap, ILK through it and phosphatidylinositol 3-hydroxy kinase (PI3K) product - PIP3 binding is activated [6]. ILK C-terminal amino acids containing 186,451 for the kinase catalytic domain, and in