Disease relevance of ILK

• Chicken gizzard integrin-linked kinase cDNA was cloned, sequenced, expressed in E. coli, and shown to phosphorylate myosin light chain in the absence of Ca(2+) at Ser(19) and Thr(18) [1].
• We have previously shown that the administration of Salmonella enteritidis (SE)-immune lymphokines (ILK) into either 18-d-old developing embryos or day-of-hatch chicks and poults conferred increased resistance to SE organ invasion [2].
• We have previously reported that the prophylactic administration of factor(s) from T-cell supernatants derived from Salmonella enteritidis-immune chickens (ILK) have a favorable effect in controlling or eliminating salmonellosis in neonatal poultry [3].

High impact information on ILK

• Subcellular fractionation revealed two distinct populations of integrin-linked kinase, including a Triton X-100-insoluble component that phosphorylates myosin in a Ca(2+)-independent manner [1].
• Ca2+-independent smooth muscle contraction. a novel function for integrin-linked kinase [1].
• Here, we have demonstrated that overexpression of ILK was sufficient to induce actin filament rearrangements, to form cell motility structures, and to increase cell migration and invasion in a phosphatidylinositol 3-kinase (PI3K)-dependent manner [4].
• However, the signaling pathways involved in ILK-mediated cellular structure and motility remain to be elucidated [4].
• We have shown that overexpression of a dominant-negative ILK was sufficient to abolish fibronectin peptide (PHSRN)-induced rearrangements of actin filaments and cell migration and invasion [4].

Chemical compound and disease context of ILK

• We used an anti-inflammatory dose of dexamethasone (DEX) and Salmonella enteritidis (SE)-immune lymphokines (ILK) followed by oral SE challenge to chicks to determine the effects of these treatments on SE organ invasion and in vitro function of PMNs derived from peripheral blood [5].

Biological context of ILK

• MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected [6].
• Assays with the catalytic subunit of type 1 phosphatase indicated that only the C-terminal fragment of MYPT1 phosphorylated by zipper-interacting protein kinase, and ILK inhibited activity [6].
• Chemotaxis of PMNs derived from chicks treated with either ILK alone or DEX alone significantly increased 2-fold over control levels [5].
• On Day 18 of embryogenesis, injections were made into the amnion with either ILK or nonimmune ILK (NILK) or were not injected (untreated) [7].

Anatomical context of ILK

• We have shown that lymphokines (ILK) from T cells of birds immunized against Salmonella enteritidis (SE) induce a granulocytic (PMN) inflammatory response in chicks challenged with SE [8].
• P33(33-165) is chemotactic for heterophils both in vitro and in vivo, inducing an influx of heterophils into the peritoneum in a response similar to that observed with ILK [9].
• The injection of both the ILK and live SE (but not formalin-killed SE) resulted in an increased influx of inflammatory heterophils into the peritoneum that peaked at 4 h after the injections with no increase in peritoneal macrophages [10].

Associations of ILK with chemical compounds

• Integrin-linked kinase (ILK) is a cytoplasmic effector of integrin receptors [4].
• The heterophil accumulation was not influenced by polymyxin B, but was sensitive to heat treatment (100 C for 1 h) of the ILK, suggesting that lipopolysaccharide (LPS) did not contribute to the induced accumulation of heterophils [10].
• Treatment of the chicks with nordihydroguaiaretic acid or indomethacin did not abrogate the induced heterophil accumulation, suggesting that arachidonic acid metabolites were not involved in the SE/ILK-induced accumulation of peritoneal heterophils [10].

Other interactions of ILK

• Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase [6].

Analytical, diagnostic and therapeutic context of ILK

• ILK was associated with the MP holoenzyme, shown by Western blots and in-gel kinase assays [6].

References