Disease relevance of IL8

• The latter is a requisite for epidemiological studies designed to test whether IL8 alleles are risk factors for acquiring or maintaining bacterial infections in production environments [1].
• A dose titration of P. haemolytica and E. coli endotoxins showed that a relatively low level of P. haemolytica endotoxin induced high levels of bovine IL-8 mRNA [2].
• We also studied the induction of IL-8 mRNA synthesis in bovine alveolar macrophages (BAM) stimulated with heat-killed Pasteurella haemolytica [2].
• Variables assessed included ingestion and killing of M avium subsp paratuberculosis; expression of tumor necrosis factor (TNF)-alpha, IL-12, IL-8, major histocompatability (MHC) class II, vacuolar H+ ATPase, and B cell CLL/lymphoma 2 (BCL-2); production of nitric oxide; acidification of phagosomes; and apoptosis of macrophages [3].
• Finally, PIMs contain TNF-alpha, and their depletion reduces cells positive for IL-8 (P < 0.05) and TNF-alpha (P < 0.05) and histopathological signs of acute lung inflammation in calves infected with Mannheimia hemolytica [4].

High impact information on IL8

• These results indicated that IL-8 participated in the impairment of renal functions in experimental acute immune complex-mediated glomerulonephritis through activating as well as recruiting neutrophils [5].
• Anti-IL-8 antibody treatment decreased the number of neutrophils in glomeruli by 40% and dramatically prevented the fusion of epithelial cell foot process [5].
• Prevention of proteinuria by the administration of anti-interleukin 8 antibody in experimental acute immune complex-induced glomerulonephritis [5].
• Enhanced SEMA5A induces expression of at least nine genes related to the host's immune response, including TNF-alpha and IL-8 [6].
• The combination of RA and IFN-alpha also acted synergistically on endothelial cells by reducing their responsiveness to both interleukin-8 and tumor conditioned media [7].

Chemical compound and disease context of IL8

• Bovine macrophages, when exposed to P. levii or E. coli LPS, produced mRNA for TNF-alpha, IL-1beta, and IL-8 [8].
• The in vivo infusion of IL8 increased the 35sulfate uptake by GBM and augmented the urinary albumin/creatinine ratio, suggesting that IL8 may induce albuminuria by altering the metabolism of the GBM sulfated compounds [9].
• Tilmicosin does not inhibit interleukin-8 gene expression in the bovine lung experimentally infected with Mannheimia (Pasteurella) haemolytica [10].
• Luminal perfusion of FBS significantly suppressed plasma IL-8 levels after 1 h of total ischemia and 1 h after initiation of reperfusion ( P< 0.05) [11].

Biological context of IL8

• Based on the breadth of germplasm in bovine diversity panel, the five haplotype structures for IL8 are estimated to represent >98% of those present in these DNA segments in commercial populations of U.S. beef cattle [1].
• Seven single-nucleotide polymorphism (SNP) markers were identified by sequencing two IL8 DNA segments amplified from the panel of 17 popular cattle breeds (MARC beef cattle diversity panel, version 2.1) [1].
• In the present study, we determined the nucleotide sequence for bovine IL-8 cDNA [2].
• The amino acid sequence encoded by this cDNA shares 76 and 87% homology with the human and swine IL-8 proteins, respectively [2].
• IL-8 encodes a proinflammatory cytokine that plays a central role in cell-mediated immunity by attracting and activating neutrophils in the early stages of host defense against bacterial invasion [1].

Anatomical context of IL8

• Interleukin-8 (IL-8) is a neutrophil and T-lymphocyte chemotactic and activating factor [2].
• It also resulted in an increase in expression of TNF-alpha, IL-12, IL-8, MHC class II, and vacuolar H+ ATPase; decrease in expression of BCL-2; increase in acidification of phagosomes; apoptosis of macrophages; and production of nitric oxide [3].
• Mesenteric lymph nodes draining sites of M. avium subsp. paratuberculosis infection expressed higher levels of IL-1alpha, IL-8, IL-2, and IL-10 mRNA than similar tissues from control uninfected cattle expressed [12].
• Among all the cytokines tested (IL-8, TNF alpha, MCP-1 and IL-1beta), we found that lysoPC most consistently stimulated human monocytes to produce IL-1beta in a dose and time dependent manner [13].
• OBJECTIVE: Several studies reported that the levels of proinflammatory cytokines such as TNF-alpha, IL-1beta, IL-6, and IL-8 are elevated in the cerebrospinal fluid (CSF) of patients after subarachnoid hemorrhage (SAH) [14].

Associations of IL8 with chemical compounds

• Neutrophil adhesion to ECMs altered responses to PAF and IL-8, although some functions were more responsive to modulation [15].
• Microparticles prepared from either chitosan or starch microparticles, applied apically, induced the basolateral release of IL-6 and IL-8 from polarized Calu-3 cells [16].
• RESULTS: Incubation with TNF-alpha, IL-8, PAF, and LPS primed neutrophils for oxygen radical release but caused minimal oxygen radical release by themselves [17].
• CpG-DNA-induced IL-8 mRNA expression and release was also blocked by the NO synthase inhibitor Nomega-nitro-L-arginine methyl ester [18].
• Recent studies indicate that peroxynitrite (ONOO-) may function as an intracellular signal for the production of IL-8, one of the key regulators of leukocyte trafficking in inflammation [18].

Regulatory relationships of IL8

• Although PAF and IL-8 inhibited TNF-alpha-induced ROS production in neutrophils adhered to collagen, fibronectin, and laminin, PAF enhanced ROS production strongly in HSP-adherent cells [15].
• This study investigated the effect of bovine interleukin-8 (IL-8) and granulocyte colony-stimulating factor (G-CSF) on priming and activation of bovine neutrophils in vitro and in vivo [19].

Other interactions of IL8

• IL-8 and ECIP-1 genes were placed on the cattle genetic map with single-nucleotide polymorphism (SNP) markers amplified from genomic DNA [20].
• A clear inflammatory response was shown by a significant (P < 0.05), dose dependent, increase of lactoferrin and IL-8 secretion within 24h in response to S. aureus or LPS [21].
• Lung tissue removed from neonatal calves with acute Mannheimia haemolytica pneumonia showed that rapid up-regulation of the basal mRNA expression of tracheal antimicrobial peptide (TAP), NF-kappa B, and intercellular adhesion molecule 1 occurred after infection; TAP and interleukin 8 expression were highly correlated [22].
• Tests were carried out using experimental NMR data for protein G, interleukin-8, villin 14T, and a 12 base-pair duplex of DNA, and simulated NMR data for bovine pancreatic trypsin inhibitor [23].
• Furthermore, the receptor shows 36% identity to both the human interleukin-8 (IL-8) and angiotensin II receptors but only 21% identity to the human NPY Y1 receptor [24].

Analytical, diagnostic and therapeutic context of IL8

• Molecular cloning and expression of bovine interleukin-8 [2].
• Quantitation of the cytokines TNF-alpha, IL-8 and IL-10 in bovine milk using real-time TaqMan PCR [25].
• Northern blot analysis of total RNA showed that P. haemolytica induced early, abundant, and consistent synthesis of IL-1, TNF-alpha, and IL-8 mRNA [26].
• The cytokine response of Mac-T cells to these treatments was quantified by measuring mRNA content of interleukin (IL)-1alpha, IL-1beta, IL-8, and tumor necrosis factor (TNF)-alpha by use of a quantitative reverse transcriptase-polymerase chain reaction assay [27].
• The supernatants were assayed for IL-8, monocyte chemotactic protein-(MCP)-1, and TNF-alpha by ELISA [28].

References