Disease relevance of IL1B

• Sequences encoding mature bovine IL-1 alpha and IL-1 beta were inserted into E. coli expression plasmids and biologically active proteins were synthesized as judged by the ability of the recombinant proteins to induce proliferation of bovine thymocytes [1].
• Infection of bovine brain microvessel endothelial cells with Cowdria ruminantium elicits IL-1 beta, -6, and -8 mRNA production and expression of an unusual MHC class II DQ alpha transcript [2].
• We then used the cloned genes as probes in Northern (RNA) blots and investigated the kinetics of TNF-alpha and IL-1 beta mRNA expression in bovine alveolar macrophages stimulated with purified LPS from Pasteurella haemolytica 12296 [3].
• Heparin fails to potentiate the effects of IL-1 beta-mediated bone resorption of fetal rat long bones in vitro [4].
• The inhibition of the catabolic effects induced by IL1-beta and LPS appears related to glucosamine toxicity [5].

High impact information on IL1B

• Treatment of cultured bovine brain microvascular endothelial cells (BMECs) with interleukin 1 beta (IL-1 beta), an inflammatory cytokine, was shown to induce the accumulation of sulfoglucuronosyl paragloboside (SGPG), a glycolipid bearing the HNK-1 epitope [6].
• Attachment of human lymphocytes to the IL-1 beta-activated BMEC cells could be blocked either by incubation of the human lymphocytes with an anti-L-selectin antibody or by application of an anti-SGPG antibody to the BMECs [6].
• Treatment of BASMCs with tumor necrosis factor-alpha (TNF-alpha) or interleukin-1 beta (IL-1 beta) resulted in a significant increase in L-arginine transport (approximately 20%) and in the induction of NO release [7].
• IL-1 beta is a proinflammatory cytokine secreted chiefly by monocytes and macrophages [8].
• Infection induced the production of IL-1 beta, -6, and -8 mRNAs, and this effect was potentiated by IFN-gamma [2].

Biological context of IL1B

• The cytogenetic position of PAX8 on BTA 11 and on its homologue OAR 3p lies in the region where the interleukin beta (IL1B) gene has been previously located, (BTA 11q22. 1-->q22.3 and OAR 3p25-->q26 respectively; Lòpez-Corrales et al., 1998) [9].
• The results indicated that PAX8 as well as interleukin beta and interleukin alpha (IL1B and IL1A) genes detected on the human chromosome segment HSA 2q13-->q21 maintain a similar order and location in these three related species [9].
• Bovine YAC and cosmid clones were used as FISH probes to determine the order (centromere to telomere) of four of these genes on OAR 2q, as well as the location of IL1B on OAR 3p [10].
• The effect of LPS on TNF-alpha and IL-1 beta gene expression was dose dependent, and induction was observed at a concentration of 0.01 microgram/ml [3].
• Bovine tumor necrosis factor alpha (TNF-alpha) and interleukin-1 beta (IL-1 beta) cDNAs were generated by reverse transcription and then by PCR amplification from lipopolysaccharide (LPS)-stimulated alveolar macrophage RNA [3].

Anatomical context of IL1B

• In contrast, neither IL-1 alpha nor IL-1 beta induced astrocyte proliferation in serum-free medium but showed some synergistic effect with serum after 72 h [11].
• Using human IL-1 alpha and IL-1 beta probes, cDNAs for the corresponding bovine genes were isolated from an alveolar macrophage library [1].
• The suppressive activity of IL-1 beta was more potent than that of IL-1 alpha in spite of the same lymphocytes activating factor (LAF) activity [12].
• Accordingly, we investigated the effects of recombinant human interleukin-1 alpha (IL-1 alpha), recombinant human interleukin-1 beta (IL-1 beta), and recombinant human tumor necrosis factor alpha (TNF alpha) on bovine nasal chondrocyte (BNC) responsiveness [13].
• Functional studies of bovine alveolar neutrophils elicited with recombinant bovine IL-1 beta [14].

Associations of IL1B with chemical compounds

• Bradykinin, acetylcholine, and IL1B EC-dependent effects were reversed with the nitric oxide (NO) synthase inhibitor L-NNA [15].
• As a result of the amplification of specific cDNAs by 35 cycles of PCR, the IL-1 alpha mRNA was detected from 0.01 ng of poly (A) + RNA, and IL-1 beta mRNA was detected from 0.1 pg of poly (A) + RNA isolated from PBMCs stimulated with lipopolysaccharide (LPS) for 4 h [16].
• Poly (A) + RNAs isolated from PBMCs by guanidium thiocyanate/oligo (dT)-cellulose chromatography extraction, were reverse-transcribed and the complementary DNAs amplified in a polymerase chain reaction primed with bovine IL-1 alpha and IL-1 beta sequence-specific primers [16].
• IL-1 alpha and IL-1 beta stimulated a time (0-72 hr) and concentration-dependent (0.01-10 ng/ml) production of collagenase, gelatinase, caseinase, and prostaglandin E2 (PGE2) in BNC monolayer cultures [13].
• IL-1 beta (0.03 U/L) stimulated nitrite production by BVSMCs [17].

Regulatory relationships of IL1B

• In all cultures of marrow from postmenopausal women, IL-1 beta suppressed IGFBP-3 secretion to either undetectable levels or levels between 11% and 35% of control [18].

Other interactions of IL1B

• The level of HSP72 expression was not elevated by treatment with interleuken (IL)-1 alpha (10 ng ml-1), IL-1 beta (10 ng ml-1), tumour necrosis factor (TNF)-alpha (200 ng ml-1), or TNF-beta (200 ng ml-1) [19].
• No statistical differences were observed in the expression of interferon-gamma, IL-1 beta, TNF-alpha, and GM-CSF among lepromatous, tuberculoid, and noninfected groups [20].
• In particular, S. uberis infection was characterized by the sustained elevation of higher milk levels of IL-1 beta, IL-10, IL-12, IFN-gamma, and C5a, relative to S. marcescens infection [21].
• CONCLUSIONS: Our data suggest that proteoglycan and collagen degradation are regulated through different mechanisms: IL-1 beta induces the synthesis of active enzymes that degrade proteoglycans, such as 'aggrecanase', and inactive proMMPs [22].
• A positive correlation was observed between the concentrations of IL-1ra and IL-1 beta in the colostrum samples [23].

Analytical, diagnostic and therapeutic context of IL1B

• Using 5 ng of poly (A) + RNA isolated from fresh bovine PBMCs unstimulated with any mitogen as template for RT-PCR, both IL-1 alpha and IL-1 beta mRNAs were detected at a low level [16].
• Specificity of the cDNA fragments was verified by sequence analysis based on known bovine IL-1 alpha, IL-1 beta, IL-2, and IFN-gamma gene sequences [24].
• A 17-kd human recombinant IL-1 receptor antagonist protein (IRAP) caused a concentration-dependent (0.2-200 ng/ml) suppression of the effects of IL-1 alpha and IL-1 beta in cartilage organ cultures [25].
• However, when these drugs were added to the stimulus for IL-1 beta production, there was a significant increase in both IL-1 beta release and total IL-1 beta production, as measured by ELISA [8].
• The expressed proteins were confirmed as TNF-alpha and IL-1 beta by Western blot (immunoblot) analysis and bioassays [3].

References