Disease relevance of IL1A

• 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].
• No disruption of the BBB occurred for up to 2 h after the i.v. injection of 2 micrograms/mouse of IL-2 (10(5) U/kg of body weight), 2 micrograms of IL-1 alpha (10(7) U/kg), or 2 micrograms of IL-1 beta (10(7) U/kg) [2].
• Intraglomerular expressions of IL-1 alpha and platelet-derived growth factor (PDGF-B) mRNA in experimental immune complex-mediated glomerulonephritis [3].
• In this study we investigated intraglomerular expressions of PDGF-B and IL-1 alpha mRNA in mice with bovine serum albumin (BSA) nephritis, a model of immune complex-mediated glomerulonephritis, using the reverse transcription-polymerase chain reaction (RT-PCR) method [3].
• From these studies, we conclude that TNF and IL-1 alpha directly increase vascular endothelial cell permeability in vitro and speculate that these cytokines may be involved in the acute vascular endothelial injury associated with endotoxic shock [4].

High impact information on IL1A

• M40 cells were also resistant to growth inhibition by tumor necrosis factor alpha (TNF alpha) and interleukin-1 alpha (IL-1 alpha) but were inhibited by interferon-gamma (IFN gamma) and heparin [5].
• IRAP inhibited the binding of radiolabeled IL-1 alpha to rabbit articular chondrocytes [6].
• 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 [7].
• 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 [8].
• On the other hand, IL-1 alpha and beta did not affect the WRO cell growth [8].

Biological context of IL1A

• 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].
• 3. The genes for IL1A and IL1B were both assigned to Chromosome (Chr) 3, in the region q1.2-->q1.3 and q1.1-->q1.4, respectively [10].
• TNF alpha also demonstrated a neuropeptide-specific pattern of modulation of second-messenger effects on chromaffin cell neuropeptide levels similar to those seen with IL-1 alpha [11].

Anatomical context of IL1A

• The degree of T cell proliferation induced by infected cells was directly correlated with the amount of mRNA produced for the T cell stimulatory cytokines IL-1 alpha and IL-6, as assessed by a semiquantitative technique [12].
• In addition, bovine IL-1 beta mRNA is approx. 10-fold more abundant than IL-1 alpha mRNA in stimulated alveolar macrophages [1].
• Recombinant human interleukin-1 alpha (IL-1 alpha) increased prostacyclin synthesis in endothelial cells by 66% and prostaglandin E2 (PGE2) synthesis in fibroblasts by 91% [13].
• Such microspheres are avidly taken up by macrophages, and directing IL-1 alpha into these cells may activate them to participate in antitumor responses in vivo [14].
• A bovine hyaline cartilage proteinase inhibitor is active against some serine proteinases and inhibits the IL-1 alpha-mediated matrix degradation of bovine articular cartilage explants [15].

Associations of IL1A with chemical compounds

• 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].
• 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].
• The presence of a Factor Xa cleavage site in the IL-1 alpha proprotein suggests that Factor Xa may be involved in the processing of ovine IL-1 alpha to its mature form [17].
• 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 [18].
• Stimulation of VIP and substance P biosynthesis by forskolin was markedly enhanced by IL-1 alpha, while forskolin stimulation of enkephalin and neurotensin biosynthesis was unaffected [11].

Other interactions of IL1A

• There was an early increase in transcripts for genes encoding proinflammatory mediators (IFNG, IL1A, TNF, and IL12) in N'Dama by 14 days postinfection (dpi) compared with preinfection levels that was not detected in the susceptible Boran breed [19].
• TREATMENT: Fibronectin fragments or IL-1 alpha, which potently cause proteoglycan (PG) loss from cartilage, were added to cultures also containing the catabolism-blocking agents: insulin-like growth factor-1, or N-acetylcysteine, or Arg-Gly-Asp-Ser peptide, and the effects of these agents on blocking PG loss determined [20].

Analytical, diagnostic and therapeutic context of IL1A

• 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 [21].
• RT-PCR transcript analysis detected an increase in IL-1 alpha, IL-1 beta, IL-2, and IFN-gamma mRNA expression that was usually correlated with the detection of these soluble cytokines by the bioassays [21].
• Bovine articular chondrocytes treated with interleukin-1 alpha (IL-1 alpha) produced enhanced levels of stromelysin mRNA, however, Northern blots could not determine the percentage of cells responding [22].

References