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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1995-6-1
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pubmed:abstractText |
Interleukin-1 (IL-1) is primarily an inflammatory cytokine. Biologically, IL-1 is more closely related to tumor necrosis factor (TNF) than any other cytokine or interleukin, although the structure and receptors for IL-1 and TNF are clearly distinct. IL-1 is active in the low pM and fM range and IL-1 receptors (IL-1R) are expressed in most cells, although less than 100 receptors per cell is not an uncommon finding. Based on short-term blockade of IL-1 receptors in humans and animals and IL-1 beta knock-out mice, there is no evidence that IL-1 beta plays a role in development, or normal homeostasis such as metabolism, hematopoiesis, renal and hepatic function or regulation of blood pressure. On the other hand, IL-1 alpha is found constitutively produced by various epithelial cells, keratinocytes of the skin and in the brain. In these locations, IL-1 may contribute to cell growth and repair functions. During inflammation, injury, immunological challenge or infection, IL-1 is produced and because of its multiple biological properties, IL-1 must contribute to disease. Most studies on IL-1 are derived from experiments in which humans or animals are injected with IL-1 or IL-1 is added to cells in vitro. The biological properties of IL-1 suggest that its effects often mimic host responses to infection, inflammation, injury or immunologic challenge. Using specific IL-1 blockade, it is clear IL-1 is playing a critical role in some disease processes. This review will focus on IL-1 as a cytokine of primary and strategic importance to the initiation and progression of inflammatory and infectious diseases.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:issn |
1148-5493
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
517-31
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7727685-Animals,
pubmed-meshheading:7727685-Gene Expression,
pubmed-meshheading:7727685-Heart,
pubmed-meshheading:7727685-Humans,
pubmed-meshheading:7727685-Inflammation,
pubmed-meshheading:7727685-Interleukin-1,
pubmed-meshheading:7727685-Interleukin-6,
pubmed-meshheading:7727685-Muscle, Smooth, Vascular,
pubmed-meshheading:7727685-Receptors, Interleukin-1,
pubmed-meshheading:7727685-Recombinant Proteins,
pubmed-meshheading:7727685-Shock, Septic,
pubmed-meshheading:7727685-Tumor Necrosis Factor-alpha
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pubmed:articleTitle |
The biological properties of interleukin-1.
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pubmed:affiliation |
Department of Medicine, Tufts University School of Medicine, Boston, Massachusetts, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Review
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