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| - | '''Interleukin-1 beta(IL-1β)''' | + | '''HUMAN INTERLEUKIN-1 BETA''' |
| | == Headline text == | | == Headline text == |
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| - | IL-1β along with IL-1α is one of cytokines secreted from local inflammatory cells, are belong to IL-1 family. while the former is dominate and they have been distinguished by the cell with which they interact. IL-1β precursor need to be activated by protease (convertase or IL-1β converting enzyme) to form IL-1 active species. The active mature IL-1 mediates several components of the acute phase reaction, including the febrile response, secretion of adrenocorticotropic hormone (ACIH), and the synthesis of acute phase proteins.
| + | <Structure load='9ilb' size='500' frame='true' align='right' caption='HUMAN INTERLEUKIN-1 BETA' scene='57/571319/Scene1/1' /> |
| - | interleukin 1(IL-1) cytokines could mediate innate and adaptive immunity
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| - | which was first found in 1988 in
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| - | [Acute-phase proteins are a class of proteins whose plasma concentrations increase (positive acute-phase proteins) or decrease (negative acute-phase proteins) in response to inflammation. This response is called the acute-phase reaction (also called acute-phase response).
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| - | Inflammatory cells and red blood cells
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| - | In response to injury, local inflammatory cells (neutrophil granulocytes and macrophages) secrete a number of cytokines into the bloodstream, most notable of which are the interleukins IL-1, IL-6 and IL-8, and TNF-α. The liver responds by producing a large number of acute-phase reactants. At the same time, the production of a number of other proteins is reduced; these are, therefore, referred to as "negative" acute-phase reactants. Increased acute phase proteins from the liver may also contribute to the promotion of sepsis]
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| - | History
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| - | THREE-DIMENSIONAL STRUCTURE OF IL-1β
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| - | The molecule resembles a conical barrel with a shallow open face on one end and a closed face on the other. Themolecule contains 12 antiparallel 13-strands, where six of these (131, 14, 15, 18, 19, and 1312) constitute an antiparallel 1 barrel. The overall structure of the molecule consists of three similar fragments (Fl, F2, F3), each containing two pairs of 1 strands. Three pairs of 1 strands (one pair from each of the fragments) form the six stranded barrel; the other three pairs cover one end of the barrel, referred to as the "closed end." The amino and carboxy termini are close to each other at the "open end" of the barrel. The molecule has internal pseudo threefold symmetry, with each subunit (Fl, F2, F3) having a 13L13 motif. There are five 1-hairpins in this molecule, two of them in the open end and three at the closed end. The polypeptide a-carbon backbone of IL13, viewed perpendicular to the barrel axis, is shown in Fig. 1. 24 hydrophobic side chains line the inner surface of the barrel and both the ends of the barrel have concentrations of exposed polar residues.
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| - | pdb: 4DEP(Structure of the IL-1b signaling complex)
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| - | 9ILB(HUMAN INTERLEUKIN-1 BETA)
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| - | 1ITB(TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA)
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| - | Function and property Linker
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| - | we demonstrate that the inactive cytokine, 31 kD interleukin 18 (IL-lfl), can be converted rapidly to an 18 kD biologically active species by human mast cell chymase
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| - | [Interleukin 1 was discovered by Igal Gery in 1972.[5][6][7] He named it lymphocyte-activating factor (LAF) because it was a lymphocyte mitogen. It was not until 1985 that interleukin 1 was discovered to consist of two distinct proteins, now called interleukin-1 alpha and interleukin-1 beta.[2]
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| - | IL-1β is a member of the interleukin 1 family of cytokines. This cytokine is produced by activated macrophages as a proprotein, which is proteolytically processed to its active form by caspase 1 (CASP1/ICE). This cytokine is an important mediator of the inflammatory response, and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis. The induction of cyclooxygenase-2 (PTGS2/COX2) by this cytokine in the central nervous system (CNS) is found to contribute to inflammatory pain hypersensitivity. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2.[8]
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| - | IL-1β is biosynthesized as a 31KDa polypeptide precursor and processed by converting enzyme to cause proinflammatory reaction.
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| - | Clinical significance: Biomarker
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| - | recent studies have implicated IL-1 as an autocrine growth factorin certain acute and chronic myelocytic
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| - | leukemias.
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| - | The molecular cloning of a protease that generates active IL-1β provides new insight into IL-1 biology and offers a new target for the development of therapeutic agents
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| - | IL-1β receptor linker
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| - | binding site
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| - | Reference
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| - | Ternary complex paradigm
| + | <scene name='57/571319/Scene1/1'>HUMAN INTERLEUKIN-1 BETA</scene> |
| - | [[Image:Ternary complex paradigm.png||300px|left|]]
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| - | <scene name='57/571319/Human_il_1beta/1'>TextToBeDisplayed</scene> | + | '''TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA''' |
| - | <Structure load='9ILB' size='400' frame='true' align='right' caption='Human Interleukin-1 Beta='/> | + | == Headline text == |
| - | <scene name='57/571319/Scene_2/1'>TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA</scene> | + | |
| | + | <Structure load='1ITB' size='500' frame='true' align='right' caption='TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA' scene='57/571319/Scene_2/2' /> |
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| | + | <scene name='57/571319/Scene_2/2'>TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA</scene> |
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| | + | '''STRUCTURE OF THE INTERLEUKIN-1BETA SIGNALING COMPLEX''' |
| | + | == Headline text == |
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| | + | <Structure load='4DEP' size='500' frame='true' align='right' caption='INTERLEUKIN-1BETA SIGNALING COMPLEX' scene='57/571319/Scene_3/1' /> |
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| | + | <scene name='57/571319/Scene_3/1'>INTERLEUKIN-1BETA SIGNALING COMPLEX</scene> |
