PMID: 16978691, The two agonists, IL-1greek alpha and IL-1beta, both initially are synthesized as 31 kDa precursors, pro-IL-1greek small letter alpha and pro-IL-1¦Â, which are then cleaved into their mature 17 kDa forms PMID: 16978691 IL-18 is cleaved via the same enzyme, IL-1 converting enzyme (ICE), as IL-1¦Â, although the biological effects can differ.

PMID: 16978691,12244123,10077553 FN contains multiple binding sites which bind to other molecules such as heparin (heparin I and II), collagen (Type I module, domains 6?9 (I6¡Ý9) and Type II module, domains 1 and 2 (II1,2)), fibrin (Fibrin I and II), and cellular surface integrin receptors which bind via the cell-binding repeats (I1¡Ý9,II1,2, and III9¡Ý10)

PMID:16978691 Collagen was found to stimulate the greatest mRNA expression, followed by FN, while fibrin was found to induce little to no IL-1beta mRNA expression.

PMID:16978691 Collagen was found to stimulate the greatest mRNA expression, followed by FN, while fibrin was found to induce little to no IL-1beta mRNA expression.

PMID: 16978691,1386877 GM-CSF and TNF-alpha may also further induce the production of IL-1ra

PMID: 16978691,1386877 GM-CSF and TNF-alpha may also further induce the production of IL-1ra

PMID: 16978691,1386877 GM-CSF and TNF-alpha may also further induce the production of IL-1ra

PMID: 16978691,1386877 GM-CSF and TNF-alpha may also further induce the production of IL-1ra

PMID: 16978691 Bacteria can bind to the surface receptors of host cells, including macrophages, through bacterial fimbriae.

PMID: 16978691 Beta1 integrin binding with anti-integrin ¦Â1 antibody resulted in an increase in phosphorylation of pp76 and an increase in IL-1beta mRNA expression.

PMID: 16978691 Beta1 integrin binding with anti-integrin ¦Â1 antibody resulted in an increase in phosphorylation of pp76 and an increase in IL-1beta mRNA expression.

PMID: 16978691, The two agonists, IL-1greek alpha and IL-1beta, both initially are synthesized as 31 kDa precursors, pro-IL-1greek small letter alpha and pro-IL-1¦Â, which are then cleaved into their mature 17 kDa forms

PMID: 16978691 Beta1 integrin binding with anti-integrin ¦Â1 antibody resulted in an increase in phosphorylation of pp76 and an increase in IL-1beta mRNA expression.

PMID: 16978691 In parallel with the IL-1beta study, anti-beta1 integrin and anti-beta3 integrin antibody pre-treatment also resulted in a general decrease in matrix metalloprotease-2 (MMP-2) and matrix metalloprotease-9 (MMP-9) secretion and mRNA expression.

PMID: 16978691 In parallel with the IL-1beta study, anti-beta1 integrin and anti-beta3 integrin antibody pre-treatment also resulted in a general decrease in matrix metalloprotease-2 (MMP-2) and matrix metalloprotease-9 (MMP-9) secretion and mRNA expression.

PMID: 16978691,1386877 GM-CSF and TNF-alpha may also further induce the production of IL-1ra

PMID: 16978691 IL-1 alpha, IL-1beta, and IL-1ra all bind to the biologically active IL-1RI receptor, however IL-1¦Â binds somewhat less efficiently than the other cytokines.

PMID: 16978691 IL-1 alpha, IL-1beta, and IL-1ra all bind to the biologically active IL-1RI receptor, however IL-1¦Â binds somewhat less efficiently than the other cytokines.

PMID: 16978691 IL-1RII binds 10?100 times more preferentially to IL-1¦Â than IL-1 alpha or IL-1ra and in soluble form can even bind pro-IL-1beta

PMID: 16978691 IL-1RII binds 10?100 times more preferentially to IL-1¦Â than IL-1 alpha or IL-1ra and in soluble form can even bind pro-IL-1beta

PMID: 16978691,12244123,10077553 FN contains multiple binding sites which bind to other molecules such as heparin (heparin I and II), collagen (Type I module, domains 6?9 (I6¡Ý9) and Type II module, domains 1 and 2 (II1,2)), fibrin (Fibrin I and II), and cellular surface integrin receptors which bind via the cell-binding repeats (I1¡Ý9,II1,2, and III9¡Ý10)

PMID: 16978691,12244123,10077553 FN contains multiple binding sites which bind to other molecules such as heparin (heparin I and II), collagen (Type I module, domains 6?9 (I6¡Ý9) and Type II module, domains 1 and 2 (II1,2)), fibrin (Fibrin I and II), and cellular surface integrin receptors which bind via the cell-binding repeats (I1¡Ý9,II1,2, and III9¡Ý10)

PMID: 16978691,12244123,10077553 FN contains multiple binding sites which bind to other molecules such as heparin (heparin I and II), collagen (Type I module, domains 6?9 (I6¡Ý9) and Type II module, domains 1 and 2 (II1,2)), fibrin (Fibrin I and II), and cellular surface integrin receptors which bind via the cell-binding repeats (I1¡Ý9,II1,2, and III9¡Ý10)