A new nomenclature for IL-1-family genes

Sims, John E.; Pan, Yang; Smith, Dirk E.; Nicklin, Martin J.H.; Barton, Jenny L.; Bazán, J. Fernando; Kastelein, Robert A.; Busfield, Samantha J.; Ford, J. E.; Lin, Huiyun; Mulero, Julio J.; Kumar, Sanjay; Pan, James; Young, Peter R.

doi:10.1016/s1471-4906(01)02040-3

Cited by 156 publications

(109 citation statements)

References 6 publications

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“…The IL-1 and FGF gene families are composed of at least 10 and 23 members, respectively (10)(11)(12)(13), and membership is defined by structural homology with the prototype members of each gene family, namely IL-1␣͞IL-1␤ and FGF1͞FGF2. Although the IL-1 and FGF prototypes exhibit limited primary sequence homology (14), these prototype polypeptides are viewed as crystallographic homologs (15).…”

mentioning

confidence: 99%

“…Furthermore, the IL-1 and FGF prototypes do not contain classical signal peptide sequences to direct their export through the endoplasmic reticulum-Golgi apparatus (16), and although only 3 of the 23 FGF genes lack this feature, 8 of the 10 IL-1 genes lack a classical signal peptide sequence. Because it is well established that the IL-1 and FGF prototypes function in the extracellular compartment as ligands for high-affinity cell-surface receptors (11,13), the identification of the mechanism(s) used by the IL-1 and FGF prototypes for nonclassical release could potentially yield new insight into proinflammatory and angiogenic disorders.…”

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confidence: 99%

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Copper chelation represses the vascular response to injury

Mandinov

Mandinova²,

Kyurkchiev³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

122

117

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The induction of an acute inflammatory response followed by the release of polypeptide cytokines and growth factors from peripheral blood monocytes has been implicated in mediating the response to vascular injury. Because the Cu 2؉ -binding proteins IL-1␣ and fibroblast growth factor 1 are exported into the extracellular compartment in a stress-dependent manner by using intracellular Cu 2؉ to facilitate the formation of S100A13 heterotetrameric complexes and these signal peptideless polypeptides have been implicated as regulators of vascular injury in vivo, we examined the ability of Cu 2؉ chelation to repress neointimal thickening in response to injury. We observed that the oral administration of the Cu 2؉ chelator tetrathiomolybdate was able to reduce neointimal thickening after balloon injury in the rat. Interestingly, although immunohistochemical analysis of control neointimal sections exhibited prominent staining for MAC1, IL-1␣, S100A13, and the acidic phospholipid phosphatidylserine, similar sections obtained from tetrathiomolybdate-treated animals did not. Further, adenoviral gene transfer of the IL-1 receptor antagonist during vascular injury also significantly reduced the area of neointimal thickening. Our data suggest that intracellular copper may be involved in mediating the response to injury in vivo by its ability to regulate the stress-induced release of IL-1␣ by using the nonclassical export mechanism employed by human peripheral blood mononuclear cells in vitro.phosphatidylserine ͉ interleukin 1 ͉ restenosis ͉ tetrathiomolybdate ͉ fibroblast growth factor

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mentioning

confidence: 99%

mentioning

confidence: 99%

Copper chelation represses the vascular response to injury

Mandinov

Mandinova²,

Kyurkchiev³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

122

117

View full text Add to dashboard Cite

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“…Состав семейства ИЛ-1 В настоящее время на основе функциональной специ-фичности, гомологии аминокислотных последова-тельностей, третичной белковой структуры, простран-ственной конфигурации, расположения гена и рецеп-торного взаимодействия ряд цитокиновых молекул объе-динен в семейство ИЛ-1 [2]. Наиболее изученными из них являются ИЛ-1α, ИЛ-1β, рецепторный антаго-нист ИЛ-1 (ИЛ-1Ra).…”

Section: вестник рамн /2012/ № 11unclassified

The Role of Interleukin-1 and Associated Cytokines in Gastric Carcinogenesis

Матвеева

Мосина

2012

Annals RAMS

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“…Like most members of the IL-1 family, IL-18 lacks a signal peptide. Recently, several new members of the IL-1 family were identified by sequence homology, some of which have a determined biological function, whereas others remain without a known activity (7)(8)(9). One of the members, IL-1H4, was found to bind IL-18R␣, but its biological function has yet to be determined (7,10,11).…”

Section: Identification Of a Critical Ig-like Domain In Il-18 Receptomentioning

confidence: 99%

Identification of a Critical Ig-Like Domain in IL-18 Receptor α and Characterization of a Functional IL-18 Receptor Complex

Azam

Novick

Bufler

et al. 2003

The Journal of Immunology

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Steady state mRNA levels in various human tissues reveal that the proinflammatory cytokine IL-18 is constitutively and ubiquitously expressed. However, limited IL-18R α-chain (IL-18Rα) expression in tissues may restrict ligand-acting sites and contribute to a specific response for IL-18. To study the IL-18R complex, [125I]IL-18 was studied for binding to the cell surface receptors of IL-18-responsive NK and macrophagic KG-1 cells. After cross-linking, [125I]IL-18 formed three IL-18R complexes with sizes of approximately 93, 160, and 220 kDa. In KG-1 cells, Scatchard analysis revealed the presence of 135 binding sites/cell, with an apparent dissociation constant (Kd) of 250 pM; in NK cells, there were 350 binding sites per cell with an apparent Kd of 146 pM. Each domain of extracellular IL-18Rα was cloned and individually expressed in Escherichia coli. An mAb specifically recognized the membrane-proximal third domain; this mAb blocked IL-18-induced IFN-γ production in NK cells. Furthermore, deletion of the membrane-proximal third domain of IL-18Rα prevented the formation of IL-18R ternary complex with IL-18R β-chain. The present studies demonstrate that the biologically active IL-18R complex requires the membrane-proximal third Ig-like domain in IL-18Rα for the formation of IL-18R ternary complex as well as for signal transduction involved in IL-18-induced IFN-γ in NK cells.

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A new nomenclature for IL-1-family genes

Cited by 156 publications

References 6 publications

Copper chelation represses the vascular response to injury

Copper chelation represses the vascular response to injury

The Role of Interleukin-1 and Associated Cytokines in Gastric Carcinogenesis

Identification of a Critical Ig-Like Domain in IL-18 Receptor α and Characterization of a Functional IL-18 Receptor Complex

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