Phagocyte-specific S100 proteins: a novel group of proinflammatory molecules (Q28191271)

Europe PubMed Central

title

Phagocyte-specific S100 proteins: a novel group of proinflammatory molecules (English)

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4

Cord Sunderkötter

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author name string

Johannes Roth

1

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Thomas Vogl

2

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Clemens Sorg

3

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Cord Sunderkötter

Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis

4

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language of work or name

English

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publication date

April 2003

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published in

Trends in Immunology

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volume

24

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issue

4

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page(s)

155-8

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cites work

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7 January 2021

Loss of S100A9 (MRP14) results in reduced interleukin-8-induced CD11b surface expression, a polarized microfilament system, and diminished responsiveness to chemoattractants in vitro

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Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9)

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High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14.

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Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry

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The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells

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Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells

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Regulation and proinflammatory properties of the chemotactic protein, CP-10.

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The Ca2+-binding proteins S100A8 and S100A9 are encoded by novel injury-regulated genes

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Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells

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Hyperzincaemia and hypercalprotectinaemia: a new disorder of zinc metabolism.

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Growth-inhibitory and apoptosis-inducing activities of calprotectin derived from inflammatory exudate cells on normal fibroblasts: regulation by metal ions

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S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14

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Calcium-dependent secretion in human neutrophils: a proteomic approach

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RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides

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The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses

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Receptor-dependent cell stress and amyloid accumulation in systemic amyloidosis

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Blockade of RAGE–amphoterin signalling suppresses tumour growth and metastases

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Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease

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10.1016/S1471-4906(03)00062-0

Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

1372306

1372306

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference