Monoclonal antibody 5.5 reacts with p8,14, a myeloid molecule associated with some vascular endothelium

Hogg, Nancy; Allen, Catherine A.; Edgeworth, Jonathan D

doi:10.1002/eji.1830190615

Cited by 125 publications

(81 citation statements)

References 24 publications

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“…These 8 and 14 kD peptides belong to the S100 protein family which is a subfamily of proteins with Ca ϩϩ -binding motif, EF-hand in each molecule. 7) The subunits have also been termed L1 light and heavy chains, 8) p8 and p14, 9) migration inhibitory factor-related protein (MRP)8 and MRP14, 10) and calgranulin A and B.…”

Section: Introductionmentioning

confidence: 99%

Calprotectin (S100A8/S100A9), an Inflammatory Protein Complex from Neutrophils with a Broad Apoptosis-Inducing Activity

Yui

Nakatani

Mikami

2003

Biological & Pharmaceutical Bulletin

281

211

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Calprotectin, a complex of two calcium-binding proteins that belong to the S100 protein family, is abundant in the cytosolic fraction of neutrophils. A high level of calprotectin reportedly exists in extracellular fluid during various inflammatory conditions, such as rheumatoid arthritis, cystic fibrosis and abscesses. However, the exact biological role(s) of the factor is now under investigation. We recently observed that neutrophils contain a factor that shows growth-inhibitory and apoptosis-inducing activities against various cell types including tumor cells and normal fibroblasts, and we identified that factor as calprotectin. The findings suggest that calprotectin exerts a regulatory activity in inflammatory processes through its effect on the survival or growth states of cells participating in the inflammatory reaction. It is also possible that calprotectin, at a high concentration, might have a deleterious effect on fibroblasts and influence the recovery of inflammatory tissue. Therefore, the protein factor may be a new drug target to control inflammatory reactions. We found that a few of the Amaryllidaceae alkaloids effectively inhibited the growth-inhibitory and apoptosis-inducing activities of calprotectin. In this article, we focus on the biological functions of calprotectin in extracellular fluids, focusing on its apoptosis-inducing activity.

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Section: Introductionmentioning

confidence: 99%

Calprotectin (S100A8/S100A9), an Inflammatory Protein Complex from Neutrophils with a Broad Apoptosis-Inducing Activity

Yui

Nakatani

Mikami

2003

Biological & Pharmaceutical Bulletin

281

211

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“…The proteins MRP-8/14 can be found in the cytosol of these cells as monomers or heterodimers [5]. The sub-unity of 13.2 kDa, referred to as MRP-14 by Odink et al [2], was previously known as p14 [6], L1 heavy chain [7], calgranulin B [8], and the sub-unity of 10.8 kDa, correspondingly as MRP-8, p8, L1 light chain, calgranulin A. More recently the complex of these proteins was called calprotectin [9].…”

Section: Introductionmentioning

confidence: 99%

Antinociceptive effect of the calcium-binding protein MRP-14 and the role played by neutrophils on the control of inflammatory pain

Giorgi

Pagano

Dias

et al. 1998

Journal of Leukocyte Biology

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Macrophages secrete a variety of chemical mediators that play a central role in the pathophysiology of inflammatory pain. Therefore, the activation or deactivation of these cells in an inflammatory focus could modulate the intensity of the algogenic response. Based on these premises and on our previous demonstration that the calciumbinding protein MRP-14, highly expressed in neutrophils, deactivates activated macrophages in vitro, we decided to investigate the role of MRP-14 and of neutrophils in the control of inflammatory pain in mice. Our results show that this protein is endowed with antinociceptive activity. When tested in the writhing model it was able to inhibit pain response but did not change the behavior of the animals in the hot plate test. This observation indicates that MRP-14 down-regulates inflammatory but not central pain. Using a model of acute neutrophilic peritonitis induced by glycogen, a close correlation between neutrophil migration and antinociception was detected. Surgical adrenalectomy demonstrated that the antinociceptive response induced by glycogen was not due to endogenous liberation of glucocorticoids. The treatment of animals either with a monoclonal antibody anti-MRP-14 or a monoclonal antibody that depletes the animals of neutrophils reverts the antinociceptive response observed in the glycogen-induced peritonitis. These data define the calcium-binding protein MRP-14 as a novel mediator for the control of inflammatory pain and consequently discloses an anti-inflammatory role for the neutrophil. J. Leukoc. Biol. 64: 214-220; 1998.

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“…They are postulated to have intracellular functions either in control of the cell cycle, transduction of the Ca2+ signal, or inhibition of specific phosphorylation events [ 10,l I]. MRPS and MRP14 associate to heterocomplexes of various molecular ratios and are able to form a new epitope defined by the monoclonal antibody 27E 10 [12,13]. Elevated plasma levels of these two Ca2+ binding proteins can be found in different kinds of inflammatory diseases, such as cystic fibrosis [ 10,141, chronic bronchitis [ 151 and Crohn's disease [N.…”

Section: Introductionmentioning

confidence: 99%

The myeloic related protein MRP8/14 (27E10 antigen)— usefulness as a potential marker for disease activity in ulcerative colitis and putative biological function

Lügering

Stoll

Schmid

et al. 1995

Eur J Clin Investigation

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Abstract. MRP8, MRP14 and their heterodimer MRP8/14 (27E10 antigen) are myeloic related proteins which have been shown to have a major role in inflammatory and immunological responses. In the present study monospecific antibodies against MRPs were used to investigate immunohistochemically the distribution of these proteins in routinely processed bowel tissues from 23 patients with ulcerative colitis (UC). MRP8, MRP14 and their heterocomplex MRP8/l4 were demonstrated in the majority of granulocytes and macrophages in tissues of patients with active UC. Furthermore by employing the ELISA technique we measured MRP8/14 serum levels in 62 patients with UC and the results were compared with those for healthy controls. Disease activities were determined by established clinical activity indices. Serum MRP8/14 concentrations were significantly ( P < 0.0001) increased in patients with active ulcerative colitis. No enhancement of serum levels were found for MRP14 and MRP8 alone, respectively. The follow-up of individual patients with initially active disease showed a decrease of MRP8/14 serum levels in parallel with clinical improvement following the start of therapy. It is thus concluded that MRP8/14 accurately reflects the degree of disease activity in UC. Further, possible biological function of MRPs seems to be associated with the heterodimeric form (27E10 antigen) rather than with individual proteins. Our morphological results confirm the finding of enhanced MRP8/14 serum levels in patients with active UC.

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Monoclonal antibody 5.5 reacts with p8,14, a myeloid molecule associated with some vascular endothelium

Cited by 125 publications

References 24 publications

Calprotectin (S100A8/S100A9), an Inflammatory Protein Complex from Neutrophils with a Broad Apoptosis-Inducing Activity

Calprotectin (S100A8/S100A9), an Inflammatory Protein Complex from Neutrophils with a Broad Apoptosis-Inducing Activity

Antinociceptive effect of the calcium-binding protein MRP-14 and the role played by neutrophils on the control of inflammatory pain

The myeloic related protein MRP8/14 (27E10 antigen)— usefulness as a potential marker for disease activity in ulcerative colitis and putative biological function

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