Epidermal and dermal distribution of a myelomonocytic antigen (L1) shared by epithelial cells in various inflammatory skin diseases

Gabrielsen, Tor-Øivind; Dale, Inge; Brandtzæg, Per; Hoel, Per Sigurd; Fagerhol, Magne K.; Larsen, Tove; Thune, P

doi:10.1016/s0190-9622(86)70152-7

Cited by 73 publications

(36 citation statements)

References 10 publications

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“…However, deregulated expression of several members of the S100 family, including S100A8 and S100A9, under various pathologic conditions has been reported (7,35). Besides the well-documented expression in inflammatory skin diseases (15), S100A8 and S100A9 and other members of the S100 family recently have been associated with rheumatoid arthritis (36), psoriasis (37), cutaneous wound repair (16), and various experimental and human neoplasms (4, 17 -19). It is noteworthy that the patterns of differential gene expression in cancer, particularly in prostate and liver cancer, strongly correlate with the pattern of differential gene expression during wound-healing processes (38).…”

Section: Resultsmentioning

confidence: 99%

“…The proteins were suggested to form S100A8/S100A9 heterocomplexes (12,13), which were shown to be secreted by activated monocytes (14). Expression of S100A8 and S100A9 in epithelial tissues was first described in context with squamous epithelia, e.g., various inflammatory skin diseases (15), and with murine and human wound repair (16). More recently, an association of S100 protein expression with adenocarcinomas in humans has emerged.…”

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confidence: 99%

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Calcium-Binding Proteins S100A8 and S100A9 as Novel Diagnostic Markers in Human Prostate Cancer

Hermani¹,

Heß

Servi³

et al. 2005

Clinical Cancer Research

224

158

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Purpose: S100 proteins comprise a family of calcium-modulated proteins that have recently been associated with epithelial tumors. We examined the expression of two members of this family, S100A8 and S100A9, together with the S100 receptor RAGE (receptor for advanced glycation end products) in human prostate adenocarcinomas and in prostatic intraepithelial neoplasia. Experimental Design:Tissue specimens of 75 patients with organ-confined prostate cancer of different grades were analyzed by immunohistochemistry for expression of S100A8, S100A9, and RAGE. In addition, in situ hybridization of S100A8 and S100A9 was done for 20 cases. An ELISA was applied to determine serum concentrations of S100A9 in cancer patients compared with healthy controls or to patients with benign prostatic hyperplasia (BPH). Results: S100A8, S100A9, and RAGE were up-regulated in prostatic intraepithelial neoplasia and preferentially in high-grade adenocarcinomas, whereas benign tissue was negative or showed weak expression of the proteins. There was a high degree of overlap of S100A8 and S100A9 expression patterns and of S100A8 or S100A9 and RAGE, respectively. Frequently, a gradient within the tumor tissue with an increased expression toward the invaded stroma of the prostate was observed. S100A9 serum levels were significantly elevated in cancer patients compared with BPH patients or healthy individuals. Conclusion: Our data suggest that enhanced expression of S100A8, S100A9, and RAGE is an early event in prostate tumorigenesis and may contribute to development and progression or extension of prostate carcinomas. Furthermore, S100A9 in serum may serve as useful marker to discriminate between prostate cancer and BPH.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Calcium-Binding Proteins S100A8 and S100A9 as Novel Diagnostic Markers in Human Prostate Cancer

Hermani¹,

Heß

Servi³

et al. 2005

Clinical Cancer Research

224

158

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“…It has been found in renal tissue from SLE patients with glomerulonephritis, especially with proliferative lesions, and in the epidermis where it is produced by keratinocytes lesions. 4,44,115 Skin stressors, including UV exposure, 116 lead to an inflammatory response, which is usually part of the physiological mechanism of wound healing, but might also be responsible for autoimmune disregulation in skin lesions. 21 Patients with SLE have higher serum CLP levels compared with healthy individuals and also SS patients.…”

Section: Systemic Lupus Erythematosusmentioning

confidence: 99%

Calprotectin in rheumatic diseases

Ometto

Friso

Astorri

et al. 2016

Exp Biol Med (Maywood)

136

105

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Calprotectin is an acute-phase protein produced by monocytes and neutrophils in the circulation and inflamed tissues. Calprotectin seems to be more sensitive than CRP, being able to detect minimal residual inflammation and is a candidate biomarker in inflammatory diseases. High serum levels are associated with some severe manifestations of rheumatic diseases, such as glomerulonephritis and lung fibrosis. Calprotectin levels in other fluids, such as saliva and synovial fluid, might be helpful in the diagnosis of rheumatic diseases. Of interest is also the potential role of calprotectin as a target of treatment. AbstractCalprotectin is a heterodimer formed by two proteins, S100A8 and S100A9, which are mainly produced by activated monocytes and neutrophils in the circulation and in inflamed tissues. The implication of calprotectin in the inflammatory process has already been demonstrated, but its role in the pathogenesis, diagnosis, and monitoring of rheumatic diseases has gained great attention in recent years. Calprotectin, being stable at room temperature, is a candidate biomarker for the follow-up of disease activity in many autoimmune disorders, where it can predict response to treatment or disease relapse. There is evidence that a number of immunomodulators, including TNF-a inhibitors, may reduce calprotectin expression. S100A8 and S100A9 have a potential role as a target of treatment in murine models of autoimmune disorders, since the direct or indirect blockade of these proteins results in amelioration of the disease process. In this review, we will go over the biologic functions of calprotectin which might be involved in the etiology of rheumatic disorders. We will also report evidence of its potential use as a disease biomarker.

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“…Calprotectin, a protein complex composed of two calcium-binding proteins, S100A8 and S100A9, is constitutively expressed by cells of the innate immune system. Calprotectin represents 45% of neutrophil cytosolic protein weight [6] and is induced in epithelial cells in association with stress conditions [7]. Calprotectin is found in high concentrations in body fluids such as saliva and serum.…”

Section: Introductionmentioning

confidence: 99%

Oxidation of methionine 63 and 83 regulates the effect of S100A9 on the migration of neutrophils in vitro

Sroussi

Berline

Palefsky

2006

Journal of Leukocyte Biology

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The calcium-binding proteins S100A8 and S100A9 and their heterocomplex calprotectin are abundant cytosolic constituents in human neutrophils, constitutively expressed by mucosal epithelium and in association with inflammation by epidermal keratinocytes. S100A8 and S100A9 are pleiotropic proteins, which partake in the regulation of leukocyte migration. This study was designed to investigate the effect of S100A9 on neutrophil migration and to explore the mechanisms that regulate this effect. Based on previous results with S100A8, we hypothesized that S100A9 repels neutrophils and that oxidation of S100A9 regulates this function. Using standard Transwell chemotaxis assays and site-directed mutagenesis, we show that S100A9 exerts a chemo-repulsive (fugetactic) effect on peripheral neutrophils, an effect abolished by oxidation of S100A9. After substitution of methionine 63 and 83 for alanine, S100A9 maintained its fugetaxis activity, even in inhibitory, oxidative conditions. Together, the data suggest that S100A9 serves as a molecular switch for oxidative control of inflammation regulated by the oxidation of species-conserved methionine residues. In healthy mucosal tissue, expression of S100A9 by the epithelium may serve to inhibit leukocyte recruitment. However, conditions of oxidative stress, including infection and overgrowth of opportunistic pathogens, may abrogate this activity by neutralizing S100A9 as a result of its oxidative alteration. J. Leukoc. Biol. 81: 818 -824; 2007.

show abstract

Epidermal and dermal distribution of a myelomonocytic antigen (L1) shared by epithelial cells in various inflammatory skin diseases

Cited by 73 publications

References 10 publications

Calcium-Binding Proteins S100A8 and S100A9 as Novel Diagnostic Markers in Human Prostate Cancer

Calcium-Binding Proteins S100A8 and S100A9 as Novel Diagnostic Markers in Human Prostate Cancer

Calprotectin in rheumatic diseases

Oxidation of methionine 63 and 83 regulates the effect of S100A9 on the migration of neutrophils in vitro

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