DOCSLIB.ORG

S100A7 (Psoriasin): a Story of Mice Tissue, Except That the Overall S100A7 Levels Are Markedly Increased

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
S100A7 (Psoriasin): a Story of Mice Tissue, Except That the Overall S100A7 Levels Are Markedly Increased View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector COMMENTARY See related article on page 1600 is observed during epidermal differ- entiation in vivo. This pattern of local- ization is recapitulated in psoriatic S100A7 (Psoriasin): a Story of Mice tissue, except that the overall S100A7 levels are markedly increased. These and Men properties appear to be biologically 1,2,3,4 1 important, as S100A7 and other S100 Richard L. Eckert and Kathleen C. Lee proteins are transglutaminase substrates S100 proteins are calcium-regulated proteins that regulate fundamental bio- and are incorporated as components of logical processes. S100A7 (psoriasin), functions as a transglutaminase substrate/ the keratinocyte cornified envelope. cornified envelope precursor, signal transduction protein, chemokine, and anti- Thus, movement to the cell periphery bacterial protein in normal epidermis. S100A7 is markedly increased in epider- would position S100A7 in a location to mal hyperproliferative disorders. The murine homolog of S100A7 and S10015 serve as a substrate of the membrane- has been identified, providing a valuable tool for studying the regulation and anchored cornified envelope assembly function of this protein in epidermis. enzyme type I transglutaminase. Journal of Investigative Dermatology (2006) 126, 1442–1444. doi:10.1038/sj.jid.5700265 In the intracellular compartment, S100A7 appears to interact with epi- dermal fatty acid-binding protein (E- FABP) (Hagens et al., 1999a; Ruse et The S100 proteins are a family of expressed in wound healing, inflam- al., 2003). Although E-FABP is involved more than 20 low-molecular weight matory and hyperproliferative skin in lipid metabolism and transport, the EF hand-containing calcium-regulated diseases, and skin cancer (Broome role of the intracellular S100A7–E- proteins that exist in cells as antiparal- et al., 2003; Madsen et al., 1992; FABP interaction in not known. It is lel homo- and heterodimers. Many of Madsen et al., 1991). S100A7 levels interesting that S100A7 is also found the genes encoding this family of pro- are increased in psoriasis, Darier’s dis- in the extracellular environment. It teins are clustered on chromosomal ease, atopic dermatitis, mycosis fun- is reported to be found in psoriatic location 1q21 in the epidermal dif- goides, inflammatory lichen sclerosus plaque exudate, as is its binding part- ferentiation complex (Ridinger et al., et atrophicus, and skin cancer. These ner E-FABP. In this context, S100A7 is 1998). S100 proteins have no known findings suggest an important role for intrinsic enzymatic activity; however, S100A7 in a variety of common skin The S100A15 sequence the S100 protein dimer undergoes a diseases (Eckert et al., 2004). conformational change upon calcium S100A7 has several documented will provide an binding. This conformation change roles in epidermis, including function- important new tool exposes protein domains designed to ing as a transglutaminase substrate/ to identify the role of permit S100A7 to interact with spe- cornified envelope precursor, signal cific target proteins, inducing them transduction protein, chemokine, and S100A7 and S100A15 to modulate target protein function antibacterial agent. The relative impor- in normal epidermal and serve as intracellular shuttle pro- tance of these various functions in the | development and in teins (Donato, 2001; Heizmann et context of different environmental al., 2002). Ultimately, activated S100 stimuli or after treatment with prophy- cutaneous diseases and proteins regulate fundamental cell lactic agents is an important area of cancer. processes, including cell proliferation, study. Immunohistological studies of differentiation, and apoptosis (Donato, cultured cells and human epidermis thought to have an antibacterial action 2001; Heizmann et al., 2002). Thirteen reveal that the S100A7 homodimer is (Glaser et al., 2005; Hagens et al., members of this protein family are distributed in the cytoplasm in non- 1999b). In addition, S100A7 may be expressed in various compartments differentiated keratinocytes but redis- released from cultured keratinocytes, in the epidermis (Eckert et al., 2004). tributes to the cell periphery when and it may act as a chemotactic agent S100A7 (psoriasin), S100A8 (MRP8), cultured keratinocytes are challenged (Jinquan et al., 1996), a function that and S100A9 (MRP14) are of particu- with a differentiation stimulus. A simi- has been reported for S100A7 in non- lar interest, as they are highly over- lar redistribution to the cell periphery epidermal tissues. It is important to note that the func- 1Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleve- tion of S100A7 may differ in normal land, Ohio, USA; 2Department of Biochemistry, Case Western Reserve University School of Medicine, versus stressed keratinocytes. The Cleveland, Ohio, USA; 3Department of Dermatology, Case Western Reserve University School of Medi- putative and identified functions of 4 cine, Cleveland, Ohio, USA; and Department of Oncology, Case Western Reserve University School of S100A7 in keratinocytes are shown Medicine, Cleveland, Ohio, USA schematically in Figure 1. In nor- Correspondence: Dr. Richard L. Eckert, Department of Physiology and Biophysics, Room E532, Case Western Reserve University School of Medicine, 2109 Adelbert Rd., Cleveland, Ohio 44106-4970, USA. mal cultured keratinocytes, S100A7 E-mail: [email protected] expression is increased by agents that 1442 Journal of Investigative Dermatology (2006), Volume 126 COMMENTARY a in the psoriatic environment? Second, what is the major role of S100A7 in normal keratinocyte differentiation, and does this role change in disease states? Addressing these questions will require extensive human studies as well as studies of the role of S100A7 in murine models. Previous studies have identified several human S100A7 b genes and a gene encoding human S100A15 (Wolf et al., 2003) — which is 95% identical to S100A7 — that are clustered on chromosome 1q21 (Eckert et al., 2004); however, the murine form of the gene had not been previ- ously reported. In this issue, Wolf et al. (2006) describe the isolation of a murine S100 gene that is assigned as the murine homolog to human S100A7 on the basis of the structure of the gene and its position in the genome. The phy- logenic tree suggests that murine S100A15 may be the ancestral gene for the human S100A7 and S100A15 genes. The isolation of this gene is the Figure 1. Regulation of expression and mechanism of S100A7 action in keratinocytes. (a) In normal first identification of a murine mem- keratinocytes, expression of S100A7 is increased by a mechanism that is dependent on protein kinase ber of the S100A7/S100A15 family of C (PKC) and activator protein-1 (AP1) transcription factors. (b) S100A7 exists as a dimer in cells and, in proteins. Wolf et al. (2006) show that response to increased intracellular calcium, forms a complex with two molecules of epidermal fatty acid- murine S100A15 is expressed in the binding protein (E-FABP). This complex (or components of the complex) is speculated to follow at least suprabasal murine epidermal layers. In four possible mechanistic paths: movement to the plasma membrane, where it serves as a transglutaminase addition, murine S100A15 is detected substrate and antibacterial entity; participation in regulation of lipid metabolism; functioning as a cytokine; and functioning as a released antibacterial complex. TG1, type I transglutaminase. as monomers and as high-molecular weight, apparently covalently cross- linked forms, in extracts of cultured human keratinocytes. The accumula- enhance keratinocyte differentiation E-FABP has been implicated as having tion of high-molecular weight forms (phorbol ester, calcium, etc.), a find- a role in lipid metabolism and intra- is increased when the cells are treated ing that is consistent with the presence cellular movement, and so S100A7 with agents (for example, calcium) of S100A7 in the suprabasal differenti- may play a role in shuttling E-FABP that promote keratinocyte differen- ated layers of epidermis (Figure 1a). to the proper subcellular location or tiation and activate type I transgluta- S100A7 is presumed to exist in the facilitating E-FABP activity. In stressed minase. It is striking that formation of cells as a homodimer. In response to keratinocytes, the role of these pro- high-molecular weight forms requires the differentiation stimulus-dependent teins may change. Active export or cell transglutaminase activity and is inhib- increase in intracellular calcium level, breakdown may facilitate the release ited by competitive transglutaminase S100A7 undergoes a conformational of S100A7 and E-FABP, allowing them inhibitors. In addition, these high- change that exposes protein motifs that to act as chemokines and/or antibac- molecular weight bands colocalize interact with E-FABP (Figure 1b). This terial agents. In this context, S100A7 on gels with anti-isopeptide bond interaction is associated with move- expression level may be controlled by immunoreactivity, suggesting that the ment of the S100A7–E-FABP complex agents such as interferon. S100A15 is covalently cross-linked to to the cell periphery, where S100A7 Because this model is speculative, other proteins via isopeptide bonds, and E-FABP are incorporated as corni- key questions regarding the role of the same linkages that are used in cor- fied envelope components. S100 pro-
Load more

Recommended publications
  • S100A7 Promotes the Migration and Invasion of Osteosarcoma Cells Via the Receptor for Advanced Glycation End Products
    ONCOLOGY LETTERS 3: 1149-1153, 2012 S100A7 promotes the migration and invasion of osteosarcoma cells via the receptor for advanced glycation end products KEN KATAOKA*, TOMOYUKI ONO*, HITOSHI MURATA, MIKA MORISHITA, KEN-ICHI YAMAMOTO, MASAKIYO SAKAGUCHI and NAM-HO HUH Department of Cell Biology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8558, Japan Received December 14, 2011; Accepted February 1, 2012 DOI: 10.3892/ol.2012.612 Abstract. Osteosarcoma is the most common malignant tumor significantly improved the 5-year survival rate of osteosarcoma of bone in childhood and adolescence. Despite intensive patients from 15 to 70% (2). However, 30-40% of patients still research for new therapies, the outcome in patients with metas- succumb to the disease, mainly due to distant metastasis to tasis remains extremely poor. S100 proteins are involved in the the lung (3). Despite intensive research for new therapies, the proliferation, cell cycle progression and metastasis of numerous outcome in patients with metastasis remains extremely poor. malignant tumors, including osteosarcoma. In the present study, The S100 protein family consists of 20 calcium-binding we identified S100A7 as a candidate to promote the migra- proteins with EF hand motifs (4). S100 proteins have been tion of osteosarcoma cells. S100A7 promoted the migration shown to have intracellular and extracellular roles in the regula- and invasion of osteosarcoma cells as assayed in vitro. An in tion of diverse processes, including protein phosphorylation, vitro pull-down assay revealed the binding of the recombinant cell growth and motility, cell-cycle regulation, transcription, S100A7 protein with its putative receptor, the receptor for differentiation and cell survival (5).
    [Show full text]
  • Inflammation-Mediated Skin Tumorigenesis Induced by Epidermal C-Fos
    Downloaded from genesdev.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Inflammation-mediated skin tumorigenesis induced by epidermal c-Fos Eva M. Briso,1 Juan Guinea-Viniegra,1 Latifa Bakiri,1 Zbigniew Rogon,2 Peter Petzelbauer,3 Roland Eils,2 Ronald Wolf,4 Mercedes Rinco´ n,5 Peter Angel,6 and Erwin F. Wagner1,7 1BBVA Foundation-Spanish National Cancer Research Center (CNIO) Cancer Cell Biology Program, CNIO, 28029 Madrid, Spain; 2Division of Theoretical Bioinformatics, German Cancer Research Center (DKFZ), 69120 Heidelberg, Germany; 3Skin and Endothelium Research Division (SERD), Department of Dermatology, Medical University of Vienna, A-1090 Vienna, Austria; 4Department of Dermatology and Allergology, Ludwig-Maximilian University, Munich, Germany; 5Division of Immunobiology, Department of Medicine, University of Vermont, 05405 Burlington, Vermont, USA; 6Division of Signal Transduction and Growth Control, DKFZ, DKFZ-Center for Molecular Biology of the University of Heidelberg (ZMBH) Alliance, 69120 Heidelberg, Germany Skin squamous cell carcinomas (SCCs) are the second most prevalent skin cancers. Chronic skin inflammation has been associated with the development of SCCs, but the contribution of skin inflammation to SCC development remains largely unknown. In this study, we demonstrate that inducible expression of c-fos in the epidermis of adult mice is sufficient to promote inflammation-mediated epidermal hyperplasia, leading to the development of preneoplastic lesions. Interestingly, c-Fos transcriptionally controls mmp10 and s100a7a15 expression in keratinocytes, subsequently leading to CD4 T-cell recruitment to the skin, thereby promoting epidermal hyperplasia that is likely induced by CD4 T-cell-derived IL-22. Combining inducible c-fos expression in the epidermis with a single dose of the carcinogen 7,12-dimethylbenz(a)anthracene (DMBA) leads to the development of highly invasive SCCs, which are prevented by using the anti-inflammatory drug sulindac.
    [Show full text]
  • Multifactorial Erβ and NOTCH1 Control of Squamous Differentiation and Cancer
    Multifactorial ERβ and NOTCH1 control of squamous differentiation and cancer Yang Sui Brooks, … , Karine Lefort, G. Paolo Dotto J Clin Invest. 2014;124(5):2260-2276. https://doi.org/10.1172/JCI72718. Research Article Oncology Downmodulation or loss-of-function mutations of the gene encoding NOTCH1 are associated with dysfunctional squamous cell differentiation and development of squamous cell carcinoma (SCC) in skin and internal organs. While NOTCH1 receptor activation has been well characterized, little is known about how NOTCH1 gene transcription is regulated. Using bioinformatics and functional screening approaches, we identified several regulators of the NOTCH1 gene in keratinocytes, with the transcription factors DLX5 and EGR3 and estrogen receptor β (ERβ) directly controlling its expression in differentiation. DLX5 and ERG3 are required for RNA polymerase II (PolII) recruitment to the NOTCH1 locus, while ERβ controls NOTCH1 transcription through RNA PolII pause release. Expression of several identified NOTCH1 regulators, including ERβ, is frequently compromised in skin, head and neck, and lung SCCs and SCC-derived cell lines. Furthermore, a keratinocyte ERβ–dependent program of gene expression is subverted in SCCs from various body sites, and there are consistent differences in mutation and gene-expression signatures of head and neck and lung SCCs in female versus male patients. Experimentally increased ERβ expression or treatment with ERβ agonists inhibited proliferation of SCC cells and promoted NOTCH1 expression and squamous differentiation both in vitro and in mouse xenotransplants. Our data identify a link between transcriptional control of NOTCH1 expression and the estrogen response in keratinocytes, with implications for differentiation therapy of squamous cancer. Find the latest version: https://jci.me/72718/pdf Research article Multifactorial ERβ and NOTCH1 control of squamous differentiation and cancer Yang Sui Brooks,1,2 Paola Ostano,3 Seung-Hee Jo,1,2 Jun Dai,1,2 Spiro Getsios,4 Piotr Dziunycz,5 Günther F.L.
    [Show full text]
  • 1 Supporting Information for a Microrna Network Regulates
    Supporting Information for A microRNA Network Regulates Expression and Biosynthesis of CFTR and CFTR-ΔF508 Shyam Ramachandrana,b, Philip H. Karpc, Peng Jiangc, Lynda S. Ostedgaardc, Amy E. Walza, John T. Fishere, Shaf Keshavjeeh, Kim A. Lennoxi, Ashley M. Jacobii, Scott D. Rosei, Mark A. Behlkei, Michael J. Welshb,c,d,g, Yi Xingb,c,f, Paul B. McCray Jr.a,b,c Author Affiliations: Department of Pediatricsa, Interdisciplinary Program in Geneticsb, Departments of Internal Medicinec, Molecular Physiology and Biophysicsd, Anatomy and Cell Biologye, Biomedical Engineeringf, Howard Hughes Medical Instituteg, Carver College of Medicine, University of Iowa, Iowa City, IA-52242 Division of Thoracic Surgeryh, Toronto General Hospital, University Health Network, University of Toronto, Toronto, Canada-M5G 2C4 Integrated DNA Technologiesi, Coralville, IA-52241 To whom correspondence should be addressed: Email: [email protected] (M.J.W.); yi- [email protected] (Y.X.); Email: [email protected] (P.B.M.) This PDF file includes: Materials and Methods References Fig. S1. miR-138 regulates SIN3A in a dose-dependent and site-specific manner. Fig. S2. miR-138 regulates endogenous SIN3A protein expression. Fig. S3. miR-138 regulates endogenous CFTR protein expression in Calu-3 cells. Fig. S4. miR-138 regulates endogenous CFTR protein expression in primary human airway epithelia. Fig. S5. miR-138 regulates CFTR expression in HeLa cells. Fig. S6. miR-138 regulates CFTR expression in HEK293T cells. Fig. S7. HeLa cells exhibit CFTR channel activity. Fig. S8. miR-138 improves CFTR processing. Fig. S9. miR-138 improves CFTR-ΔF508 processing. Fig. S10. SIN3A inhibition yields partial rescue of Cl- transport in CF epithelia.
    [Show full text]
  • (Rage) in Progression of Pancreatic Cancer
    The Texas Medical Center Library DigitalCommons@TMC The University of Texas MD Anderson Cancer Center UTHealth Graduate School of The University of Texas MD Anderson Cancer Biomedical Sciences Dissertations and Theses Center UTHealth Graduate School of (Open Access) Biomedical Sciences 8-2017 INVOLVEMENT OF THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN PROGRESSION OF PANCREATIC CANCER Nancy Azizian MS Follow this and additional works at: https://digitalcommons.library.tmc.edu/utgsbs_dissertations Part of the Biology Commons, and the Medicine and Health Sciences Commons Recommended Citation Azizian, Nancy MS, "INVOLVEMENT OF THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN PROGRESSION OF PANCREATIC CANCER" (2017). The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access). 748. https://digitalcommons.library.tmc.edu/utgsbs_dissertations/748 This Dissertation (PhD) is brought to you for free and open access by the The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at DigitalCommons@TMC. It has been accepted for inclusion in The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access) by an authorized administrator of DigitalCommons@TMC. For more information, please contact [email protected]. INVOLVEMENT OF THE RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS (RAGE) IN PROGRESSION OF PANCREATIC CANCER by Nancy
    [Show full text]
  • Comparative Genomics Search for Losses of Long-Established Genes on the Human Lineage
    Comparative Genomics Search for Losses of Long-Established Genes on the Human Lineage Jingchun Zhu1, J. Zachary Sanborn1, Mark Diekhans1, Craig B. Lowe1, Tom H. Pringle1, David Haussler1,2* 1 Center for Biomolecular Science and Engineering, University of California Santa Cruz, Santa Cruz, California, United States of America, 2 Howard Hughes Medical Institute, University of California Santa Cruz, Santa Cruz, California, United States of America Taking advantage of the complete genome sequences of several mammals, we developed a novel method to detect losses of well-established genes in the human genome through syntenic mapping of gene structures between the human, mouse, and dog genomes. Unlike most previous genomic methods for pseudogene identification, this analysis is able to differentiate losses of well-established genes from pseudogenes formed shortly after segmental duplication or generated via retrotransposition. Therefore, it enables us to find genes that were inactivated long after their birth, which were likely to have evolved nonredundant biological functions before being inactivated. The method was used to look for gene losses along the human lineage during the approximately 75 million years (My) since the common ancestor of primates and rodents (the euarchontoglire crown group). We identified 26 losses of well-established genes in the human genome that were all lost at least 50 My after their birth. Many of them were previously characterized pseudogenes in the human genome, such as GULO and UOX. Our methodology is highly effective at identifying losses of single-copy genes of ancient origin, allowing us to find a few well-known pseudogenes in the human genome missed by previous high-throughput genome-wide studies.
    [Show full text]
  • Structural Characterization of S100A15 Reveals a Novel Zinc Coordination
    Murray et al. BMC Structural Biology 2012, 12:16 http://www.biomedcentral.com/1472-6807/12/16 RESEARCH ARTICLE Open Access Structural characterization of S100A15 reveals a novel zinc coordination site among S100 proteins and altered surface chemistry with functional implications for receptor binding Jill I Murray1,2, Michelle L Tonkin2, Amanda L Whiting1, Fangni Peng2, Benjamin Farnell1,2, Jay T Cullen3, Fraser Hof1 and Martin J Boulanger2* Abstract Background: S100 proteins are a family of small, EF-hand containing calcium-binding signaling proteins that are implicated in many cancers. While the majority of human S100 proteins share 25-65% sequence similarity, S100A7 and its recently identified paralog, S100A15, display 93% sequence identity. Intriguingly, however, S100A7 and S100A15 serve distinct roles in inflammatory skin disease; S100A7 signals through the receptor for advanced glycation products (RAGE) in a zinc-dependent manner, while S100A15 signals through a yet unidentified G-protein coupled receptor in a zinc-independent manner. Of the seven divergent residues that differentiate S100A7 and S100A15, four cluster in a zinc-binding region and the remaining three localize to a predicted receptor-binding surface. Results: To investigate the structural and functional consequences of these divergent clusters, we report the X-ray crystal structures of S100A15 and S100A7D24G, a hybrid variant where the zinc ligand Asp24 of S100A7 has been substituted with the glycine of S100A15, to 1.7 Å and 1.6 Å resolution, respectively. Remarkably, despite replacement of the Asp ligand, zinc binding is retained at the S100A15 dimer interface with distorted tetrahedral geometry and a chloride ion serving as an exogenous fourth ligand.
    [Show full text]
  • PDF Download
    S100A7 Polyclona Antibody Catalog No : YT6273 Reactivity : Human,Rat,Mouse, Applications : IHC, ELISA Gene Name : S100A7 PSOR1 S100A7C Protein Name : S100A7 Human Gene Id : 6278 Human Swiss Prot P31151 No : Immunogen : Synthesized peptide derived from human S100A7 Specificity : This antibody detects endogenous levels of human S100A7 Formulation : Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. Source : Rabbit Dilution : IHC-p 1:50-200, ELISA(peptide)1:5000-20000 Purification : The antibody was affinity-purified from mouse ascites by affinity- chromatography using specific immunogen. Concentration : 1 mg/ml Storage Stability : -20°C/1 year Background : S100 calcium binding protein A7(S100A7) Homo sapiens The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus. The protein is 1 / 2 overexpressed in hyperproliferative skin diseases, exhibits antimicrobial activities against bacteria and induces immunomodulatory activities. [provided by RefSeq, Nov 2014], Function : mass spectrometry: PubMed:8526920,similarity:Belongs to the S-101 family.,similarity:Contains 2 EF-hand domains.,subcellular location:Secreted by a non-classical secretory pathway.,subunit:Interacts with RANBP9.,tissue specificity:Fetal ear, skin, and tongue and human cell lines.
    [Show full text]
  • Probing the S100 Protein Family Through Genomic and Functional Analysis$
    Genomics 84 (2004) 10–22 www.elsevier.com/locate/ygeno Probing the S100 protein family through genomic and functional analysis$ Timothy Ravasi,a,b,* Kenneth Hsu,c Jesse Goyette,c Kate Schroder,a Zheng Yang,c Farid Rahimi,c Les P. Miranda,b,1 Paul F. Alewood,b David A. Hume,a,b and Carolyn Geczyc a SRC for Functional and Applied Genomics, CRC for Chronic Inflammatory Diseases, University of Queensland, Brisbane 4072, QLD, Australia b Institute for Molecular Bioscience, University of Queensland, Brisbane 4072, QLD, Australia c Cytokine Research Unit, School of Medical Sciences, University of New South Wales, Sydney 2052, NSW, Australia Received 25 November 2003; accepted 2 February 2004 Available online 10 May 2004 Abstract The EF-hand superfamily of calcium binding proteins includes the S100, calcium binding protein, and troponin subfamilies. This study represents a genome, structure, and expression analysis of the S100 protein family, in mouse, human, and rat. We confirm the high level of conservation between mammalian sequences but show that four members, including S100A12, are present only in the human genome. We describe three new members of the S100 family in the three species and their locations within the S100 genomic clusters and propose a revised nomenclature and phylogenetic relationship between members of the EF-hand superfamily. Two of the three new genes were induced in bone-marrow-derived macrophages activated with bacterial lipopolysaccharide, suggesting a role in inflammation. Normal human and murine tissue distribution profiles indicate that some members of the family are expressed in a specific manner, whereas others are more ubiquitous.
    [Show full text]
  • Nori Human S100A7 ELISA Kit-Datasheet 1. Madsen P, Et
    Nori Human S100A7 ELISA Kit-DataSheet S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.[1] S100A7 is a member of the S100 family of proteins containing 2 EF- hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus. The protein functions as a prominent antimicrobial peptide mainly against E. coli. S100A7 also displays antimicrobial properties. It is secreted by epithelial cells of the skin and is a key antimicrobial protein against Escherichia coli by disrupting their cell membranes. S100A7 is highly homologous to S100A15 but distinct in expression, tissue distribution and function.[2][3] S100A7 is markedly over-expressed in the skin lesions of psoriatic patients, but is excluded as a candidate gene for familial psoriasis susceptibility. The expression of psoriasin is induced in skin wounds[4] through activation of the epidermal growth factor receptor. S100A7 has been shown to interact with COP9 constitutive photomorphogenic homolog subunit 5,[5] FABP5[2][3] and RANBP9.[8] S100A7 interacts with RAGE (receptor of advanced glycated end products).[2][9] References 1. Madsen P, et al. (1991). J. Invest. Dermatol. 97 (4): 701–12. 2. Wolf R, et al. (2008) J. Immunol. 181 (2): 1499–506.
    [Show full text]
  • S100A7 Antibody Cat
    S100A7 Antibody Cat. No.: 18-401 S100A7 Antibody Immunohistochemistry of paraffin-embedded human Immunohistochemistry of paraffin-embedded mouse lung esophagus using S100A7 antibody (18-401) at dilution of using S100A7 antibody (18-401) at dilution of 1:100 (40x 1:100 (40x lens). lens). Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat Recombinant fusion protein containing a sequence corresponding to amino acids 1-101 of IMMUNOGEN: human S100A7 (NP_002954.2). TESTED APPLICATIONS: IHC APPLICATIONS: IHC: ,1:50 - 1:200 Properties September 28, 2021 1 https://www.prosci-inc.com/s100a7-antibody-18-401.html PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: S100A7 S100A7, S100 calcium binding protein A7 (psoriasin 1), HGNC:10497, PSOR1, S100A7c, ALTERNATE NAMES: S100 calcium-binding protein A7, S100 calcium-binding protein A7 (psoriasin 1), psoriasin 1, Psoriasin, S100A7C GENE ID: 6278 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least BACKGROUND: 13 members which are located as a cluster on chromosome 1q21. This protein differs from the other S100 proteins of known structure in its lack of calcium binding ability in one EF-hand at the N-terminus.
    [Show full text]
  • Reduced Expression of Ranbpm Is Associated with Poorer Survival
    ANTICANCER RESEARCH 37 : 4389-4397 (2017) doi:10.21873/anticanres.11833 Reduced Expression of RanBPM Is Associated with Poorer Survival from Lung Cancer and Increased Proliferation and Invasion of Lung Cancer Cells In Vitro ZEHANG ZHAO 1,2 , SHAN CHENG 1, CATHERINE ZABKIEWICZ 2, JINFENG CHEN 3, LIJIANG ZHANG 3, LIN YE 2 and WEN G. JIANG 1,2 1Cardiff University-Capital Medical University Joint Centre for Biomedical Research & Cancer Institute, Capital Medical University, Beijing, P.R. China; 2Cardiff China Medical Research Collaborative, Cardiff University School of Medicine, Cardiff, U.K.; 3Key Laboratory of Carcinogenesis and Translational Research, Ministry of Education, Department of Thoracic Surgery II, Beijing Cancer Hospital & Institute, Peking University School of Oncology, Beijing, P.R. China Abstract. Background/Aim: Ran binding protein particularly activation of growth-promoting pathways and microtubule-organizing centre (RanBPM), also known as inhibition of tumor-suppressor pathways (3-6). It is critical RanBP9, is a scaffold protein conserved through evolution. to have a better understanding of the genetic and molecular We investigated the role of RanBPM in human lung cancer. machinery involved in the tumorigenesis and disease Materials and Methods: Transcripts of RanBPM were progression of lung cancer for future targeted therapy (7-9). determined in 56 human lung cancers along with paired Unfortunately, little progress has been made in the treatment normal lung tissues using real-time PCR. Association with of advanced or metastatic lung cancer due to remaining gaps prognosis was analyzed by online Kaplan –Meier survival in the knowledge of the mechanisms of the disease (10-12). analysis. In vitro lung cancer cell functional assays Therefore, there has been great interest in the identification examined the impact of RanBPM-knockdown on cellular of novel molecular targets or biomarkers to facilitate early growth and invasion.
    [Show full text]