Moonlighting Activity of Secreted Inflammation- Regulatory Proteins
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Moonlighting proteins exhibit multiple activities in different cellular compartments, and their abnormal regulation could play animportant role in many diseases. To date, many proteins have been identified with moonlighting activity, and more such proteinsare being gradually identified. Among the proteins that possess moonlighting activity, several secreted proteins exhibit multipleactivities in different cellular locations, such as the extracellular matrix, nucleus, and cytoplasm. While acute inflammation startsrapidly and generally disappears in a few days, chronic inflammation can last for months or years. This is generally because of thefailure to eliminate the cause of inflammation, along with repeated exposure to the inflammatory agent. Chronic inflammation isnow considered as an overwhelming burden to the general wellbeing of patients and noted as an underlying cause of several diseases. Moonlighting proteins can contribute to the process of chronic inflammation; therefore, it is imperative to overview someproteins that exhibit multiple functions in inflammatory diseases. In this review, we will focus on inflammation, particularly unravellingseveral well-known secreted proteins with multiple functions in different cellular locations.
Abstract
Moonlighting proteins exhibit multiple activities in different cellular compartments, and their abnormal regulation could play animportant role in many diseases. To date, many proteins have been identified with moonlighting activity, and more such proteinsare being gradually identified. Among the proteins that possess moonlighting activity, several secreted proteins exhibit multipleactivities in different cellular locations, such as the extracellular matrix, nucleus, and cytoplasm. While acute inflammation startsrapidly and generally disappears in a few days, chronic inflammation can last for months or years. This is generally because of thefailure to eliminate the cause of inflammation, along with repeated exposure to the inflammatory agent. Chronic inflammation isnow considered as an overwhelming burden to the general wellbeing of patients and noted as an underlying cause of several diseases. Moonlighting proteins can contribute to the process of chronic inflammation; therefore, it is imperative to overview someproteins that exhibit multiple functions in inflammatory diseases. In this review, we will focus on inflammation, particularly unravellingseveral well-known secreted proteins with multiple functions in different cellular locations.
참고문헌 (56)
- Smith LM, "Proteoform: a single term describing protein complexity", Nat Methods, 10, pp.186~187 (2013)[DOI]
- Munoz J, "From the human genome to the human proteome", Angew Chem Int Ed Engl, 53, pp.10864~10866 (2014)[DOI]
- Jeffery CJ, "Moonlighting proteins--an update", Mol Biosyst, 5, pp.345~350 (2009)[DOI]
- Copley SD, "Moonlighting is mainstream: paradigm adjustment required", Bioessays, 34, pp.578~588 (2012)[DOI]
- Henderson B, "Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease", Infect Immun, 79, pp.3476~3491 (2011)[DOI]
- Kainulainen V, "Dancing to another tune-adhesive moonlighting proteins in bacteria", Biology (Basel), 3, pp.178~204 (2014)
- Min KW, "Moonlighting proteins in cancer", Cancer Lett, 370, pp.108~116 (2016)[DOI]
- Shacter E, "Chronic inflammation and cancer", Oncology (Williston Park), 16, pp.217~226 (2002)
- Akiyama H, "Inflammation and Alzheimer's disease", Neurobiol Aging, 21, pp.383~421 (2000)[DOI]
- Kuzan A, "Thymosin <TEX>${\beta}$<", TEX> as an actin-binding protein with a variety of functions, 2016, pp.25, 1331~1336
- Jain AK, "Selective nonsteroidal anti-inflammatory drugs induce thymosin beta-4 and alter actin cytoskeletal organization in human colorectal cancer cells", J Pharmacol Exp Ther, 311, pp.885~891 (2004)[DOI]
- Lee SI, "Thymosin beta-4 suppresses osteoclastic differentiation and inflammatory responses in human periodontal ligament cells", PLoS One, 11, pp.e0146708~ (2016)[DOI]
- Conte E, "Protective effects of thymosin <TEX>${\beta}4$<", TEX> in a mouse model of lung fibrosis, 2012, pp.1269, 69~73
- Bao W, "Cardioprotection by systemic dosing of thymosin beta four following ischemic myocardial injury", Front Pharmacol, 4, pp.149~ (2013)
- Bock-Marquette I, "Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair", Nature, 432, pp.466~472 (2004)[DOI]
- Goldstein AL, "Advances in the basic and clinical applications of thymosin <TEX>${\beta}4$<", TEX>, 2015, pp.15(Suppl 1), S139~S145
- Piludu M, "Thymosin beta 4 may translocate from the cytoplasm in to the nucleus in HepG2 cells following serum starvation. An ultrastructural study", PLoS One, 10, pp.e0119642~ (2015)[DOI]
- Huff T, "Nuclear localisation of the G-actin sequestering peptide thymosin beta4", J Cell Sci, 117, pp.5333~5341 (2004)[DOI]
- Santra M, "Thymosin <TEX>${\beta}4$<", TEX> up-regulation of microRNA-146a promotes oligodendrocyte differentiation and suppression of the Toll-like proinflammatory pathway, 2014, pp.289, 19508~19518
- Shen XZ, "The peptide network regulated by angiotensin converting enzyme (ACE) in hematopoiesis", Cell Cycle, 10, pp.1363~1369 (2011)[DOI]
- Thomas E. Eling, "NSAID Activated Gene (NAG-1), a Modulator of Tumorigenesis", BMB reports, 39(6), pp.649~655 (2006), 한국생화학분자생물학회
- Chrysovergis K, "NAG-1", GDF-15 prevents obesity by increasing thermogenesis, lipolysis and oxidative metabolism, 2014, pp.38, 1555~1564
- Bootcov MR, "MIC-1, a novel macrophage inhibitory cytokine, is a divergent member of the TGF-beta superfamily", Proc Natl Acad Sci U S A, 94, pp.11514~11519 (1997)[DOI]
- Detmer K, "Lineage-restricted expression of bone morphogenetic protein genes in human hematopoietic cell lines", Blood Cells Mol Dis, 25, pp.310~323 (1999)[DOI]
- Baek SJ, "Cyclooxygenase inhibitors induce the expression of the tumor suppressor gene EGR-1, which results in the up-regulation of NAG-1, an antitumorigenic protein", Mol Pharmacol, 67, pp.356~364 (2005)
- Baek SJ, "Cyclooxygenase inhibitors regulate the expression of a TGF-beta superfamily member that has proapoptotic and antitumorigenic activities", Mol Pharmacol, 59, pp.901~908 (2001)[DOI]
- Baek SJ, "Resveratrol enhances the expression of non-steroidal anti-inflammatory drug-activated gene (NAG-1) by increasing the expression of p53", Carcinogenesis, 23, pp.425~434 (2002)[DOI]
- Li PX, "Placental transforming growth factor-beta is a downstream mediator of the growth arrest and apoptotic response of tumor cells to DNA damage and p53 overexpression", J Biol Chem, 275, pp.20127~20135 (2000)[DOI]
- Tan M, "PTGF-beta, a type beta transforming growth factor (TGF-beta) superfamily member, is a p53 target gene that inhibits tumor cell growth via TGF-beta signaling pathway", Proc Natl Acad Sci U S A, 97, pp.109~114 (2000)[DOI]
- Cekanova M, "Nonsteroidal anti-inflammatory drug-activated gene-1 expression inhibits urethane-induced pulmonary tumorigenesis in transgenic mice", Cancer Prev Res (Phila), 2, pp.450~458 (2009)[DOI]
- Kim JM, "NAG-1", GDF15 transgenic mouse has less white adipose tissue and a reduced inflammatory response, 2013, pp.2013, 641851~
- Min KW, "NAG-1", GDF15 accumulates in the nucleus and modulates transcriptional regulation of the Smad pathway, 2016, pp.35, 377~388
- Emmerson PJ, "The metabolic effects of GDF15 are mediated by the orphan receptor GFRAL", Nat Med, 23, pp.1215~1219 (2017)[DOI]
- Hsu JY, "Non-homeostatic body weight regulation through a brainstem-restricted receptor for GDF15", Nature, 550, pp.255~259 (2017)[DOI]
- Mullican SE, "GFRAL is the receptor for GDF15 and the ligand promotes weight loss in mice and nonhuman primates", Nat Med, 23, pp.1150~1157 (2017)[DOI]
- Yang L, "GFRAL is the receptor for GDF15 and is required for the anti-obesity effects of the ligand", Nat Med, 23, pp.1158~1166 (2017)[DOI]
- D'Cunha J, "Immunoregulatory properties of ISG15, an interferon-induced cytokine", Proc Natl Acad Sci U S A, 93, pp.211~215 (1996)[DOI]
- Speer SD, "ISG15 deficiency and increased viral resistance in humans but not mice", Nat Commun, 7, pp.11496~ (2016)[DOI]
- Dos Santos PF, "ISG15-induced IL-10 is a novel anti-inflammatory myeloid axis disrupted during active tuberculosis", J Immunol, 200, pp.1434~1442 (2018)[DOI]
- Jeon YJ, "ISG15 and immune diseases", Biochim Biophys Acta, 1802, pp.485~496 (2010)[DOI]
- Malakhova OA, "ISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral response", J Biol Chem, 283, pp.8783~8787 (2008)[DOI]
- Gonzalez-Sanz R, "ISG15 is upregulated in respiratory syncytial virus infection and reduces virus growth through protein ISGylation", J Virol, 90, pp.3428~3438 (2016)[DOI]
- Zhang X, "Human intracellular ISG15 prevents interferon-<TEX>${\alpha}", {\beta}$<, Nature, pp.2015, 517[DOI]
- Shapiro SD, "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages", J Biol Chem, 268, pp.23824~23829 (1993)
- Liu SL, "Matrix metalloproteinase-12 is an essential mediator of acute and chronic arterial stiffening", Sci Rep, 5, pp.17189~ (2015)[DOI]
- Molet S, "Increase in macrophage elastase (MMP-12) in lungs from patients with chronic obstructive pulmonary disease", Inflamm Res, 54, pp.31~36 (2005)[DOI]
- Niu H, "Matrix metalloproteinase 12 modulates high-fat-diet induced glomerular fibrogenesis and inflammation in a mouse model of obesity", Sci Rep, 6, pp.20171~ (2016)[DOI]
- Nenan S, "Macrophage elastase (MMP-12): a pro-inflammatory mediator", Mem Inst Oswaldo Cruz, 100(Suppl 1), pp.167~172 (2005)[DOI]
- Wang X, "Overexpression of human matrix metalloproteinase-12 enhances the development of inflammatory arthritis in transgenic rabbits", Am J Pathol, 165, pp.1375~1383 (2004)[DOI]
- Marchant DJ, "A new transcriptional role for matrix metalloproteinase- 12 in antiviral immunity", Nat Med, 20, pp.493~502 (2014)[DOI]
- Zittermann SI, "Basic fibroblast growth factor (bFGF, FGF-2) potentiates leukocyte recruitment to inflammation by enhancing endothelial adhesion molecule expression", Am J Pathol, 168, pp.835~846 (2006)[DOI]
- Kanazawa S, "VEGF, basic-FGF, and TGF-beta in Crohn's disease and ulcerative colitis: a novel mechanism of chronic intestinal inflammation", Am J Gastroenterol, 96, pp.822~828 (2001)
- Shao X, "FGF2 cooperates with IL-17 to promote autoimmune inflammation", Sci Rep, 7, pp.7024~ (2017)[DOI]
- Arese M, "Nuclear activities of basic fibroblast growth factor: potentiation of low-serum growth mediated by natural or chimeric nuclear localization signals", Mol Biol Cell, 10, pp.1429~1444 (1999)[DOI]
- Ader I, "The radioprotective effect of the 24 kDa FGF-2 isoform in HeLa cells is related to an increased expression and activity of the DNA dependent protein kinase (DNA-PK) catalytic subunit", Oncogene, 21, pp.6471~6479 (2002)[DOI]
- Li S, "Nuclear basic fibroblast growth factor regulates triple-negative breast cancer chemo-resistance", Breast Cancer Res, 17, pp.91~ (2015)[DOI]
