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Sender's message: Sepsis or genomics or altitude: JKB_daily1

Sent on Saturday, 2014 October 11
Search: (sepsis[MeSH Terms] OR septic shock[MeSH Terms] OR altitude[MeSH Terms] OR genomics[MeSH Terms] OR genetics[MeSH Terms] OR retrotransposons[MeSH Terms] OR macrophage[MeSH Terms]) AND ("2009/8/8"[Publication Date] : "3000"[Publication Date]) AND (("Science"[Journal] OR "Nature"[Journal] OR "The New England journal of medicine"[Journal] OR "Lancet"[Journal] OR "Nature genetics"[Journal] OR "Nature medicine"[Journal]) OR (Hume DA[Author] OR Baillie JK[Author] OR Faulkner, Geoffrey J[Author]))

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PubMed Results

Items 1 - 3 of 3

1.	Nat Med. 2014 Aug;20(8):857-69. doi: 10.1038/nm.3653. Preparing the ground for tissue regeneration: from mechanism to therapy. Forbes SJ1, Rosenthal N2. Author information: 1MRC Centre for Regenerative Medicine, University of Edinburgh, Edinburgh, UK. 21] National Heart and Lung Institute, Imperial College London, London, UK. [2] Australian Regenerative Medicine Institute, Monash University, Melbourne, Victoria, Australia. Abstract Chronic diseases confer tissue and organ damage that reduce quality of life and are largely refractory to therapy. Although stem cells hold promise for treating degenerative diseases by 'seeding' injured tissues, the regenerative capacity of stem cells is influenced by regulatory networks orchestrated by local immune responses to tissue damage, with macrophages being a central component of the injury response and coordinator of tissue repair. Recent research has turned to how cellular and signaling components of the local stromal microenvironment (the 'soil' to the stem cells' seed), such as local inflammatory reactions, contribute to successful tissue regeneration. This Review discusses the basic principles of tissue regeneration and the central role locally acting components may play in the process. Application of seed-and-soil concepts to regenerative medicine strengthens prospects for developing cell-based therapies or for promotion of endogenous repair.
	PMID: 25100531 [PubMed - indexed for MEDLINE]
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2.	Nat Med. 2014 Aug;20(8):936-41. doi: 10.1038/nm.3626. Epub 2014 Jul 20. The ribonuclease activity of SAMHD1 is required for HIV-1 restriction. Ryoo J1, Choi J2, Oh C1, Kim S2, Seo M 2, Kim SY2, Seo D3, Kim J4, White TE5, Brandariz-Nuñez A5, Diaz-Griffero F5, Yun CH6, Hollenbaugh JA7, Kim B8, Baek D9, Ahn K2. Author information: 11] Creative Research Initiative Center for Antigen Presentation, Seoul National University, Seoul, Republic of Korea. [2] Department of the Interdisciplinary Program in Genetic Engineering, Seoul National University, Seoul, Republic of Korea. 21] Creative Research Initiative Center for Antigen Presentation, Seoul National University, Seoul, Republic of Korea. [2] Department of Biological Sciences, Seoul National University, Seoul, Republic of Korea. 3Department of Biological Sciences, Seoul National University, Seoul, Republic of Korea. 41] Department of Biological Sciences, Seoul National University, Seoul, Republic of Korea. [2] Center for RNA Research, Institute for Basic Science, Seoul, Republic of Korea. 5Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, USA. 6Department of Agricultural Biotechnology, Seoul National University, Seoul, Republic of Korea. 7Center for Drug Discovery, Department of Pediatrics, Emory School of Medicine, Atlanta, Georgia, USA. 81] Center for Drug Discovery, Department of Pediatrics, Emory School of Medicine, Atlanta, Georgia, USA. [2] School of Pharmacy, Kyung Hee University, Seoul, Republic of Korea. 91] Department of Biological Sciences, Seoul National University, Seoul, Republic of Korea. [2] Center for RNA Research, Institute for Basic Science, Seoul, Republic of Korea. [3] Bioinformatics Institute, Seoul National University, Seoul, Republic of Korea. Comment in A new activity for SAMHD1 in HIV restriction. [Nat Med. 2014] A new activity for SAMHD1 in HIV restriction.Yang Z, Greene WC. Nat Med. 2014 Aug; 20(8):808-9. Abstract The HIV-1 restriction factor SAM domain- and HD domain-containing protein 1 (SAMHD1) is proposed to inhibit HIV-1 replication by depleting the intracellular dNTP pool. However, phosphorylation of SAMHD1 regulates its ability to restrict HIV-1 without decreasing cellular dNTP levels, which is not consistent with a role for SAMHD1 dNTPase activity in HIV-1 restriction. Here, we show that SAMHD1 possesses RNase activity and that the RNase but not the dNTPase function is essential for HIV-1 restriction. By enzymatically characterizing Aicardi-Goutières syndrome (AGS)-associated SAMHD1 mutations and mutations in the allosteric dGTP-binding site of SAMHD1 for defects in RNase or dNTPase activity, we identify SAMHD1 point mutants that cause loss of one or both functions. The RNase-positive and dNTPase-negative SAMHD1D137N mutant is able to restrict HIV-1 infection, whereas the RNase-negative and dNTPase-positive SAMHD1Q548A mutant is defective for HIV-1 restriction. SAMHD1 associates with HIV-1 RNA and degrades it during the early phases of cell infection. SAMHD1 silencing in macrophages and CD4(+) T cells from healthy donors increases HIV-1 RNA stability, rendering the cells permissive for HIV-1 infection. Furthermore, phosphorylation of SAMHD1 at T592 negatively regulates its RNase activity in cells and impedes HIV-1 restriction. Our results reveal that the RNase activity of SAMHD1 is responsible for preventing HIV-1 infection by directly degrading the HIV-1 RNA.
	PMID: 25038827 [PubMed - indexed for MEDLINE]
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3.	Nat Med. 2014 Aug;20(8):942-7. doi: 10.1038/nm.3614. Epub 2014 Jul 6. A Gpr120-selective agonist improves insulin resistance and chronic inflammation in obese mice. Oh da Y1, Walenta E1, Akiyama TE2, Lagakos WS1, Lackey D1, Pessentheiner AR3, Sasik R1, Hah N4, Chi TJ1, Cox JM2, Powels MA2, Di Salvo J2, Sinz C2, Watkins SM5, Armando AM6, Chung H1, Evans RM7, Quehenberger O8, McNelis J1, Bogner-Strauss JG9, Olefsky JM1. Author information: 1Division of Endocrinology and Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. 2Merck Research Laboratories, Kenilworth, New Jersey, USA. 31] Division of Endocrinology and Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. [2] Institute of Biochemistry, Graz University of Technology, Graz, Austria. 4Gene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, California, USA. 5Lipomics Technologies, West Sacramento, California, USA. 6Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 71] Gene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, California, USA. [2] Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, California, USA. 81] Division of Endocrinology and Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. [2] Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 9Institute of Biochemistry, Graz University of Technology, Graz, Austria. Comment in Diabetes: Gpr120 agonist has anti-inflammatory and insulin-sensitizing effects. [Nat Rev Endocrinol. 2014] Diabetes: Gpr120 agonist has anti-inflammatory and insulin-sensitizing effects.Greenhill C. Nat Rev Endocrinol. 2014 Sep; 10(9):510. Epub 2014 Jul 22. Abstract It is well known that the ω-3 fatty acids (ω-3-FAs; also known as n-3 fatty acids) can exert potent anti-inflammatory effects. Commonly consumed as fish products, dietary supplements and pharmaceuticals, ω-3-FAs have a number of health benefits ascribed to them, including reduced plasma triglyceride levels, amelioration of atherosclerosis and increased insulin sensitivity. We reported that Gpr120 is the functional receptor for these fatty acids and that ω-3-FAs produce robust anti-inflammatory, insulin-sensitizing effects, both in vivo and in vitro, in a Gpr120-dependent manner. Indeed, genetic variants that predispose to obesity and diabetes have been described in the gene encoding GPR120 in humans (FFAR4). However, the amount of fish oils that would have to be consumed to sustain chronic agonism of Gpr120 is too high to be practical, and, thus, a high-affinity small-molecule Gpr120 agonist would be of potential clinical benefit. Accordingly, Gpr120 is a widely studied drug discovery target within the pharmaceutical industry. Gpr40 is another lipid-sensing G protein-coupled receptor, and it has been difficult to identify compounds with a high degree of selectivity for Gpr120 over Gpr40 (ref. 11). Here we report that a selective high-affinity, orally available, small-molecule Gpr120 agonist (cpdA) exerts potent anti-inflammatory effects on macrophages in vitro and in obese mice in vivo. Gpr120 agonist treatment of high-fat diet-fed obese mice causes improved glucose tolerance, decreased hyperinsulinemia, increased insulin sensitivity and decreased hepatic steatosis. This suggests that Gpr120 agonists could become new insulin-sensitizing drugs for the treatment of type 2 diabetes and other human insulin-resistant states in the future. PMCID: PMC4126875 [Available on 2015/2/1]
	PMID: 24997608 [PubMed - indexed for MEDLINE]
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