L adhesion molecule 1 (Glycam1), mRNA [NM_008134] Mus musculus 0 day neonate thymus cDNA, RIKEN full-length enriched library, clone: A430085B12 solution: unclassifiable, complete insert sequence. [AK040303] Mus musculus oxidized low-density lipoprotein (lectin-like) receptor 1 (Olr1), mRNA [NM_138648] Mus musculus collagen triple helix repeat containing 1 (Cthrc1), mRNA [NM_026778] Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone: 1700018G05 solution: unclassifiable, full insert sequence. [AK006087] RIKEN cDNA 4932438A13 gene [Source: MGI Symbol; Acc: MGI: 2444631] [ENSMUST00000148698] Mus musculus cell adhesion molecule with homology to L1CAM (Chl1), mRNA [NM_007697] Mus musculus CD72 antigen (Cd72), transcript variant 2, mRNA [NM_007654] Mus musculus secreted Ly6/Plaur domain containing 1 (Slurp1), mRNA [NM_020519] Mus musculus 13 days embryo forelimb cDNA, RIKEN full-length enriched library, clone: 5930400C17 solution: unclassifiable, complete insert sequence. [AK031058] Mus musculus tetratricopeptide repeat domain 25 (Ttc25), mRNA [NM_028918] Mus musculus plakophilin 1 (Pkp1), mRNA [NM_019645] Mus musculus 3 days neonate thymus cDNA, RIKEN full-length enriched library, clone: A630081D01 solution: unclassifiable, complete insert sequence. [AK042310]Gene symbol 9930013L23Rik 9930013L23RikUniGenelD Mm.160389 Mm.Fold change (NET-A vs. placebo) eight.04 5.P-value 0.001 0.Glycam1 B930042K01RikMm.219621 Mm.three.85 three.0.020 0.Olr1 Cthrc1 1700018G05RikMm.DYRK2 MedChemExpress 293626 Mm.41556 Mm.three.69 three.69 3.0.009 0.042 0.4932438A13Rik Chl1 Cd72 SlurpMm.207907 Mm.251288 Mm.Cereblon medchemexpress 188157 Mm.3.14 3.12 three.11 3.09 2.0.030 0.025 0.024 0.002 0.Ttc25 Pkp1 A630081D01RikMm.31590 Mm.4494 Mm.two.87 two.80 two.0.048 0.011 0.A single gene was not attributed using a gene symbol (marked in light grey) nor did it obtain a UniGeneID (marked in mid-grey).same extent. MMPs are identified to be involved in proteolytic degradation of extracellular matrix and MMP-9 levels are improved in unstable atherosclerotic plaques (Sigala et al., 2010). Additionally, overexpression of activated MMP-9 in macrophages was shown to boost the incidence of plaque rupture in ApoE-deficient mice (Gough et al., 2006). For that reason, the larger expression of Mmp9 could result in enhanced degradation of extracellular matrix and destabilization with the fibrous cap of atherosclerotic plaques. A limitation of this conclusion is that spontaneous plaque rupture, as seen in humans, will not take place in mice. However, the up-regulation of Mmp9 may possibly nevertheless imply improved destabilization of atherosclerotic plaques in general. Moreover, S100a9 was up-regulated in each progestin therapy groups. It is5042 British Journal of Pharmacology (2014) 171 5032?recognized that S100A8/A9 type heterodimers (Kerkhoff et al., 1999) and S100A8 and S100A9 proteins have been detected in plaque-derived material (McCormick et al., 2005). Offered this observation and their potential to enhance macrophage LDL uptake (Lau et al., 1995) and to market monocyteinfiltration at sites of inflammation (Eue et al., 2000) these proteins could possibly also be involved in regulation of atherothrombosis. Especially, the heterodimeric type of S100A8/A9 may well be involved in thrombosis for the reason that expression of each genes was induced by more than sixfold in thrombosis-prone mice substituted with MPA, even though in NET-A-treated animals only S100a9 was up-regulated. Expression of Ppbp was elevated in MPA- and NET-A-treated animals. Morrell described that pro-platelet basic protein (Ppbp) as well.
