ライフサイエンスコーパス: MCP-2

1 ficantly higher IL-10, IP-10, MIP-1betam and MCP-2.

2 is essential for the chemotactic activity of MCP-2.

3 d this accounts for the unique activities of MCP-2.

4 cross-desensitization studies indicate that MCP-2 acts via CCR5.

5 MCP-2 also bound to and induced chemotaxis of CCR5/293 c

6 ) brain samples in which decreased levels of MCP-2 and increased levels of mir-146a were observed, su

7 nt (eotaxin, monocyte chemotactic protein-2 (MCP-2) and -3 (MCP-3), liver and activation-regulated ch

8 monocyte chemotactic protein 1 [MCP-1], and MCP-2) and the serum levels of other proinflammatory cyt

9 monocyte chemoattractant protein 1 (MCP-1), MCP-2, and granulocyte colony-stimulating factor in endo

10 significant increases in MIP-1beta, IL-28A, MCP-2, and IFN-alpha as compared with mock-infected cell

11 a, monocyte chemoattractant protein (MCP)-1, MCP-2, and interferon-inducible protein-10 in the pancre

12 to monocyte chemoattractant protein (MCP)-4, MCP-2, and MCP-1 in chemotaxis assays.

13 Hepatic CCR2, MCP-1, MCP-2, and MCP-3 messenger RNA expression was increased

14 or monocyte chemoattractant protein (MCP)-1, MCP-2, and MCP-3, in hepatic fibrosis.

15 gen species production in response to MCP-1, MCP-2, and MCP-3.

16 e sequence homology to other C-C chemokines, MCP-2 appears to have unique functional properties in co

17 The MCP-2 binding was competed for by MCP-1 and MCP-3, but l

18 ansfected with C-C chemokine receptors, 125I-MCP-2 bound to human embryonic kidney 293 cells transfec

19 ies of MCP-2 on leukocytes, we observed that MCP-2, but not MCP-1, effectively competed with MIP-1bet

20 Confocal microscopy indicates that MCP-2 caused remarkable and dose-dependent internalizati

21 MIP-1beta/CCL-4, MIP-2/CXCL2/3, MCP-1/CCL-2, MCP-2/CCL-8, MCP-3/CCL-7, MCP-5/CCL-12, KC/CXCL-1, and L

22 merization of the CCR2 ligands MCP-1 (CCL2), MCP-2 (CCL8), MCP-3 (CCL7), MCP-4 (CCL13), and eotaxin (

23 ractions of three CC chemokines, MCP-1/CCL2, MCP-2/CCL8, and MCP-3/CCL7, with HS-derived oligosacchar

24 of the chemokine receptor, CCR2 (MCP-1/CCL2, MCP-2/CCL8, MCP-3/CCL7, MCP-4/CCL13, and Eotaxin/CCL11),

25 CL4) and monocyte chemoattractant protein 2 (MCP-2; CCL8) mRNA levels from mycoplasma-infected mice a

26 Mig (CXCR3 ligand), TARC (CCR4 ligand), and MCP-2 (CCR5 ligand) were detected in intratumoral blood

27 mir-146a prevented HIV-induced secretion of MCP-2 chemokine.

28 2) and CC (CCL5/RANTES, CCL2/MCP-1, and CCL8/MCP-2) chemokines.

29 As predicted, MCP-2 competitively inhibited MIP-1beta binding to HEK29

30 evels of monocyte chemoattractant protein 2 (MCP-2), demonstrating that chemokine induction also occu

31 nal interactions between the two subunits of MCP-2 dimer: a hydrogen bond between pGlu1 and Asn17 and

32 Recombinant MCP-2 has Gln1 at the N terminus, 12-15% of which cycliz

33 mokines, the actual functional receptors for MCP-2 have not yet been identified.

34 showed significant migration in response to MCP-2, in addition to responding to other specific chemo

35 Furthermore, MCP-2 induces a robust, pertussis toxin-sensitive calciu

36 Furthermore, MCP-2 inhibited the entry/replication of HIV-1ADA in CCR

37 in-2 (IL-2), monocyte chemotactic protein 2 (MCP-2), interferon gamma inducible protein-10 (IP-10), i

38 These data confirm that MCP-2 is a ligand for CCR5 on CD4(+) lymphocytes and can

39 ene targets for mir-146a, the chemokine CCL8/MCP-2 is a ligand for the CCR5 chemokine receptor and a

40 MCP-2 is a potent inhibitor of HIV-1 by virtue of its hi

41 We further show that CCL8/MCP-2 is a target for mir-146a in HIV-1 infected microgl

42 MCP-2 is also a member of the CC chemokine subfamily and

43 Monocyte chemotactic protein 2 (MCP-2) is a CC chemokine that utilizes multiple cellular

44 ta1, and TNF-alpha cytokines while restoring MCP-2 levels, suggesting that H4K12ac may be playing a m

45 ta for binding to monocytes, suggesting that MCP-2 may interact with CCR5.

46 ed from studies on leukocytes suggested that MCP-2 may share the receptors with these C-C chemokines,

47 response of eosinophils to eotaxin, RANTES, MCP-2, MCP-3, and MCP-4 was shown to be mediated through

48 nd for CCR2, which responds to murine MCP-1, MCP-2, MCP-3, and MCP-5.

49 (GRO), IL-5, IL-6, IL-7, IL-8, IL-10, MCP-1, MCP-2, MCP-3, and monokine induced by gamma-interferon.

50 Others (MCP-2, MCP-3, eotaxin, lymphotactin, LARC, TCA-3) displa

51 There was no compensatory upregulation of MCP-2, MCP-3, or MCP-5 in MCP-1-null mice with EAE.

52 beta interferon) and chemokine (RANTES, MIG, MCP-2, MIP-1alpha, and interleukin-8) expression was exa

53 The chemotactic activity of such MCP-2 mixture, which contains 12-15% pGlu1-form and 85-8

54 n 1 (TRAF1), interleukin-1alpha (IL-1alpha), MCP-2, N-cadherin, and beta1 integrin (CD29).

55 e identified high affinity binding sites for MCP-2 on human peripheral blood monocytes.

56 rther characterize the binding properties of MCP-2 on leukocytes, we observed that MCP-2, but not MCP

57 tractant protein-1 (MCP-1), MCP-3, MCP-5, or MCP-2 plus MCP-5 revealed that MCP-3 and MCP-1 are the C

58 er when compared with that of fully cyclized MCP-2 preparation.

59 Furthermore, MIP-1beta- and MCP-2-producing cells and CD4+ T cells were found to be

60 after transplantation, the chemokines MCP-1, MCP-2, RANTES, MIG, IP-10, I-TAC, and two CC chemokine r

61 on of CD4+ Th cells expressing the MIP-1beta/MCP-2 receptor, CCR5, in the lungs of mice.

62 We demonstrate that MCP-2 specifically inhibits replication of R5 HIV-1 and

63 determined the complete crystal structure of MCP-2 that contains both pGlu1 and an intact C-terminus.

64 eptor for RANTES, MIP-1alpha, MIP-1beta, and MCP-2 that functions as the front line coreceptor for hu

65 ed genes, including chemokine ligand 8 (CCL8/MCP-2), that may provide possible targets for early-stag

66 The binding of 125I-MCP-2 to these receptor-transfected cells was displaced

67 These results clearly demonstrate that MCP-2, unlike MCP-1, uses both CCR1 as well as CCR2B as

68 These results indicated that MCP-2 uses CCR5 as one of its functional receptors and i

69 MCP-2 was highly expressed in stromal cells in 3 patient

70 MCP-2 was the next most potent ligand, with an IC(50) of

71 In this study, by using radioiodinated MCP-2, we identified high affinity binding sites for MCP

72 IL-10, IL-6, MIP-1alpha, MIP-1beta, and MCP-2 were associated with increased odds of SM.