ライフサイエンスコーパス: sialoadhesin

1 -regulated genes, including Siglec-1 (CD169, sialoadhesin).

2 ntarity of scaffold structure and binding to sialoadhesin.

3 Sialoadhesin, a macrophage restricted lectin that binds

4 structures were differentially recognized by sialoadhesin, a mammalian macrophage sialic acid binding

5 carbohydrate binding specificities of three sialoadhesins, a subgroup of I-type lectins (immunoglobu

6 cell surface ligands for the I-type lectins sialoadhesin and CD22.

7 Modulating the interaction between sialoadhesin and its sialic acid ligands has important i

8 Expression of sialoadhesin and Siglec-F ligands increased, and that of

9 Given similarities between sialoadhesin and the unidentified macrophage lectin in o

10 e selectins), I-type lectins (e.g., CD22 and sialoadhesin), and a complement regulatory protein (the

11 and 7-deoxysialic acid derivatives supported sialoadhesin binding at near control levels (the other d

12 These data are consistent with sialoadhesin binding to one face of the sialic acid moie

13 Sialoadhesin (but not CD22) binding is selectively enhan

14 Sialoadhesin (CD169) facilitates T-cell priming when ove

15 We determined that sialoadhesin (CD169; Siglec-1) is required for the captu

16 Siglec-1 (sialoadhesin, CD169) is a surface receptor on human cell

17 dependent viral entry into AMs used ACE2 and Sialoadhesin/CD169, whereas IM entry used DC-SIGN/CD209.

18 Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glyco

19 ion to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprot

20 rs ago, only four Siglecs were known, namely sialoadhesin, CD22, myelin-associated glycoprotein and C

21 lectin in our model, we hypothesized porcine sialoadhesin contributed to recognition of human erythro

22 lectins myelin-associated glycoprotein, and sialoadhesin did not disrupt their ability to mediate si

23 Fc, and another sialic acid binding protein, sialoadhesin, each bind to neurons in a sialic acid- dep

24 In contrast, sialoadhesin had less exacting specificity, binding to g

25 ing overlapped that of the macrophage marker sialoadhesin in frozen sections and coincided with that

26 we show that receptor sialylation of soluble sialoadhesin inhibits its binding to Jurkat cell ligands

27 ese data support the hypothesis that porcine sialoadhesin is a xenogeneic receptor that mediates porc

28 Since sialoadhesin is expressed on some macrophages in vivo, w

29 Thus, some sialoadhesin ligands are masked by 9-O-acetylation, pres

30 -deficient or B- and T-deficient mice lacked sialoadhesin+ marginal zone macrophages and lacked MAdCA

31 a > GT1b, GD1a >> GM1 (nonbinding)), whereas sialoadhesin-mediated adhesion was comparable with alpha

32 in vivo macrophage sialylconjugates enhances sialoadhesin-mediated lectin activity.

33 nhibited approximately 90% by an antiporcine sialoadhesin monoclonal antibody and by human erythrocyt

34 (pSn CHO) bound human erythrocytes, while a sialoadhesin mutant cell line did not.

35 The neural sialoadhesins, myelin-associated glycoprotein (MAG) and

36 Monocytes overexpress sialoadhesin nonspecifically during ITx rejection and sy

37 Ac) on the surface of human erythrocytes and sialoadhesin on the surface of the porcine Kupffer cells

38 Surface expression of SIGLEC1, also known as sialoadhesin or CD169, is considered a primary determina

39 able transgenic cell line expressing porcine sialoadhesin (pSn CHO) bound human erythrocytes, while a

40 2, CD33, myelin-associated glycoprotein, and sialoadhesin) show that OB-BP1, OB-BP2/Siglec-5, and CD3

41 ition of interferon-inducible 44 (IFI44) and sialoadhesin (Siglec-1) to COMP and TSP-1 in multiple re

42 First, we report that binding of siglec-1 (sialoadhesin), siglec-3 (CD33), siglec-4a (myelin-associ

43 Sialoadhesin (Sn) is a macrophage (Mphi)-restricted rece

44 Sialoadhesin (Sn) is a sialic acid-binding Ig-like lecti

45 CD169 is known as sialoadhesin (Sn), a macrophage-specific adhesion and en

46 he identification of two of these ligands as sialoadhesin (Sn), an Mo-specific membrane molecule, and

47 to Ig domains from another Ig family member, sialoadhesin (Sn), which also binds to sialic acid in th

48 Several siglecs, including sialoadhesin (Sn, siglec-1) and siglec-5, bind to NeuAca

49 Sialoadhesin (Sn, Siglec-1, CD169) is a member of the si

50 Sialoadhesin (Sn, Siglec-1, CD169), a sialic acid-bindin

51 tures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid

52 Human siglec-1 (sialoadhesin) strongly prefers Neu5Ac over Neu5Gc.

53 Binding of MAG, SMP, and sialoadhesin was abrogated by chemical modification of e

54 Expression of sialoadhesin was confirmed by immunofluorescence in porc

55 The binding of the sialosides to sialoadhesin was evaluated by an enzyme-linked immunosor

56 MAG), Schwann cell myelin protein (SMP), and sialoadhesin, were compared by measuring siglec-mediated

57 he macrophage-specific cell surface receptor sialoadhesin, which is a member of the newly recognized