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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

35 Monocytes overexpress sialoadhesin nonspecifically during ITx rejection and sy

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

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

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

39 2, CD33, myelin-associated glycoprotein, and sialoadhesin) show that OB-BP1, OB-BP2/Siglec-5, and CD3

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

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

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

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

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

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

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

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

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

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

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

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

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

53 Expression of sialoadhesin was confirmed by immunofluorescence in porc

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

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

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