ライフサイエンスコーパス: ASGP-R

1 ears to be an independent variable affecting ASGP-R activity.

2 cubation of PHUECs in asialofetuin (ASF), an ASGP-R ligand, significantly reduced invasion.

3 between lacto-N-neotetraose-terminal LOS and ASGP-R allows gonococcal entry into PHUECs.

4 the physiologic relationship between PSS and ASGP-R activity may aid in the interpretation of quantit

5 o determine the relationship between PSS and ASGP-R density in the absence of parenchymal disease.

6 taken a genetic approach using wild-type and ASGP-R-deficient mice to determine that the ASGP-R in vi

7 As ASGP-R-mediated endocytosis is clathrin dependent, clath

8 The pH dissociation profiles of ASOR.ASGP-R complexes were also identical for complexes conta

9 n that content of plasma membrane-associated ASGP-R is decreased after ethanol exposure, although the

10 binding is based on the correlation between ASGP-R density and hepatic functional reserve.

11 For both ASGP-R and APN and for both treatments, the block in tra

12 y transfected SK-Hep-1 cell lines expressing ASGP-R complexes containing H1 and either H2b or H2c had

13 mutant LOS lacking the galactose ligand for ASGP-R.

14 05) in the presence of antibody specific for ASGP-R as well as the introduction of competing sugars i

15 eloped a novel fluorescent polarization (FP) ASGP-R binding assay to determine the binding affinities

16 rat hepatic lectins (RHL) 1, 2, and 3; human ASGP-R contains two subunits, HHL1 and HHL2.

17 ecular weight corresponding to that of human ASGP-R.

18 In summary, the H2 subunit of the human ASGP-R contains functional, although weak, signal(s) for

19 The human ASGP-R contains two subunits, H1 and H2.

20 The human ASGP-R is a hetero-oligomeric complex composed of H1 and

21 The human ASGP-R is a hetero-oligomeric complex composed of two su

22 TSA also impaired ASGP-R endocytic trafficking, but to a lesser extent.

23 e the sequences of subunits in all mammalian ASGP-R species are highly conserved especially at the re

24 The mean ASGP-R density (nmol/g of liver) was significantly decre

25 heart time-activity data was used to measure ASGP-R concentration, as well as hepatic plasma volume a

26 e to investigate the capability of the minor ASGP-R subunit, H2, to function independently of H1, bec

27 assay to determine the binding affinities of ASGP-R-targeted molecules.

28 study was to further clarify the capacity of ASGP-R to phagocytose apoptotic cells in relationship to

29 de in the carbohydrate recognition domain of ASGP-R but not preimmune antibody.

30 hway, such as transcytosis, for the entry of ASGP-R.ASOR complexes into these cells.

31 s based on using the three-pronged ligand of ASGP-R as a computational probe to derive the 3D conform

32 Co-localization of ASGP-R with gonococci was observed.

33 Siaalpha2,6Gal are elevated in the plasma of ASGP-R-deficient mice.

34 This work demonstrates the presence of ASGP-R on human sperm.

35 In order to study the function(s) of ASGP-R palmitoylation, we mutated these Cys residues to

36 e preparations from rat liver as a source of ASGP-R and Cy5 fluorophore-labeled triGalNAc synthetic l

37 re compatible with the trimeric structure of ASGP-R.

38 ion may be related to altered trafficking of ASGP-R.

39 s no effect on ER-to-Golgi transportation of ASGP-R, however, it results in its deposition in cis-med

40 e Golgi-to-plasma membrane transportation of ASGP-R.

41 constitutive recycling of hetero-oligomeric ASGP-R complexes.

42 resent with H1 in the same hetero-oligomeric ASGP-R complexes.

43 Binding of purified ASGP-R ligand decreased in the presence of gonococci.

44 Following deglycosylation of purified ASGP-R, we detected the H2b and H2c proteins in HepG2 an

45 Rat ASGP-R contains three subunits, designated rat hepatic l

46 We have determined that the rat ASGP-R specifically binds oligosaccharides terminating w

47 on the newly defined specificity of the rat ASGP-R we hypothesize that glycoproteins bearing structu

48 blood may be endogenous ligands for the rat ASGP-R.

49 owed that human asialoglycoprotein receptor (ASGP-R) and the terminal lactosamine of lacto-N-neotetra

50 Using the asialoglycoprotein receptor (ASGP-R) as a model, we have previously shown decreased b

51 niques that use asialoglycoprotein receptor (ASGP-R) binding is based on the correlation between ASGP

52 tibodies to the asialoglycoprotein receptor (ASGP-R) demonstrated the presence of this receptor on in

53 Asialoglycoprotein receptor (ASGP-R) has been actively investigated for targeted deli

54 the liver, the asialoglycoprotein receptor (ASGP-R) has been shown to be involved in the phagocytosi

55 hologues of the asialoglycoprotein receptor (ASGP-R) in different mammals differ in their specificity

56 The hepatic asialoglycoprotein receptor (ASGP-R) internalizes desialylated glycoproteins via the

57 l human hepatic asialoglycoprotein receptor (ASGP-R) is a hetero-oligomer composed of two subunits, d

58 The asialoglycoprotein receptor (ASGP-R) is an abundant, carbohydrate-specific, endocytic

59 The hepatic asialoglycoprotein receptor (ASGP-R) is an endocytic receptor that mediates the inter

60 mmalian hepatic asialoglycoprotein receptor (ASGP-R) is an endocytic recycling receptor that mediates

61 The hepatic asialoglycoprotein receptor (ASGP-R) is posttranslationally modified in the Golgi en

62 can bind to the asialoglycoprotein receptor (ASGP-R) on human sperm.

63 fficking of the asialoglycoprotein receptor (ASGP-R) was impaired in ethanol-treated WIF-B cells.

64 ligands of the asialoglycoprotein receptor (ASGP-R), thyroglobulin, asialothyroglobulin, and antibod

65 ctable trimeric asialoglycoprotein receptor (ASGP-R), which consists of human hepatic subunits (two s

66 ntified for the asialoglycoprotein receptor (ASGP-R), which is abundantly expressed by parenchymal ce

67 ytes called the asialoglycoprotein receptor (ASGP-R), which is known to have a high affinity for spec

68 zed through the asialoglycoprotein receptor (ASGP-R).

69 The asialoglycoprotein-receptor (ASGP-R) located on liver parenchymal cells was originall

70 that H2b and H2c are not present in the same ASGP-R complexes with H1.

71 study provides detailed information about TA-ASGP-R interactions and the symmetry of the complex.

72 Microscopy studies showed that ASGP-R traffics to the cell surface after gonococcal cha

73 olated the receptor and identified it as the ASGP-R.

74 require desialylation before removal by the ASGP-R on hepatocytes.

75 In conclusion, the ASGP-R is involved in the recognition and uptake of apop

76 e basis of their relative affinities for the ASGP-R and their relative abundance.

77 nor has a naturally occurring ligand for the ASGP-R been identified.

78 GalNAc); however, endogenous ligands for the ASGP-R have not to date been definitively identified.

79 iaalpha2,6Gal are endogenous ligands for the ASGP-R, and that the ASGP-R helps to regulate the relati

80 A significant change in the ASGP-R density occurs with PSS in the absence of parench

81 ng either both (hH1 and hH2) subunits of the ASGP-R (3T3-22Z cells) or both hH1 and a functionally de

82 re, we have determined that subunit 1 of the ASGP-R accounts for the binding of terminal Siaalpha2,6G

83 The recombinant subunit 1 of the ASGP-R from the rat (RHL-1 or rat hepatic lectin) and th

84 epatocytes expressing the hH1 subunit of the ASGP-R fused to green fluorescent protein, we could show

85 from the circulation, and the ability of the ASGP-R hepatic lectin-1 subunit to bind SiaGGnM-BSA, we

86 and antibody binding characteristics of the ASGP-R in rats fed ethanol over a 5-week time course.

87 We conclude that palmitoylation of the ASGP-R is required for its efficient endocytosis of liga

88 In summary, an early inactivation of the ASGP-R occurs during ethanol exposure followed by an act

89 thanol feeding, biosynthetic labeling of the ASGP-R was decreased in the ethanol cells, indicating im

90 cells, indicating impaired synthesis of the ASGP-R.

91 ng terminal Siaalpha2,6Gal will saturate the ASGP-R and compete with each other on the basis of their

92 ogenous ligands for the ASGP-R, and that the ASGP-R helps to regulate the relative concentration of s

93 ASGP-R-deficient mice to determine that the ASGP-R in vivo does indeed account for the rapid clearan

94 We have also determined that the ASGP-R is able to bind core-substituted oligosaccharides

95 Our data indicate that the ASGP-R is initially inactivated during the time course o

96 We recently demonstrated that the ASGP-R mediates the clearance of glycoproteins bearing S

97 We propose that the ASGP-R mediates the clearance of glycoproteins that bear

98 These data suggest that the ASGP-R on human sperm cells recognizes and binds wild-ty

99 Thus, the ASGP-R appears to directly participate in the rapid in v

100 a fluorescent-labeled probe specific to the ASGP-R mRNA demonstrated this message in uninfected and

101 alofetuin, which can selectively bind to the ASGP-R.

102 proteins bind to and cointernalize with the ASGP-R in cultured human hepatocytes.

103 ral ligand readily able to interact with the ASGP-R.

104 s spent in determining binding affinities to ASGP-R.

105 (e.g., triGalNAc) bind with high affinity to ASGP-R and, when conjugated to a therapeutic agent, can

106 Reaction of hydroxylamine-treated ASGP-R with [14C]iodoacetamide resulted in the specific

107 ury as altered uptake of apoptotic cells via ASGP-R may result in the release of proinflammatory medi