ライフサイエンスコーパス: LAMP-2

1 the lysosome-associated membrane protein-2 (Lamp-2).

2 tors DC-LAMP and CD68, as well as LAMP-1 and LAMP-2.

3 d the alternatively spliced domains of avian LAMP-2.

4 zed with the late endosomal/lysosomal marker LAMP-2 (2 and 4 h postinfection), while less than 10% of

5 ase report, who have primary deficiencies of LAMP-2, a principal lysosomal membrane protein.

6 PLEKHM2 joins LAMP-2 and BAG3 as a disease gene altering autophagy res

7 ed with colocalization of the phagosome with LAMP-2 and BiP, while colocalization with LAMP-1 and cat

8 sosome associated membrane protein (LAMP)-1, LAMP-2 and the a2 isoform of V-ATPase (a2V, an enzyme in

9 identified two VEGF-C/NRP-2-regulated genes, LAMP-2 and WDFY-1, that have previously been suggested t

10 intensely for the lysosomal proteins Lamp-1, Lamp-2, and cathepsin D as well as for G(M3) ganglioside

11 dosomal/lysosomal markers, including LAMP-1, LAMP-2, and cathepsin D.

12 n aberrant compartment that contains LAMP-1, LAMP-2, and NPC1, but not CI-MPR, similar to the cholest

13 port a mechanistic relationship between anti-LAMP-2 antibodies and ANCA glomerulonephritis.

14 There was no correlation between anti-LAMP-2 antibodies and disease activity.

15 The prevalence of anti-LAMP-2 antibodies and their relationship to disease in A

16 ermore, Wistar Kyoto rats injected with anti-LAMP-2 antibodies did not develop glomerulonephritis.

17 However, in contrast to anti-LAMP-2 antibodies from ANCA-positive patients, these ant

18 Staining for the LAMP-1 and LAMP-2 antigens showed that the vesicles are enlarged ly

19 ese distinct cargo proteins, only LAMP-1 and LAMP-2 are concentrated in the AP-3-positive membrane do

20 In summary, we identify LAMP-2 as an endocytic receptor on human MoDC that route

21 Furthermore, we detected LAMP-2 autoantibodies in two ANCA-negative patients.

22 LAMP-2 autoantibodies rapidly became undetectable after

23 Prevalence of LAMP-2 autoantibodies was similar in both those with mye

24 ysosomal membrane proteins CD63, lamp-1, and lamp-2, but not of nonlysosomal proteins.

25 howed increased lysosomal proteins including LAMP-2, cathepsin D and LC3.

26 ysosome, as documented by the acquisition of LAMP-2, cathepsin D, and lysosomal tracer Texas Red oval

27 osomal membrane proteins LAMP-1 (CD107a) and LAMP-2 (CD107b) after peptide stimulation.

28 n this study we identify LAMP-1 (CD107a) and LAMP-2 (CD107b) on the surface of human monocyte-derived

29 U-Omp19 retains the Ag in Lamp-2(+) compartments after its internalization and pro

30 AMP-1, and to a lesser extent that of CD107b/LAMP-2, correlated with lymphocyte CG content.

31 Our data indicate that in hepatocytes LAMP-2 deficiency either directly or indirectly leads to

32 oskeletal myopathy, we conclude that primary LAMP-2 deficiency is the cause of Danon disease.

33 In LAMP-2-deficient hepatocytes the half-life of both early

34 e 6-phosphate receptor was slightly lower in LAMP-2-deficient hepatocytes, whereas that of 46-kDa man

35 In LAMP-2-deficient mice autophagic vacuoles accumulate in

36 From these results and the finding that LAMP-2-deficient mice manifest a similar vacuolar cardio

37 l upregulation of this splice variant of the lamp-2 gene.

38 Depletion of Lamp-1 and Lamp-2 had no measurable effect on endosomal/lysosomal p

39 d against human lysosome membrane protein-2 (LAMP-2), has recently been described as a sensitive and

40 encoding the lysosome-associated protein-2 (LAMP-2) have been identified in these patients, suggesti

41 sine signal from the human lysosomal protein LAMP-2, HTGYEQF.

42 cation using the lysosomal marker protein 2 (LAMP-2) immunolabeling showed higher neuronal lysosomal

43 Co-localization of p62 and LAMP-2 in affected cells indicates that formation or rec

44 accumulation of the proteins LC3-II, p62 and LAMP-2 in neurons and astrocytes of mice with mutations

45 afficking of the lysosomal membrane protein, Lamp-2, in contrast to fibroblasts from AP-3-deficient p

46 maturation of cathepsin D and degradation of Lamp-2, indicating a general impairment of lysosomal act

47 derived dendritic cells (MoDC) and show only LAMP-2 is internalized after ligation by specific Abs, i

48 Lysosomal membrane protein 2 (LAMP-2) is a target of antineutrophil cytoplasmic autoan

49 Overexpression of Lamp-2 isoform A (Lamp-2a), an established component of

50 ernae and post-Golgi vesicles containing the LAMP 2 late endosomal-lysosomal marker.

51 D and the lysosomal glycoproteins LAMP-1 and LAMP-2 localized to the C. burnetii vacuole but not the

52 h large vacuoles that are immunoreactive for LAMP-2 (lysosomal-associated membrane protein 2), consis

53 CpG-A shows higher co-localization with LAMP-2(+) lysosomes than CpG-B and induces DNase II loca

54 n CpG-B and induces DNase II localization in LAMP-2(+) lysosomes.

55 In conclusion, antibodies that react with LAMP-2 may exist at very low titers in a minority of pat

56 diac muscle sections revealed the absence of LAMP-2 on immunohistochemical staining.

57 Finally, IgG from LAMP-2-positive ANCA-negative patients bound specificall

58 epidermal growth factor (EGF) trafficking to LAMP-2-positive compartments and EGF receptor degradatio

59 reductase (GILT) is an enzyme located in the Lamp-2-positive compartments of APC.

60 WNK4 expression also increased LAMP-2-positive lysosomal content, indicating that the k

61 tibodies from all 8 patients bound to native LAMP-2 purified from human glomeruli and recombinant hLA

62 We measured anti-LAMP-2 reactivity in 680 sera samples (two academic cent

63 trols used to define a reference range, anti-LAMP-2 reactivity was present in 21% of ANCA sera from t

64 pression of CD107a/LAMP-1, but not of CD107b/LAMP-2, reduced the granule-mediated killing of transfec

65 the lysosome-associated membrane protein-2 (LAMP-2) regulate these pathways influencing immune recog

66 Deglycosylation of Lamp-1 and Lamp-2 resulted in their rapid degradation, whereas Limp

67 ize with the late endosomal-lysosomal marker LAMP-2, similar to killed L. pneumophila.

68 e 1500-fold and 10,000-fold higher than anti-LAMP-2 titers, respectively.

69 tation, the frequencies of autoantibodies to LAMP-2 were 89%, 91%, and 80%, respectively, among three

70 Antibodies to endolyn, but not lamp-2, were preferentially internalized from the apical