ライフサイエンスコーパス: LAMP2

1 assays were used to localize cathepsin B and Lamp2.

2 r Gag and the late endosome/lysosomal marker Lamp2.

3 localization but little co-localization with LAMP2.

4 mples contained mutations in GLA, PRKAG2, or LAMP2.

5 P1 and CD63 and an increase in the amount of LAMP2.

6 AG2, lysosome-associated membrane protein 2 (LAMP2), alpha-galactosidase (GLA), and acid alpha-1,4-gl

7 Mutations in sarcomere protein, PRKAG2, LAMP2, alpha-galactosidase A (GLA), and several mitochon

8 eless, the protease plays a role in reducing LAMP2 and LAP activity levels, as these are partially re

9 th viral proteins (p17 and sigmaC), p62 with LAMP2 and LC3 with Rab7 was observed under a fluorescenc

10 Quantitation of cellular LAMP2 and NPC1 protein levels suggest that LAMP proteins

11 ompe's disease (GAA) were not found, but two LAMP2 and one PRKAG2 mutations were identified in proban

12 and the autophagy-lysosome pathway proteins Lamp2 and p62 relocalized to the area of the vimentin ac

13 ting ventricular preexcitation revealed four LAMP2 and seven PRKAG2 mutations.

14 ed markers specific for lysosomes (LAMP1 and LAMP2) and autophagosomes (LC3-II/I).

15 p62, lysosome-associated membrane protein 2 (LAMP2), and microtubule-associated protein light chain (

16 resence of acid phosphatase, accumulation of LAMP2, and fusion with rhodamine B-isothiocyanate-labele

17 did not colocalize with the lysosomal marker LAMP2, and lysosomes were redistributed and dramatically

18 ive specific genes, AP3B1, ATP6AP1, BLOC1S1, LAMP2, and RAB11A, has confirmed novel roles for these p

19 ins; ARH, a coat protein that binds megalin; LAMP2; and LC3.

20 We show here that human LAMP1 and LAMP2 bind cholesterol in a manner that buries the chole

21 LAMP2 cardiomyopathy is a profound disease process chara

22 of bone marrow-derived DC were retained in a LAMP2+ compartment.

23 The B5R protein was also associated with LAMP2-containing vesicles when F13L-GFP was coexpressed,

24 d lysosome-associated membrane protein gene (LAMP2; Danon disease) produce a cardiomyopathy in young

25 LAMP2 deficiency causes Danon's disease, an X-linked hyp

26 f the Hprt region as: Agtr2-Pem-Ant2-DXMit50-Lamp2-DXMit49.

27 some-associated membrane proteins, LAMP1 and LAMP2, from Pompe iPSC-CMs demonstrated higher electroph

28 2A), one of the three splice variants of the lamp2 gene, and this binding is limiting for their degra

29 Isoelectric focusing studies revealed that LAMP2 has a more alkaline pI in Pompe compared with cont

30 in genes and 3 other genes (GLA, PRKAG2, and LAMP2) implicated in idiopathic cardiac hypertrophy.

31 ization and substantial co-localization with LAMP2 in late endosomes.

32 Clinical features associated with defects in LAMP2 included male sex, severe hypertrophy, early onset

33 A detailed examination of LAMP2 indicated that the reduced LAMP2 levels are not th

34 ealed incorporation of CD63 and CD81 but not Lamp2 into virions budding at the plasma membrane, and t

35 We also observe that LAMP2 is located at the plasma membrane in clinical samp

36 LAMP2 is needed for chaperone-mediated autophagy, and it

37 Furthermore, we show that the depletion of LAMP2 is sufficient to increase acidosis-mediated toxici

38 ceptor, epidermal growth factor receptor, or Lamp2, is detected.

39 The gene expression of other LAMP2 isoforms and proteasome and lysosomal proteases ac

40 Transcripts for the three LAMP2 isoforms increased with B cell activation, althoug

41 mination of LAMP2 indicated that the reduced LAMP2 levels are not the result of an altered biosynthet

42 6 treated cells to sorafenib reduced p62 and LAMP2 levels, decreased the ratio of LC3 to LC3II, and r

43 the levels of three other lysosomal markers: LAMP2, lysosomal acid phosphatase (LAP), and CD63.

44 n be distinguished from cholesterol-enriched LAMP2(+) lysosomes.

45 l in the first 2 h and were instead found in LAMP2+, major histocompatibility complex class II+ (MHC-

46 t of lysosome-associated membrane protein-2 (LAMP2)(+)/mannose 6-phosphate receptor(-) vesicles that

47 ient samples, there is a high correlation of LAMP2 mRNA and protein expression with progression.

48 ster of the proband is a carrier of the same LAMP2 mutation and has HCM without skeletal myopathy or

49 ly in 7 young patients (6 boys) with defined LAMP2 mutations from the time of diagnosis (age 7-17 yea

50 this study we investigated the frequency of LAMP2 mutations in an unselected pediatric HCM populatio

51 LAMP2 mutations may account for a significant proportion

52 LAMP2 mutations typically cause multisystem glycogen-sto

53 ellular acidosis (as indicated by the marker LAMP2 near/at the plasmalemma), which can explain the ad

54 abnormalities revealed mutations in neither LAMP2 nor PRKAG2.

55 tion breakpoint and six genes (ANT2, NDUFA1, LAMP2, OCRL, IGSF1, and HDGF) at better than 100-kb reso

56 glycogen-storage cardiomyopathy produced by LAMP2 or PRKAG2 mutations resembles hypertrophic cardiom

57 hagosome-lysosome fusion by shRNAs targeting LAMP2 or Rab7a resulted in inhibition of viral protein s

58 ed, lysosomal-associated membrane protein 2 (LAMP2)-positive lysosomes.

59 nts (lysosome-associated membrane protein 2 (LAMP2)-positive).

60 y alanines, only partially co-localized with LAMP2-positive compartments following inhibition of lyso

61 elet-derived growth factor receptor alpha to LAMP2-positive endomembranes in the absence of ligand, s

62 receptor, where the receptor is shuttled to LAMP2-positive lysosomes.

63 LAMP1 and LAMP2 proteins are highly abundant, ubiquitous, mammalia

64 anocytes (ie, Silver/Pmel17, Melan-A/MART-1, LAMP2, Rab 27, transferrin, c-kit, adaptin-3, and the HP

65 of the lysosomal membrane proteins LAMP1 and LAMP2 resulted in decreased cell viability, as did treat

66 phagosome maturation) by chloroquine (CQ) or Lamp2 shRNA, it was substantially diminished by inhibiti

67 d with a marker of late endosomes/lysosomes, LAMP2, specifying redirection from a recycling to a degr

68 68, lysosomal-associated membrane protein 2 (LAMP2), stabilin-1, and macrophage receptor with collage

69 rate doxorubicin (DOX) became sequestered in LAMP2-stained lysosomes, but this was not observed in no

70 ated that intracellular Pgp was localized to LAMP2-stained lysosomes.

71 Prominent among these is LAMP2 that functions to protect lysosomal membranes from

72 degradation pathway due to overexpression of lamp2, the human form of lgp96, the degradation of Ikapp

73 e experiments show that the ability of human LAMP2 to facilitate cholesterol export from lysosomes re

74 cise resulted in rapid translocation of mTOR/LAMP2 towards the cell membrane.

75 LAMP2 upregulation by acidosis is confirmed both in vitr

76 LAMP2 was amplified from genomic DNA isolated from perip

77 cifically, in ARSACS HDFs cellular levels of Lamp2 were elevated while levels of p62, which is degrad

78 mTOR and the lysosomal protein LAMP2 were highly co-localised in basal samples.

79 Accumulation of p62 and Lamp2 were prominent in the brain suggesting the impairm

80 We also sequenced PRKAG2 and LAMP2, which encode metabolic proteins; mutations in the