Publication for Lamp1 and Lamp2

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
mmu Lamp1 lysosomal-associated membrane protein 1 16783 [link]
mmu Lamp2 lysosomal-associated membrane protein 2 16784

Pubmed ID Priority Text
18958159 0.98 LAMP-1 and LAMP-2) are recruited to the Salmonella-containing vacuole as well as Salmonella- associated filaments (Sifs) that emerge from the vacuole.
0.98 LAMP-1 depleted cells, the bacteria remain membrane bound as measured by their association with LAMP-2 protein.
0.98 LAMP-1 is predominantly used as a membrane marker for the SCV, under normal conditions of intracellular infection S. typhimurium specifically and quantitatively associate with LAMP-2.
0.98 LAMP-1 and LAMP-2 (Fig. 1B) suggesting that both proteins are prominently associated with the SCV and Sifs.
0.98 LAMP-2 knockdown cells for LAMP-1 revealed reduced association of LAMP-1 in a subset of bacterial clusters (viii).
0.98 LAMP-2 depletion measurably reduced detection of the SCV marker LAMP-1, suggesting LAMP-2 contributes to either the composition and function, or the stability of the SCV membrane.
0.98 LAMP-1 and LAMP-2.
0.97 LAMP-1 is not essential, but LAMP-2 may be partially important for the Salmonella-containing vacuolar membrane.
0.97 LAMP-2 knockdown promotes reduction of LAMP-1 at the SCV membrane
0.97 LAMP-1 and LAMP-2, while circumventing mannose-6-phosphate receptor trafficking between the Golgi and lysosomes.
0.96 LAMP-2 knockdown increases prevalence of LAMP-1 depleted bacteria.
0.96 LAMP-1 depleted Salmonella in LAMP-2 knockdown cells proliferate at an accelerated rate.
0.94 LAMP-1 and LAMP-2, suggesting that both are recruited to the SCV (indicated by the dotted line).
0.94 LAMP-1 and LAMP-2 are related proteins, we were interested in determining whether SifA is required for LAMP-2 recruitment to the SCV.
0.94 LAMP-1 and LAMP-2 levels in cells.
0.94 LAMP-2 along with that of LAMP-1 enabled each to be used as a marker for the SCV, as well as testing (in RNAi experiments) whether each was important to the SCV membrane.
0.93 LAMP-1 and LAMP-2 to Salmonella infection, we used RNAi to knockdown levels of these proteins in cells.
0.92 LAMP-1 displayed LAMP-2 levels that were modestly increased relative to control incubations.
0.91 LAMP-1 and LAMP-2 are both type I transmembrane proteins.
0.90 LAMP-1 knockdown cells were immuno-stained for LAMP-2 and revealed consistent colocalization of Salmonella with LAMP-2 (iv).
0.87 LAMP-1 and LAMP-2 consistently showed reduced actin levels.
0.79 LAMP-1/LAMP-2 double knockout is embryonically lethal.
0.78 LAMP-1 or LAMP-2 were comparable and this enabled us to ascertain the effect of knockdown of each protein on the recruitment of the other, to the SCV.
0.76 LAMP-2 did not abrogate LAMP-1 levels in cells and conversely knock down of LAMP-1 did not abrogate LAMP-2 levels in cells.
0.75 LAMP-2 function in the host is likely to be distinct from that of LAMP-1.
0.65 LAMP-1, LAMP-2 recruitment also requires SifA or a distinct SPI-2 effector.
0.63 LAMP-2 depletion increased the amount of LAMP-1 free bacteria.
0.58 LAMP-1 and LAMP-2 (Fig. 3D panels i-iii and Fig. 3E).
0.52 LAMP-1 is known to be more abundant than LAMP-2.
19929948 0.98 lysosome associated membrane protein-2 (LAMP-2) and LAMP-1, two abundant membrane proteins of late endosomes and lysosomes.
0.98 LAMP-1 and LAMP-2 (LAMP-/-), low-density lipoprotein (LDL) receptor levels and LDL uptake are increased as compared to wild-type cells.
0.98 LAMP-1 and LAMP-2 are 11 residues long and contain necessary information for their intracellular targeting after biosynthesis.
0.98 LAMP-2, when targeted to late endo-somes/lysosomes by the transmembrane and cytosolic domains of LAMP-1, was critical for the cholesterol transport.
0.97 Lysosome associated membrane protein-1 (LAMP-1) and LAMP-2 are major protein components of the lysosomal membrane.
0.96 LAMP-2A, but not LAMP-1, is able to abolish the late endosomal/lysosomal cholesterol accumulation in LAMP-/- MEFs
0.95 LAMP-/- cells was diminished by overexpression of any of the three isoforms of LAMP-2, but not by LAMP-1.
0.95 LAMP-2 single deficient MEFs showed a moderate cholesterol accumulation in late endosomes/lysosomes, while LAMP-1 single deficient MEFs were not different from wild-type cells.
0.95 LAMP-2A abolished the late endosomal/lysosomal cholesterol accumulation in LAMP-/- MEFs, while rat or mouse LAMP-1 showed no effect (Fig. 5A, B, E, and not shown).
0.94 LAMP-2 (or LAMP-1) is more likely to be critical.
0.92 LAMP-2 is more critical than LAMP-1 for the liver cholesterol homeostasis..
0.92 LAMP-/- MEFs was readily abolished by re-expression of LAMP-2, while re-expression of LAMP-1 had no effect.
0.90 LAMP-2A and LAMP-1 re-expression on late endosomal/lysosomal cholesterol accumulation in LAMP double defi-/ cient MEFs.
0.90 LAMP-/- MEFs, while expression of rat or mouse LAMP-1 was without effect.
0.89 LAMP-1 and LAMP-2 in intracellular cholesterol traffic.
0.77 LAMP-1 and LAMP-2 are distinct proteins.
0.70 LAMP-1 and LAMP-2, we generated mice deficient in each of these proteins.
0.65 LAMP-2 deficient liver compared to the wild-type liver, whereas the level of LAMP-1 deficient liver was not different from the wild-type (Fig. 4A).
0.59 LAMP-2 deficient tissue, we investigated cholesterol levels in the liver of mice deficient in LAMP-1 or LAMP-2.
0.53 LAMP-1/ LAMP-2 deficient MEFs.
31223479 0.98 LAMP-1, LAMP-2A and alpha-syn-GFP exhibited a co-localized distribution in some subcellular compartments in the DHM and Sal B treated mice (Additional file 4), further indicating increased degradation of alpha-syn aggregates via the CMA pathway.
0.98 LAMP-2A and macroautophagy by increasing LC3-II and LAMP-1, and is accompanied by the inhibition of microglial activation and neuroinflammation.
0.97 LAMP-2A and its homologous protein, LAMP-1, decreased levels of alpha-syn, reduced cytotoxicity and inhibited inflammatory responses when administered in cell and animal models.
0.97 LAMP-1 and LAMP-2A showed an increased expression level in SynT transfected H4 cells following treatment with DHM (10 muM, 48h) and Sal B (50 muM, 48h), compared to untreated cells.
0.97 LAMP-1 and LAMP-2A in more defined regions in cells treated with DHM and Sal B (Fig. 4a, b and d), whereas the untreated cells showed much less co-localization between alpha-syn and LAMP-1 or LAMP-2A (Fig. 4d), suggesting a potential relationship between the alpha-syn inclusions and the CMA pathway.
0.97 LAMP-1 and LAMP-2A via the mTOR signaling pathway.
0.96 LAMP-1, an important marker for the structure and function of lysosomal membranes and LAMP-2A, a key marker of CMA, in alpha-syn transgenic mice and decrease astrogliosis and microgliosis.
0.96 LAMP-1 and LAMP-2A clearly co-localized with alpha-syn in transgenic mice after administration of DHM and Sal B, which is in agreement with previous findings.
0.95 LAMP-1 (Fig. 6a, b, g, h) and LAMP-2A (Fig. 6c, d, i, j) significantly increased, compared with the saline control group (p<0.05) (Fig. 6a-f, left column), suggesting that DHM (Fig. 6a-f, middle column) and Sal B (Fig. 6A-F, right column) treatments activated CMA pathways in the brains of transgenic mice.
0.94 LAMP-1 (a marker of lysosomal homeostasis) and LAMP-2A (a key marker of CMA).
0.94 LAMP-1 and LAMP-2A with alpha-synuclein inclusions after treatment with DHM and Sal B. We also found increased levels of LAMP-1 and LAMP-2A both in vitro and in vivo, along with decreased levels of alpha-synuclein.
0.94 LAMP-1 (+75% +- 10.5% SEM for DHM treated group; +58% +- 9.8% SEM for Sal B treated group) and LAMP-2A (+63% +- 10.5% SEM for DHM treated group; +52% +- 8.7% SEM for Sal B treated group) levels in the lysates of SynT-aggregation H4 cells compared to the untreated group (Fig. 4c).
0.94 LAMP-1 and LAMP-2A were significantly up-regulated in DHM (Fig. 7a, c) and Sal B treated mice (Fig. 7b, d) in the CS and SNpc compared to the saline treated group, whereas levels of alpha-syn-GFP were significantly down-regulated following DHM and Sal B treatments.
0.93 LAMP-1 is highly structurally homologous to LAMP-2A suggesting that there may be an overlapping function of these two proteins.
0.93 LAMP-1 and LAMP-2A were significantly increased, while the levels of alpha-syn-GFP (the product of the transgene) were significantly decreased by DHM and Sal B treatments.
0.91 LAMP-1 (b) and LAMP-2A (c) was significantly increased after treatment with DHM or Sal B, as compared with WT alpha-syn transfected cells, rapamycin treated cells or CQ treated cells (after normalization to untreated cells).
0.90 LAMP-1 and LAMP-2A in DHM/Sal B treated groups compared with the saline treated group (8 animals/group, male).
0.65 LAMP-1, LAMP-2A in the SynT-aggregation model.
23080372 0.98 LAMP1 and LAMP2 double-deficient tissues, indicating that siRNA injection effectively inhibited the function of LAMP1 and LAMP2 in early embryos.
0.98 LAMP1 and LAMP2 siRNAs resulted in the observation of several degenerated membrane structures resembling autophagic vacuoles, which have been observed in several tissues in LAMP1 and LAMP2 double-deficient mice.
0.97 LAMP1 and LAMP2 are major protein components of the lysosome membrane.
0.97 LAMP1 and LAMP2 are functional during preimplantation development, because transcription factor EB, a master protein that regulates lysosomal biogenesis, is highly expressed after fertilization (S.T., unpublished data).
0.96 LAMP1 and LAMP2 is important for preimplantation embryo development.
0.95 LAMP1 and LAMP2, which are the major components of the lysosomal membrane and are essential for lysosomal biogenesis.
0.95 LAMP1 knockout mice have a nearly normal phenotype , whereas LAMP2 knockout mice have elevated postnatal mortality and accumulation of autophagic vacuoles in several tissues.
0.92 lysosome-associated membrane protein 1 and 2 (LAMP1 and LAMP2) were developmentally arrested at the two-cell stage.
0.91 LAMP1 and LAMP2 mRNA expression was effectively suppressed by siRNA injection, and this effect was cumulative when both siRNAs were injected together (Fig. 3C).
0.89 LAMP1 and LAMP2 siRNAs were developmentally arrested at the two-cell stage (Fig. 3A and B).
0.86 LAMP1 and LAMP2 siRNAs (Fig. 3D).
0.84 LAMP1 and LAMP2 siRNAs were developmentally arrested at the two-cell stage.
0.63 LAMP1 or LAMP2 siRNA developed normally to the blastocyst stage.
25637286 0.98 Lysosomal Associated Membrane Protein type-2 (LAMP-2) is a heavily glycosylated protein that, along with LAMP-1, constitutes the majority of all membrane proteins in the lysosome.
0.98 LAMP-2, most likely in concert with LAMP-1, has been proposed to contribute to the maturation of autophagic vacuoles and phagosomes by promoting vesicular fusion events along microtubules and is also involved in endosomal/lysosomal cholesterol trafficking.
0.97 LAMP-1/LAMP-2-double-deficient fibroblasts suggest a distinct role of LAMP-2 but not LAMP-1 in cholesterol metabolism.
0.97 LAMP-2A levels but led to a general increase in lysosomal membrane protein expression namely LAMP-2B, LAMP-1 and LIMP-2.
0.95 LAMP-2A but also LAMP-1 expression was reported after prolonged starvation.
0.92 LAMP-2A, LAMP-2B, LAMP-1 and LIMP-2 via immunoblotting and qRT-PCR analysis.
0.92 LAMP-2B (Figure 7c) as well as two other lysosomal membrane proteins investigated namely LAMP-1 (Figure 7d/e) and LIMP-2 (Figure 7f/g).
0.89 LAMP-2A levels in N2a cells, this is not unique to this isoform since a comparable upregulation was also evident for LAMP-2B, LAMP-1 and LIMP-2.
0.78 LAMP-2 in N2a cells using shRNA directed against LAMP-2 mRNA significantly reduced protein levels of LAMP-2 (Figure 6e) but not LAMP-1 (Additional file 6b) and did not alter steady-state levels of MEF2D (Figure 6f), GAPDH (Figure 6g) or Htt (Figure 6h).
0.67 LAMP-1 in LAMP-2-deficient brain as illustrated by LAMP-1 immunoblot (Additional file 2b) and immunohistological (Additional file 2c) analysis.
25586965 0.98 LAMP2A was observed adjacent ( 20-50 nm distance, STORM lateral resolution limit when detecting endogenous proteins using antibodies) to LAMP1 in wild-type cells, suggesting that they are distributed at common lysosomal microdomains.
0.98 LAMP2A is either present at non-lysosomal structures (Fig5A) or if at the lysosomal membrane, LAMP2A and LAMP1 appear partially segregated in distinct microdomains (Fig5B).
0.98 LAMP2B colocalizes with LAMP1 at lysosomes in both Ctns-/- and WT cells (Fig5C).
0.98 LAMP2A at the lysosomal membrane as detected by its colocalization with the lysosomal marker LAMP1.
0.96 LAMP2-positive but LAMP1-negative structures observed only in Ctns-/- cells further supports that LAMP2A but not LAMP2B is mislocalized in these cells.
0.90 LAMP2A localized to LAMP1-positive structures resembling lysosomes (Fig 5A, white arrows), LAMP2A localized at puncta distributed in close proximity to but different from LAMP1-positive lysosomes in Ctns-/- cells (Fig5A, arrowheads) with just a few lysosomes containing LAMP2A being identified (Fig5A, red arrow).
0.90 LAMP2A localization maintained a reticular distribution similar to that observed in untreated Ctns-/- cells (Fig10B, red panels), and colocalization of LAMP2A with the lysosomal marker LAMP1 was not restored in cysteamine-treated cells (Fig10B (merge) and C).
0.64 LAMP2A was mostly distributed at LAMP1-negative structures or in the proximity (distance >50 nm) but not adjacent to LAMP1, differently from the distribution observed for wild-type cells.
0.63 LAMP2 with LAMP1 in WT cells and partial localization of LAMP2 with LAMP1 in Ctns-/- cells.
23044750 0.98 Lamp1 and Cd63 protein in ameloblast cells including the plasma membrane at the apical pole, and Lamp1, Lamp2 and Cd63 have been shown to directly interact with known EMPs in vitro.
0.98 Lamp1, Lamp2 and Cd63 have also been described as membrane-bound protein receptors initiating AP endocytotic activities by direct interaction with all four AP complexes.
0.97 Lamp1, Lamp2 and Cd63 from the cell membrane to the lysosome, is initiated by a direct protein-protein interaction between a lysosomal targeting motif (GYXXO; where X is any amino acid and O is a bulky hydrophobic amino acid) located at the cytoplasmically located C'-terminus of all three LAMPs, and the mu/mu subunit of either AP-1, AP-2, AP-3 or AP-4 (Ap1m1, Ap2m1, Ap3m1 or Ap4m1 respectively).
0.97 Lamp1, Lamp2 and Cd63 through a well defined, externalized 20 amino-acid domain/motif, with high but not absolute homology, common to all three LAMP proteins.
0.97 Lamp1, Lamp2 and Cd63 may all share a common activity thus mutating or eliminating the function of one or two of these proteins may have little impact on endocytosis during enamel maturation.
0.96 Lamp1, Lamp2 and Cd63 in amelogenesis.
0.91 Lamp1-null mice, Lamp2 is up-regulated and appears to compensate for the loss of Lamp1 function, while Lamp2-null mice are more critically impacted.
0.66 Lamp1, Lamp2 and Tpp1 ranging from ~1.4 fold (for Ap2s1) to ~3.1 fold (for Cltc) (Figure 7).
15051738 0.98 LAMP-1 and LAMP-2 are concentrated in the AP-3-positive membrane domains.
0.98 LAMP-1 and LAMP-2 were concentrated in the AP-3-positive buds and associated vesicular profiles (Table I).
0.98 LAMP-1 and CD63 recycle from endosomes to the plasma membrane, as was previously suggested for LAMP-2 and avian LAMP-1.
0.97 LAMP-1 and LAMP-2 (but not CI-MPR and ASGPR) within the tubular endosomal compartment.
0.96 LAMP-1 and LAMP-2 are concentrated in AP-3 buds on endosomal tubules
0.95 LAMP-1 and LAMP-2 are concentrated in AP-3 buds over the attached AP-3-negative membrane tubules, by factors of 8.5 and 3.6, respectively.
0.89 LAMP-1 and LAMP-2 and displayed distinct, small-sized AP-1-positive buds.
25797357 0.98 lysosome associated membrane protein (LAMP)-1, LAMP-2 and the a2 isoform of V-ATPase (a2V, an enzyme involved in lysosome acidification).
0.98 LAMP-1 and LAMP-2 protein in uterus and placenta compared with respective control tissues as observed by immunofluorescence and western blot (Fig. 4).
0.97 lysosome associated membrane protein (LAMP)-1 and LAMP-2, in part through diminished function of a2V; (3) Altered autophagy in both uterus and placenta and in the macrophages resident in these tissues may play a role in enhancing inflammatory processes in IPTL (Fig. 8).
0.97 LAMP-1 and LAMP-2 is decreased in both inflammation-induced and non-inflammation-induced preterm labor.
0.95 LAMP-1 and LAMP-2 protein were diminished in preterm labor induced by both inflammatory and non-inflammatory stimuli.
0.81 lysosome associated membrane protein (LAMP)-1 and LAMP-2 and the lysosomal enzyme a2V in uterus, placenta and macrophages.
0.67 LAMP-1 and LAMP-2 knockout mice are viable and fertile, however, an embryonic lethal phenotype occurs in LAMP-1 and LAMP-2 double knockout mice.
29343516 0.98 LAMP2 and LAMP1 immunostaining in EpH4 cells clearly showed enhanced lysosomal biogenesis in response to OSM, with lysosomes becoming increasingly perinuclear in distribution (Fig. 5C).
0.98 LAMP1 and LAMP2 that occurs in response to OSM treatment (Figs. 3E and 5D), suggesting a role for this post-translation modification of LAMP1 and LAMP2 in lysosome function.
0.98 LAMP1, and LAMP2.
0.98 LAMP1 and LAMP2 in response to OSM treatment in EpH4 cells (Fig. 5D), mimicking that observed during involution of the mouse mammary gland.
0.97 LAMP1, LAMP2, LIMP2, and CD63/LIMP1, revealed that deglycosylation increased the number of unique peptide sequences identified for these proteins, vastly improving their representation and identification by LC-MS/MS (Table S13).
0.90 LAMP1 and LAMP2, which constitute over 50% of the lysosomal membrane proteins, is less clear.
0.57 LAMP1, LAMP2, CD63/LIMP1, and LIMP2 were detected, they were relatively under-represented.
31999726 0.98 LAMP1 (and LAMP2) may be an important factor in the overall mechanism of cholesterol efflux from the lysosome.
0.98 Lamp1, but not Lamp2, is significantly upregulated (Log2Fold, 1.08; Padj 4.66E-15), in activated microglia from Npc1-/- mice.
0.97 LAMP1 and LAMP2 are heavily glycosylated on their luminal domains; predominantly composed of N-linked glycans, N-acetylglucosamine (GlcNAc) linked to asparagine residues.
0.96 LAMP1 and LAMP2, which are similar in size and structure, together make up about 50% of all lysosomal membrane proteins, however, their exact role in the function of the lysosome is complex.
0.96 Lamp2, but not Lamp1, further suggesting a divergence in function of these two similar proteins.
0.89 LAMP1 and LAMP2 in the cerebellum of Npc1-/- mice during disease progression.
0.64 Lamp1-/-/Lamp2-/y mice are embryonically lethal.
24789143 0.98 LAMP-1- and LAMP-2-positive vesicles, suggesting that CAXIII localizes within lysosomes.
0.97 LAMP-1, LAMP-2 and CA XIII staining of intracytoplasmic vesicles overlaps, suggesting that CA XIII may be a lysosomal enzyme.
0.96 LAMP-1, LAMP-2 and CA XIII in developing teeth disclosed similar patterns of intracellular vesicular distribution in tooth-forming cells.
0.95 LAMP-1, LAMP-2 and CA XIII immunostaining displayed similar patterns of distribution in developing teeth (Fig. 6, Fig. S2, Fig. S4 & data not shown), which at postnatal stages visualized vesicles with different sizes, some of which were quite large, especially in maturation-stage ameloblasts (Fig. S4).
0.89 LAMP-1 and LAMP-2, well-known integral membrane proteins of lysosomes.
0.88 LAMP-1 and LAMP-2 staining was similar to previous findings of LAMP-1 expression in the ameloblastic lineage of mouse teeth.
26500823 0.98 LAMP1 and LAMP2 in quinacrine-treated fibroblasts (48 h, immunoblots), a response that follows the nuclear translocation of the lysosomal genesis transcription factor TFEB and upregulation of LAMP1 and -2 mRNAs (24 h).
0.98 LAMP1 and LAMP2, a 48-hr quinacrine treatment (>=1 or 0.25 microM, respectively) significantly increased the mass of late endosomal/lysosomal compartments where these proteins are found (Fig. 7).
0.98 LAMP1, LAMP2, V-ATPase subunits and the expression of hundreds of other genes encoding proteins present in lysosomes.
0.97 LAMP1 and LAMP2 in cells treated with some cationic drugs, imatinib or chloroquine.
0.97 LAMP1 and LAMP2 mRNAs in fibroblasts, the drug having a significant effect at 2.5 microM but not 250 nM (Fig. 8A).
0.69 LAMP1 and LAMP2.
20388541 0.98 Lamp-1 and Lamp-2 and proteolytic enzymes such as the cathepsins.
0.98 Lamp-1 and Lamp-2 are over-sialylated in the absence of Neu1 activity.
0.97 Lamp-1, Lamp-2a and b, and cathepsin B in total muscle lysates from Neu1-/- mice (Fig. 9B).
0.97 Lamp-1, Lamp-2a, Lamp-2b, and cathepsin B protein expression was increased and showed different mobility patterns on SDS-PAGE gel of Neu1-/- gastrocnemius muscle lysates.
0.92 Lamp-1, Lamp-2, and cathepsin B protein expression in the infiltrated areas and within the infiltrated muscle fibers (white arrows) of Neu1-/- muscle.
26095880 0.98 Lamp1 and Lamp2) that are somewhat redundant, but expression of at least one is crucial for the final lysosomal maturation step.
0.97 Lamp1 and Lamp2 which localizes to the ingested, dead cells.
0.97 Lamp1 and Lamp2 expression show that both proteins are expressed at high levels in the cell cultures at all time points (Fig. 2A and B).
0.96 Lamp1 and Lamp2 are highly expressed throughout the experiment.
0.71 Lamp1 and Lamp2 are located around the dead cells in astrocytes (blue arrow heads) and are especially visible at 3+6 d.
26883946 0.98 Lamp1 and Lamp2a.
0.98 Lamp1 and Lamp2a, yet these proteins are not detected in MV from untreated cells or exosomes (Fig. 4B).
0.97 Lamp1 and Lamp2a are involved in mineralization.
0.93 Lamp1 and Lamp2a were only detected in MV secreted by cells stimulated with osteogenic factors.
0.87 Lamp1 and Lamp2a protein levels in unstimulated and stimulated cells, thus osteogenic factors affect only the subcellular distribution of these proteins and not expression.
29463847 0.98 LAMP-1 upregulation can not compensate for the defective LAMP-2 in VMSC are more susceptible to injury leading to vasculopathy.
0.97 LAMP-1 might occur in some tissues in a LAMP-2-deficient state.
0.92 LAMP-1 vs LAMP-2 as well as lysosome enzyme contents (i.e., Cathepsin D, etc.) may differ among tissues as well as individuals.
0.88 Lamp2 dosage is reduced by 50% and could become overt under some circumstances: (1) the presence of skewed X-chromosome inactivation, (2) coexisting environmental risk factors and/or changes in female hormones, or (3) tissue-specific LAMP-1 vs LAMP-2 compensation.
0.78 LAMP-1 vs LAMP-2, and/or lysosomal enzyme contents.
9166415 0.98 LAMP-1/ LAMP-2 chimeras show differences in steady state distribution that are attributable to amino acid differences in the cytosolic tail domains of the splice variants of LAMP-2.
0.95 LAMP-1/LAMP-2 chimeras at the cell surface are different and that these differences are correlated with differences in the LAMP-2 COOH-terminal targeting signals.
0.94 LAMP-1/LAMP-2a or LAMP-1/LAMP-2b showed much higher levels of surface expression, suggesting that the steady state distribution may be influenced by the different cytosolic tail sequences.
0.90 LAMP-1/LAMP-2 chimeras was capable of being targeted to lysosomes, differences in their levels of expression at the cell surface were readily apparent in direct immunofluorescent labeling of intact cells (Fig. 1).
19523115 0.98 LAMP1 and LAMP2 in spermatocytes and spermatids.
0.98 LAMP1 and LAMP2 both contain tyrosine based signals that bind to the mu subunits of AP adaptor complexes [45].
0.98 LAMP1 and LAMP2.
0.68 LAMP1 and LAMP2.
22592897 0.98 LAMP2 abundance (Figure 4C, D; assessed with a monoclonal antibody directed to the matrix side of LAMP2 protein, which detects all isoforms), without affecting LAMP1 levels except with longer duration (72 hours) of injury (Figure 4D).
0.95 LAMP2 declined by 41% and LAMP1 declined by 44% in IR-treated GFPL-LC3 transgenic hearts (Figure 1D, G, H); and only the decline in LAMP1, which closely tracks lysosome numbers was prevented by chloroquine pretreatment, suggesting that the decline in LAMP2 was independent of lysosome pH and not related to lysosome consumption in IR-induced autophagy.
0.94 LAMP1 deficiency in mice is of no serious consequence; LAMP2 is a critical determinant of autophagosome-lysosome fusion, and mutations causing LAMP2 deficiency result in Danon disease which is characterized by autophagosome accumulation in multiple tissues including the myocardium, and cardiomyopathy.
0.56 LAMP1 and LAMP2.
24824158 0.98 LAMP1/LAMP2 knockout fibroblasts, we observed that the presence of these lysosomal components on amastigotes increases interleukin 10 production.
0.98 LAMP1/LAMP2-rich host membrane caps, macrophages produce higher amounts of IL-10 when compared with the interaction with amastigotes devoid of LAMP (Fig. 5D).
0.91 LAMP1/LAMP2 double-knockout MEF did not display these lysosomal components on their surfaces but conserved host cell debris on posterior pole (Fig. 5B).
0.88 LAMP1/LAMP2 phagolysosomal proteins, and the amastigote-containing extrusions displayed a smooth surface in contrast to the usually ruffled macrophage surface and with no apparent host membrane pores (Fig. 4D, insets).
24980141 0.98 lysosome-associated membrane protein-1 (LAMP1) and LAMP2, were abnormally accumulated in RagA/B cKO hearts (Figure 5A-B).
0.98 LAMP1 and LAMP2 were increased in RagA/B cKO hearts (Figure 5A).
0.96 LAMP1 and LAMP2 proteins present higher molecular weights in RagA/B KO MEFs compared with control MEFs.
0.95 LAMP1 and LAMP2 were about 2 fold more abundant in the RagA/B KO MEFs than the control MEFs.
30983487 0.98 LAMP1 and LAMP2A, without observable differences in cell morphology and viability compared with WT MEFs (Figure 3(a,b)).
0.98 LAMP2A (N = 11; p < 0.05) and HSPA8 (N = 11; p < 0.01) relative to LAMP1 (Figure 4(a)(i) and (ii)), indicating accumulation of LAMP2A- and HSPA8-containing complexes on the lysosomal membrane.
0.95 LAMP1 which is a transmembrane marker protein expressed in all lysosomes, only those lysosomes which contain LAMP2A and HSPA8 are CMA-active.
0.95 LAMP2A and HSPA8 levels relative to LAMP1 reflect the number of CMA-active lysosomes.
19857571 0.98 Lamp-1 (2.98 fold) and Lamp-2 (3.19 fold) (Fig. 7, left panel).
0.97 Lamp-1 (A, B) and Lamp-2 (C, D) mainly in the marginal cells of the stria vascularis.
0.96 Lamp-1, Lamp2, and other unidentified targets of Neu1 would neutralize and potentially exceed the increased positive charge of protons by V-ATPase and convergently reduce the EP in Neu1-/- cochlea.
23219390 0.98 LAMP1 and LAMP2 in pDCs.
0.97 LAMP1 and LAMP2 recruitment to the phagosome and this abrogated IRF7 activation.
0.96 LAMP1 (Figure 7E), LAMP2 (Figure 7F), or acidify (Figure S5B) in pDCs.
27424887 0.98 LAMP1 and LAMP2.
0.98 LAMP1 and LAMP2 at the cell surface in cells treated with either LRRK2 siRNA or AP3B1 siRNA, compared with control siRNA-treated cells (Fig. 3A,B, Supplementary Fig. S3A), consistent with defective trafficking of LMP proteins.
0.98 LAMP1 and LAMP2, in mammalian cells, and (iii) enlargement of secondary lysosomes in renal proximal tubules of mice.
30240610 0.98 LAMPI, LAMPII, V-ATPase, and chloride channels, which are found normally in late endocytic compartments of other cell types, and Rab7, a small GTPase, which normally regulates membrane traffic from early to late endocytic compartments.
0.98 LAMP1 and LAMPII are more enriched at the ruffled border and early endosomes after AP-3 depletion.
0.97 LAMPI and LAMPII (a 4- and 2-fold increase, respectively) at the ruffled border (Figures 5H and S4).
18606142 0.98 LAMP-2, LAMP-1 was thought to merely maintain membrane integrity against the harsh lysosomal environment, owing to its abundant sugar content.
0.98 Lamp-1 and Lamp-2 were shown to be involved in the movement of lysosomes along microtubules, because double-deficient cells have impaired organelle motility and a defect in the fusion of phagosomes with lysosomes.
27854220 0.98 LAMP2 and/or LAMP1 seem to be required for the efficient recruitment of Rab7 and the fusion of (auto)phagosomes with lysosomes in macrophages, hepatocytes, and mouse embryonic fibroblasts (MEFs).
0.97 Lamp1/2-KO MEFs was unaffected, suggesting that the role and importance of LAMP2 differ between cell types.
29872438 0.98 Lamp2 but not Lamp1 was increased after experimental stroke (Figure 4A) and analysis of mRNA levels by RT-qPCR confirmed significant upregulation of Lamp2 2 days after experimental stroke in comparison to sham surgery (Figure 4B).
0.97 lysosomal-associated membrane protein 2 (Lamp2) expression is upregulated after stroke, whereas Lamp1 remains relatively unchanged (sham n = 2, 1 day and 2 days n = 3, 5 days n = 4).
29880899 0.98 Lysosome associated membrane protein 1 (LAMP1) and LAMP2 comprise 50% of all lysosomal membrane proteins, and maintain lysosomal membrane integrity.
0.95 LAMP1 and LAMP2-deficient cells, but the underlying mechanism still remains unclear.
31661432 0.98 LAMP1 or LAMP2, respectively, indicating that it is a resident lysosomal protein.
0.97 LAMP1 or LAMP2 are known since decades, there is still a major gap of knowledge about polytopic transporter proteins, mediating the transport of metabolites between the lysosomal lumen and the cytosol, but also the import of metabolites from the cytosol to lysosomes.
19216919 0.98 LAMP-1 and LAMP-2 are transmembrane proteins localized specifically to lysosomal membranes.
20709007 0.98 CD107a and CD107b are two intracellular proteins that are normally found in lysosome, but are also a structural component of cytotoxic granules.
26649145 0.98 LAMP-1 deficiency can induce overexpression of murine LAMP-2a, while our study showed that inhibition of HDAC6 hindered the increase of LAMP-2a; as a consequence, the number of LAMP-1 was compensatory increased to resist HI-induced oxidative stress toxicity (Figure 5(c)).
30154423 0.98 LAMP1, and LAMP2, which are both the TFEB target genes (Fig. 4a, b, d).
31699817 0.98 LAMP1/2-double-deficient MEFs revealed disturbed cholesterol trafficking in LAMP2-deficient cells that depends on the domain common to all LAMP2 isoforms.
31578378 0.97 LAMP1-, LAMP2-, CTSD- and CTSZ-immunoreactivity was particularly pronounced in microglia/macrophages (Supplementary Fig. 3a-f'').
0.97 LAMP1, LAMP2, CTSD and CTSZ in mutant retinas at P240 when compared to age-matched wild-type retinas (Fig. 5).
0.97 LAMP1, LAMP2, CTSZ and CTSD was another early pathological feature of mutant retinas.
0.97 LAMP1, LAMP2 and CTSZ were increased 1.3-, 2.6- and 2.8-fold, respectively when compared with control retinas.
0.96 LAMP1, LAMP2, CTSD and CTSZ were slightly elevated in 45-day-old mutant animals (b,f,j,n, respectively) when compared to age-matched wild-type mice (a,e,i,m, respectively).
0.96 lysosomal-associated membrane protein 1 (LAMP1), lysosomal-associated membrane protein 2 (LAMP2) and the soluble lysosomal enzymes cathepsin D (CTSD) and cathepsin X/Z/P (CTSZ) in mutant retinas at P45 (Fig. 4b,f,j,n) when compared to age-matched wild-type retinas (Fig. 4a,e,i,m).
0.96 LAMP1, LAMP2, CTSD and CTSZ in 240-day-old Ppt1 ko retinas when compared to age-matched wild-type retinas (a).
0.94 LAMP1 (p < 0.05; Student's t-test), 2.6-fold for LAMP2 (p < 0.05), 2.1-fold for the CTSD precursor protein (p < 0.01), 3.9-fold for mature CTSD (p < 0.01), and 2.8-fold for CTSZ (p < 0.05) when compared to age-matched wild-type retinas (Fig. 5b-f).
0.91 LAMP1-, LAMP2-, CTSD- and CTSZ-immunoreactivity was observed in 240-day-old Ppt1 ko retinas (d,h,l,p, respectively).
0.88 LAMP1 (b), LAMP2 (c), the precursor (d) and mature (e) form of CTSD, and CTSZ (f).
0.59 LAMP1 and LAMP2 in 69.9 +- 1.7%, 82.4 +- 2.8%, 75.1 +- 2.3% and 67.9 +- 4.5% respectively of IBA1-positive cells (Supplementary Fig. 3g).
26693174 0.97 LAMP-1 and LAMP-2 are heavily glycosylated proteins and major constituents of the glycoconjugate coat on the inside of the lysosomal membrane.
0.96 LAMP-1 and LAMP-2 proteins.
0.95 LAMP-1 and LAMP-2 are not due to their deglycosylation.
0.93 LAMP-1 and LAMP-2 (Figure 5A and B; and data not shown).
0.92 LAMP-1 and LAMP-2 were much greater with C-terminal Abs than with Abs against LAMP luminal part (Figure 3A-C).
0.92 LAMP-1 do not develop overt pathologic changes, likely because of compensatory LAMP-2 upregulation.
0.74 LAMP-1 and LAMP-2.
20920792 0.97 LAMP-1 and LAMP-2 after snapin deletion were significantly reduced to 55.8+-3.0% and 27.2+-8.6%, respectively, relative to (+/+) control (Figure 5E), indicating reduced association of the dynein motor complex with late endocytic organelles in snapin-deficient neurons.
0.95 LAMP-1 and LAMP-2 (in boxes) were associated with dynein-bound organelles from snapin (-/-) mice.
0.94 LAMP-1 and LAMP-2 in snapin (-/-) cortical neurons.
0.93 LAMP-1 and LAMP-2 were consistently observed in snapin (-/-) neurons, while expression of other organelle markers including EEA1 (early endosomes), p115 (Golgi), and Calnexin (ER) exhibited no detectable change between snapin (+/+) and (-/-) neurons.
21750540 0.97 LAMP-1 and LAMP-2 supported the association of the CMA reporter with lysosomes (Fig. 3b, c).
0.81 LAMP-1 and LAMP-2, this is likely because these LAMPs are also present in endosomes (where CMA does not occur), and that not all cellular lysosomes are capable to perform CMA (although they all contain LAMPs), The unusually low level of colocalization of KFERQ-PS-CFP2 with LAMP-2A-positive structures could be explained by the same reasons as above, but in addition to the antibody used to differentiate the LAMP-2A variant from the other LAMP-2 proteins binds the same region as the CMA substrates (the 12 amino acids of the cytosolic tail).
27628032 0.97 LAMP-2-deficient and LAMP-1/2-double-deficient mouse embryonic fibroblasts (MEFs) with a tandem fluorescent-tagged LC3 we observed a failure of fusion between the autophagosomes and the lysosomes that could be rescued by complementation with LAMP-2A.
0.93 LAMP-2, doubly deficient in LAMP-1 and LAMP-2, and wild-type littermates, and analyzed the contribution of LAMP-2 to autophagosome-lysosome fusion.
28456975 0.97 LAMP-1 and LAMP-2.
0.97 LAMP-1 and LAMP-2, are additionally modified by O-linked glycans that are added to selected serine or threonine residues.
29158485 0.97 LAMP1 and LAMP2 proteins were decreased in the absence of DPPA3 (Fig. 4d; Supplementary Fig. 5a, b).
0.92 LAMP1 and LAMP2 proteins are decreased in Dppa3KO eggs (Fig. 4d; Supplementary Fig. 5a, b), it was of interest to determine if their ectopic expression could rescue the null phenotype and promote development to blastocysts.
31527516 0.97 LAMP1 and LAMP2 are decreased in PD compared with controls.
0.95 lysosome-associated membrane protein 1 (LAMP1) and LAMP2, which are responsible for protecting the lysosomal membranes from digesting themselves.
24337808 0.97 LAMP1 and LAMP2, and the role that PPCA plays in CMA by binding and targeting the latter protein, we hypothesize that PPCA may also be required for binding to LAMP1, thereby giving NEU1 the opportunity to desialylate this protein.
26183450 0.97 LAMP2+ reticular structures (Fig7B), but was not associated with LAMP1 or other organelle markers (Supplementary Fig S10), indicating that un-esterified cholesterol accumulation is localised at LAMP2+LAMP1- structures that are distinct from LAMP1+ lysosomes.
19566896 0.96 LAMP-1 (Figure 5H) and LAMP-2 (not shown) were found in all urothelial layers, with somewhat higher levels of expression in the lower cells.
0.94 LAMP-1, LAMP-2, uroplakins and Rab27b
22171050 0.96 LAMP-2A, but not of other lysosomal proteins (LAMP-1 shown here) were markedly higher in 111QHtt MEFs than in 18QHtt MEFs both when maintained in the presence of serum or after 24h serum removal (Fig. 4A).
0.82 LAMP-2A content between control and HD cells were even more pronounced (30-40% increase) when isolated mouse liver lysosomes were compared, whereas levels of other lysosomal membrane proteins (LAMP-1 shown here) remain unchanged (Fig. 4B).
23840635 0.96 Lamp-1, Lamp-2 and CD63.
24932692 0.96 LAMP-1 and LAMP-2.
27231233 0.96 LAMP1 colocalized well with LAMP2 (LAMP1 overlap with LAMP2 = 71.4 +- 6.2%, p < 0.0001), but not melanin or TYRP1 (LAMP1 overlap with melanin = 12.1 +- 2.1%, p > 0.5), indicating that not all endolysosomal proteins localize to melanosomes when overexpressed in pigment cells (Fig. 3b,c, Supplementary Fig. S2).
30048497 0.96 Lamp-2(A) expression in these cell lines has been validated by using Lamp-2 and Lamp-2A specific antibodies, Disruption of Lamp-2 expression does not affect Lamp-1 protein expression, another abundant integral membrane lysosomal protein (see S1 Fig).
31920513 0.95 LAMP1 or LAMP2 immunohistochemical staining was elevated in 6-9-month-old LRRK2 KO or KD mice, respectively.
0.93 LAMP1 and LAMP2A levels markedly decrease over the years resulting in a defective CMA activity.
0.88 LAMP1 and LAMP2 as well as cathepsin B were found to be elevated already from the first month of age (significant elevation of cathepsin D was observed at both 7 and 20 months).
0.67 LAMP1 and LAMP2 was noted, which was overall interpreted as an impairment of lysosomal function.
22426402 0.95 Lamp-1/Lamp-2 are embryonic lethal, while mice with a knockout of only one of these two proteins are viable, suggesting that there may be an overlapping function of these two proteins.
0.77 Lamp-1 is also structurally homologous to Lamp-2a and contains a C-terminal cytosolic tail with the amino acid sequence of 397KRSH400, conserving three of the four residues from Lamp-2a's 406KRHH409.
29203562 0.95 LAMP1 and LAMP2 protein levels in the Myh6-sTNF mouse hearts (Figure 5B).
0.66 lamp1 mRNA, and a non-significant increase in lamp2 mRNA levels.
30237523 0.95 LAMP-2A-labeled structures were indeed more abundant in Vps34Delta/Delta PTCs at P14 compared to WT controls and LAMP-2A extensively co-localized with LAMP-1.
0.94 LAMP-2A labels similar structures as LAMP-1, polarized in the subapical cytoplasm, and likewise segregated from megalin.
22740045 0.95 LAMP-1, two anti-LAMP-2, and anti-Cathepsin D) labeled LysoTracker-positive structures in the mouse cell lines (Fig. 12B,C).
28586379 0.95 LAMP-2 deficient fibroblasts present an accumulation of autophagic vacuoles no deficiency in protein degradation was observed, indicating that lysosomal enzyme content seemed to be unaffected by LAMP-1 or 2 deficiency.
28740222 0.95 LAMP-1) (Fig. 4A) and greater transcript levels of LAMP-1 and LAMP-2 (Fig. 4B) than found in cells transduced with the empty vector.
25263126 0.93 LAMP-1), lysosomal proteases and glycosidases (cathepsin D and beta-hexosaminidase), as well as lysosomal stability were not decreased in LAMP-2A-deficient T cells (Supplementary Fig.4a-c)
29695488 0.92 LAMP1/LAMP2 (Fig. 1 E) or cathepsin D/LAMP1 (Fig. 1 J) was robustly reduced in LAMP1- or cathepsin D-depleted neurons, respectively.
0.90 LAMP2 and cathepsin B were only partially colocalized, with 44.90 +- 3.28% (MCC based) or 41.55 +- 3.44% (particle based) of LAMP1-labeled organelles colocalizing with cathepsin B in the axons, respectively (Fig. 6, A and B).
0.63 LAMP2 shares a similar distribution pattern as LAMP1 by coimmunostaining adult DRG neurons with antibodies against LAMP2, cathepsin B, and betaIII tubulin at DIV3.
27362797 0.92 LAMP2 colocalization in cones was similar between Cre- and Cre+ littermates (Figure 6b), with a less strong increase in lysosomes per cone when compared with loss of Tsc1, as assessed by LAMP1-positive punctae (Figure 6c).
26157167 0.91 LAMP-1 or LAMP-2 immunogold-labeled sections of cells preloaded with 5-nm BSA-gold confirmed that the relative volume of LAMP-1- or LAMP-2-positive or BSA-gold-preloaded compartments increased approximately twofold (Figure 4C).
28266597 0.91 LAMP1, LAMP2 and Rab7a, markers for endosomes and lysosomes, but showed much less colocalization with Calnexin, an ER marker (Fig. 5b,c).
31225467 0.89 Lamp2 (or Lamp1), because lysosomal fluorescence is usually seen as small dots that become large puncta by the induction of autophagy (owing to the fusion of lysosomes with autophagic vacuoles).
0.76 Lamp2 (or Lamp1) puncta to autolysosomes was previously shown by correlative light electron microscopy (CLEM) analysis, and was also confirmed in the present study (see Fig. 3D).
26118642 0.82 LAMP-2B, LAMP1 or lysosomal hsp90, reinforcing the selective nature of its effect on LAMP-2A (Fig. S7A).
22809326 0.72 LAMP-1 and LAMP-2 gene knockout mice and LAMP-1/2-negative cell lines.



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