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LAMP1 is involved in the TNM (show ODZ1 Proteins) stages and histological differentiation of the esophageal squamous cell carcinoma
LAMP1 has a role in fratricide amongst T cell receptor transgenic CD8 (show CD8A Proteins)+ T cells directed against tumor-associated antigens
Impaired autophagic pathways were further shown by analyzing late autophagic vesicles; immunostaining with lysosome-associated membrane protein 1 (LAMP-1) antibody revealed enlarged and annular LAMP-1-positive organelles in AMD (show AMD1 Proteins) retinal pigment epithelium (RPE (show RPE Proteins))as opposed to smaller discrete puncta observed in normal RPE (show RPE Proteins)
The authors show here that human LAMP1 and LAMP2 (show LAMP2 Proteins) bind cholesterol in a manner that buries the cholesterol 3beta-hydroxyl group; they also bind tightly to NPC1 (show NPC1 Proteins) and NPC2 (show NPC2 Proteins) proteins that export cholesterol from lysosomes.
downregulation of FUT1 (show FUT1 Proteins), which leads to the perinuclear localization of LAMP-1 and 2, is correlated with increased rate of autophagic flux by decreasing mTOR (show FRAP1 Proteins) signaling and increasing autolysosome formation.
the assembly modes of LAMP-1 and LAMP-2 (show LAMP2 Proteins) are different, which may underlie their distinct functions
Overexpression of LAMP1 was observed in prostate cancer (PCa (show FLVCR1 Proteins)) and castration-resistant prostate cancer clinical specimens. Moreover, downstream pathways were identified using si-LAMP1-transfected cells. The discovery of tumor-suppressive miR320a-mediated pathways may provide important insights into the potential mechanisms of PCa (show FLVCR1 Proteins) metastasis.
The data implied that high LAMP1 expression is associated with unfavourable prognosis in laryngeal squamous cell carcinoma patients, and LAMP1 may be identified as a novel prognostic biomarker
The data support a viral entry mechanism dependent on binding to the lysosome-resident receptor LAMP1 and further dissociation of the membrane-distal GP1 subunits.
A unique triad of histidines of Lassa Virus GP1 (show GTPBP1 Proteins) forms a binding site for host LAMP1.
The results presented here show the major role of LAMP-2 (show LAMP2 Proteins) in caveolin traffic and membrane repair and consequently in T. cruzi invasion.
Here, we identify lamellar inclusions as the subcellular site of lipid accumulation in neurons, we uncover a vicious cycle of cholesterol synthesis and accretion, which may cause gradual neurodegeneration, and we reveal how beta-cyclodextrin, a potential therapeutic drug, reverts these changes. Our study provides new mechanistic insight in NPC (show NPC1 Proteins) disease and uncovers new targets for therapeutic approaches.
we demonstrate that galectin-3 (show LGALS3 Proteins) induces MMP9 (show MMP9 Proteins) expression via p38 MAP-kinase (show MAPK14 Proteins) pathway. LAMP1 was demonstrated to serve as one of the key mediators of galectin-3 (show LGALS3 Proteins)-induced MMP9 (show MMP9 Proteins) expression via p38 MAPK (show MAPK14 Proteins) pathway
Although surface LAMP1 promotes interactions with organ ECM (show MMRN1 Proteins) and BM, carbohydrates on LAMP1 play a decisive role in dictating lung metastasis.
The results thus for the first time provide direct evidence that cell surface LAMP1 facilitates lung metastasis by providing ligands for galectin-3 (show LGALS3 Proteins) which has been shown to be expressed in highest amounts on lungs and constitutively on its vascular endothelium.
Caveolin-1 (show CAV1 Proteins) associated adenovirus entry into human corneal cells.
study has shown that Lassa virus entry requires a pH-regulated engagement of alpha-DG and LAMP1 both of which need to be glycosylated
CD107a/LAMP-1 has a role in the protection of NK cells from degranulation-associated suicide
LAMP proteins retain TAPL (show ABCB9 Proteins) on the limiting membrane of endosomes and prevent its sorting to intraluminal vesicles.
a novel mechanism showing how Salmonella acquires LAMP1 through a SipC-Syntaxin6-mediated interaction probably to stabilize their niche in macrophages
The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may also play a role in tumor cell metastasis.
CD107 antigen-like family member A
, lysosome-associated membrane glycoprotein 1
, lysosome-associated membrane protein 1
, 120 kDa lysosomal membrane glycoprotein
, LYSOSOME-ASSOCIATED MEMBRANE GLYCOPROTEIN 1 PRECURSOR (LAMP-1) (LGP-A) (LGP-120) (CD107A) (P2B)
, Lamp I
, lysosomal membrane glycoprotein 1
, lysosomal membrane glycoprotein A
, Lysosomal associated membrane protein 1 (120 kDa)
, lysosome membrane glycoprotein LEP100
, chromaffin granule-associated membrane glycoprotein IIA
, glycoprotein IIa
, Lysosomal membrane glycoprotein A
, Lysosome-associated membrane protein 1
, lysosomal-associated membrane protein 1 L homeolog