| The Deficiency of SCARB2/LIMP-2 Impairs Metabolism via Disrupted mTORC1-Dependent Mitochondrial OXPHOS. | The Deficiency of SCARB2/LIMP-2 Impairs Metabolism via Disrupted mTORC1-Dependent Mitochondrial OXPHOS.
Zou Y, Pei J, Wang Y, Chen Q, Sun M, Kang L, Zhang X, Zhang L, Gao X, Lin Z., Free PMC Article | 08/27/2022 |
| Mouse Scarb2 Modulates EV-A71 Pathogenicity in Neonatal Mice. | Mouse Scarb2 Modulates EV-A71 Pathogenicity in Neonatal Mice.
Miwatashi W, Ishida M, Takashino A, Kobayashi K, Yamaguchi M, Shitara H, Koike S., Free PMC Article | 08/27/2022 |
| New observations from this study include altered expression of Pcp2 and Limp2 in Npc1 mutant mice relative to control, with Pcp2 exhibiting multiple isoforms and specific to the cerebella. This study provides valuable insight into pathways altered in the late-stage pathophysiology of NPC1 | Quantitative, Label-Free Proteomics in the Symptomatic Niemann-Pick, Type C1 Mouse Model Using Standard Flow Liquid Chromatography and Thermal Focusing Electrospray Ionization.
Pergande MR, Nguyen TTA, Haney-Ball C, Davidson CD, Cologna SM. | 05/2/2020 |
| Study provides multiple lines of evidence that LIMP-2 participates in lipid transport from lysosomes by transporting cholesterol (and possibly also other lipid species) through its luminal cavity to the lysosomal membrane and later to lipid droplets. Data indicate that LIMP-2 operates in parallel with Niemann Pick (NPC)-proteins, mediating a slower mode of lysosomal cholesterol export. | Lysosomal integral membrane protein-2 (LIMP-2/SCARB2) is involved in lysosomal cholesterol export.
Heybrock S, Kanerva K, Meng Y, Ing C, Liang A, Xiong ZJ, Weng X, Ah Kim Y, Collins R, Trimble W, Pomès R, Privé GG, Annaert W, Schwake M, Heeren J, Lüllmann-Rauch R, Grinstein S, Ikonen E, Saftig P, Neculai D., Free PMC Article | 12/14/2019 |
| LIMP-2 facilitates transport of phospholipids into murine fibroblasts, with a strong substrate preference for phosphatidylserine. | Lysosomal integral membrane protein-2 as a phospholipid receptor revealed by biophysical and cellular studies.
Conrad KS, Cheng TW, Ysselstein D, Heybrock S, Hoth LR, Chrunyk BA, Am Ende CW, Krainc D, Schwake M, Saftig P, Liu S, Qiu X, Ehlers MD., Free PMC Article | 10/6/2018 |
| The findings identify SR-BII as a functional SAA receptor that mediates SAA uptake and contributes to its proinflammatory signaling via the MAPK-mediated signaling pathways. | Human SR-BII mediates SAA uptake and contributes to SAA pro-inflammatory signaling in vitro and in vivo.
Baranova IN, Souza ACP, Bocharov AV, Vishnyakova TG, Hu X, Vaisman BL, Amar MJ, Chen Z, Remaley AT, Patterson AP, Yuen PST, Star RA, Eggerman TL., Free PMC Article | 04/29/2017 |
| AP-3-dependent LB targeting is facilitated by protein/protein interaction between LIMP-2/SCARB2 and PRDX6 in vitro and in vivo | Impaired Lysosomal Integral Membrane Protein 2-dependent Peroxiredoxin 6 Delivery to Lamellar Bodies Accounts for Altered Alveolar Phospholipid Content in Adaptor Protein-3-deficient pearl Mice.
Kook S, Wang P, Young LR, Schwake M, Saftig P, Weng X, Meng Y, Neculai D, Marks MS, Gonzales L, Beers MF, Guttentag S., Free PMC Article | 10/8/2016 |
| Heterologous expression of the luminal domain of LIMP-2 in wild-type cells. | Mannose 6-phosphate-independent Lysosomal Sorting of LIMP-2.
Blanz J, Zunke F, Markmann S, Damme M, Braulke T, Saftig P, Schwake M. | 06/28/2016 |
| In LIMP-2-deficient brains a significant reduction in GC activity led to lipid storage, disturbed autophagic/lysosomal function, and alpha-synuclein accumulation. | LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance.
Rothaug M, Zunke F, Mazzulli JR, Schweizer M, Altmeppen H, Lüllmann-Rauch R, Kallemeijn WW, Gaspar P, Aerts JM, Glatzel M, Saftig P, Krainc D, Schwake M, Blanz J., Free PMC Article | 04/18/2015 |
| absence of Limp-2 reduces inflammation in experimental crescentic glomerulonephritis with decreased macrophage and T-cell infiltration in the kidney. | Absence of the lysosomal protein Limp-2 attenuates renal injury in crescentic glomerulonephritis.
Lee DH, Gan PY, Katerelos M, Fraser SA, Gleich K, Holdsworth SR, Power DA. | 01/10/2015 |
| Limp-2 deficiency leads to a minor increase in circulating renin. Limp-2, however, is not required for acute or chronic stimulation of renin release. | Expression of the transmembrane lysosomal protein SCARB2/Limp-2 in renin secretory granules controls renin release.
Lee D, Desmond MJ, Fraser SA, Katerelos M, Gleich K, Berkovic SF, Power DA. | 01/25/2014 |
| The SR-BII is involved in cholesterol ester uptake for steroidogenesis and spermatogenesis in the testis. | HSL-knockout mouse testis exhibits class B scavenger receptor upregulation and disrupted lipid raft microdomains.
Casado ME, Huerta L, Ortiz AI, Pérez-Crespo M, Gutiérrez-Adán A, Kraemer FB, Lasunción MÁ, Busto R, Martín-Hidalgo A., Free PMC Article | 04/27/2013 |
| The residues between 144 and 151 are critical for SCARB2 binding to VP1 of EV71 and seven residues from the human receptor could convert murine SCARB2, an otherwise inefficient receptor, to an efficient receptor for EV71 viral infection. | Molecular determinants of enterovirus 71 viral entry: cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2.
Chen P, Song Z, Qi Y, Feng X, Xu N, Sun Y, Wu X, Yao X, Mao Q, Li X, Dong W, Wan X, Huang N, Shen X, Liang Z, Li W., Free PMC Article | 04/28/2012 |
| The data suggest that tubular proteinuria in Limp-2(-/-) mice is due to failure of endosomes containing reabsorbed proteins to fuse with lysosomes in the proximal tubule of the kidney. Failure of proteolysis is a novel mechanism for tubular proteinuria. | Tubular proteinuria in mice and humans lacking the intrinsic lysosomal protein SCARB2/Limp-2.
Desmond MJ, Lee D, Fraser SA, Katerelos M, Gleich K, Martinello P, Li YQ, Thomas MC, Michelucci R, Cole AJ, Saftig P, Schwake M, Stapleton D, Berkovic SF, Power DA. | 08/6/2011 |
| The coiled-coil structure of LIMP-2 is required for its interaction with beta-glucocerebrosidase. | Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase.
Blanz J, Groth J, Zachos C, Wehling C, Saftig P, Schwake M. | 04/12/2010 |
| These data support a role for LIMP-2 as the mannose-6-phosphate-independent trafficking receptor for beta-glucocerebrosidase. | LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase.
Reczek D, Schwake M, Schröder J, Hughes H, Blanz J, Jin X, Brondyk W, Van Patten S, Edmunds T, Saftig P. | 01/21/2010 |
| Lysosomal integral membrane protein 2 is a novel component of the cardiac intercalated disc and vital for load-induced cardiac myocyte hypertrophy. | Lysosomal integral membrane protein 2 is a novel component of the cardiac intercalated disc and vital for load-induced cardiac myocyte hypertrophy.
Schroen B, Leenders JJ, van Erk A, Bertrand AT, van Loon M, van Leeuwen RE, Kubben N, Duisters RF, Schellings MW, Janssen BJ, Debets JJ, Schwake M, Høydal MA, Heymans S, Saftig P, Pinto YM., Free PMC Article | 01/21/2010 |
| CD36 is differentially expressed by CD8+ splenic dendritic cells but is not required for cross-presentation in vivo. | CD36 is differentially expressed by CD8+ splenic dendritic cells but is not required for cross-presentation in vivo.
Belz GT, Vremec D, Febbraio M, Corcoran L, Shortman K, Carbone FR, Heath WR. | 01/21/2010 |
| CD36 is not essential for MHC class I cross-presentation of cell-associated antigen by CD8 alpha+ dendritic cells. | CD36 or alphavbeta3 and alphavbeta5 integrins are not essential for MHC class I cross-presentation of cell-associated antigen by CD8 alpha+ murine dendritic cells.
Schulz O, Pennington DJ, Hodivala-Dilke K, Febbraio M, Reis e Sousa C. | 01/21/2010 |
| SR-A and CD36 are responsible for the preponderance of modified LDL uptake in macrophages and that other scavenger receptors do not compensate for their absence | Scavenger receptors class A-I/II and CD36 are the principal receptors responsible for the uptake of modified low density lipoprotein leading to lipid loading in macrophages.
Kunjathoor VV, Febbraio M, Podrez EA, Moore KJ, Andersson L, Koehn S, Rhee JS, Silverstein R, Hoff HF, Freeman MW. | 01/21/2010 |
| Peritoneal macrophages isolated from SR-BI/BII-knockout mice demonstrated a 30% decrease in bacterial uptake when compared with macrophages from normal mice. | CLA-1 and its splicing variant CLA-2 mediate bacterial adhesion and cytosolic bacterial invasion in mammalian cells.
Vishnyakova TG, Kurlander R, Bocharov AV, Baranova IN, Chen Z, Abu-Asab MS, Tsokos M, Malide D, Basso F, Remaley A, Csako G, Eggerman TL, Patterson AP., Free PMC Article | 01/21/2010 |
| LIMP-2/LGP85 deficiency causes ureteric pelvic junction obstruction, deafness and peripheral neuropathy in mice | LIMP-2/LGP85 deficiency causes ureteric pelvic junction obstruction, deafness and peripheral neuropathy in mice.
Gamp AC, Tanaka Y, Lüllmann-Rauch R, Wittke D, D'Hooge R, De Deyn PP, Moser T, Maier H, Hartmann D, Reiss K, Illert AL, von Figura K, Saftig P. | 01/21/2010 |
| Our findings suggest an important role for LIMP2 in the control of the localization and the level of apically expressed membrane proteins such as KCNQ1, KCNE1 and megalin in the stria vascularis. | Deafness in LIMP2-deficient mice due to early loss of the potassium channel KCNQ1/KCNE1 in marginal cells of the stria vascularis.
Knipper M, Claussen C, Rüttiger L, Zimmermann U, Lüllmann-Rauch R, Eskelinen EL, Schröder J, Schwake M, Saftig P., Free PMC Article | 01/21/2010 |
| Overexpression of LGP85 causes an enlargement of early endosomes and late endosomes/lysosomes. LGP85 may participate in reorganizing the endosomal/lysosomal compartments. | A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology.
Kuronita T, Eskelinen EL, Fujita H, Saftig P, Himeno M, Tanaka Y. | 01/21/2010 |