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Lamp2  -  lysosomal-associated membrane protein 2

Mus musculus

Synonyms: CD107 antigen-like family member B, CD107b, LAMP-2, LGP-B, Lamp II, ...
 
 
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Disease relevance of Lamp2

 

Psychiatry related information on Lamp2

 

High impact information on Lamp2

 

Biological context of Lamp2

 

Anatomical context of Lamp2

 

Associations of Lamp2 with chemical compounds

  • The LAMP-1/2 double-deficient cells and, to a lesser extent, LAMP-2 single-deficient cells showed an accumulation of unesterified cholesterol in endo/lysosomal, rab7, and NPC1 positive compartments as well as reduced amounts of lipid droplets [12].
  • In these type I and type II granules, MHC class II molecules, mannose-6-phosphate receptors and lysosomal membrane proteins (lamp1 and lamp2) localize to small intralumenal vesicles [15].
  • The increased level and glycosylation of both LAMP-1 and LAMP-2 was observed also in cells treated with a synthetic chalcone carboxylic acid analog of RA and by combination of either retinoid with dibutyryl cyclic AMP [1].
  • There was no increase in large polylactosaminoglycans of lamp-1 and lamp-2 after retinoic acid treatment, but an increase in the size of small polylactosaminoglycans (included on Bio-Gel P-6) and tri- and tetra-antennary complex oligosaccharides [16].
  • The phagosomes containing live M. ptb and M. avium were significantly reduced in their ability to acquire some markers for the endocytic pathway, such as internalized calcein, BSA-gold or the membrane protein Lamp 2 [17].
 

Co-localisations of Lamp2

 

Other interactions of Lamp2

 

Analytical, diagnostic and therapeutic context of Lamp2

References

  1. Modulation of lysosomal-associated membrane glycoproteins during retinoic acid-induced embryonal carcinoma cell differentiation. Amos, B., Lotan, R. J. Biol. Chem. (1990) [Pubmed]
  2. Morphological, clinical and genetic aspects in a family with a novel LAMP-2 gene mutation (Danon disease). Lobrinus, J.A., Schorderet, D.F., Payot, M., Jeanrenaud, X., Bottani, A., Superti-Furga, A., Schlaepfer, J., Fromer, M., Jeannet, P.Y. Neuromuscul. Disord. (2005) [Pubmed]
  3. Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy. Eskelinen, E.L. Mol. Aspects Med. (2006) [Pubmed]
  4. Mouse polyomavirus utilizes recycling endosomes for a traffic pathway independent of COPI vesicle transport. Mannová, P., Forstová, J. J. Virol. (2003) [Pubmed]
  5. LAMP-2 deficient mice show depressed cardiac contractile function without significant changes in calcium handling. Stypmann, J., Janssen, P.M., Prestle, J., Engelen, M.A., Kögler, H., Lüllmann-Rauch, R., Eckardt, L., von Figura, K., Landgrebe, J., Mleczko, A., Saftig, P. Basic Res. Cardiol. (2006) [Pubmed]
  6. Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice. Tanaka, Y., Guhde, G., Suter, A., Eskelinen, E.L., Hartmann, D., Lüllmann-Rauch, R., Janssen, P.M., Blanz, J., von Figura, K., Saftig, P. Nature (2000) [Pubmed]
  7. The giant organelles in beige and Chediak-Higashi fibroblasts are derived from late endosomes and mature lysosomes. Burkhardt, J.K., Wiebel, F.A., Hester, S., Argon, Y. J. Exp. Med. (1993) [Pubmed]
  8. LAMP proteins are required for fusion of lysosomes with phagosomes. Huynh, K.K., Eskelinen, E.L., Scott, C.C., Malevanets, A., Saftig, P., Grinstein, S. EMBO J. (2007) [Pubmed]
  9. The lysosomal-associated membrane protein LAMP-1 is a novel differentiation marker for HC11 mouse mammary epithelial cells. Cella, N., Cornejo-Uribe, R.R., Montes, G.S., Hynes, N.E., Chammas, R. Differentiation (1996) [Pubmed]
  10. Differential expression of lysosomal associated membrane protein (LAMP-1) during mammalian spermiogenesis. Moreno, R.D. Mol. Reprod. Dev. (2003) [Pubmed]
  11. Functional regulation of tyrosinase and LAMP gene family of melanogenesis and cell death in immortal murine melanocytes after repeated exposure to ultraviolet B. Ota, A., Park, J.S., Jimbow, K. Br. J. Dermatol. (1998) [Pubmed]
  12. Disturbed cholesterol traffic but normal proteolytic function in LAMP-1/LAMP-2 double-deficient fibroblasts. Eskelinen, E.L., Schmidt, C.K., Neu, S., Willenborg, M., Fuertes, G., Salvador, N., Tanaka, Y., Lüllmann-Rauch, R., Hartmann, D., Heeren, J., von Figura, K., Knecht, E., Saftig, P. Mol. Biol. Cell (2004) [Pubmed]
  13. Normal lysosomal morphology and function in LAMP-1-deficient mice. Andrejewski, N., Punnonen, E.L., Guhde, G., Tanaka, Y., Lüllmann-Rauch, R., Hartmann, D., von Figura, K., Saftig, P. J. Biol. Chem. (1999) [Pubmed]
  14. Role of LAMP-2 in lysosome biogenesis and autophagy. Eskelinen, E.L., Illert, A.L., Tanaka, Y., Schwarzmann, G., Blanz, J., Von Figura, K., Saftig, P. Mol. Biol. Cell (2002) [Pubmed]
  15. Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation. Raposo, G., Tenza, D., Mecheri, S., Peronet, R., Bonnerot, C., Desaymard, C. Mol. Biol. Cell (1997) [Pubmed]
  16. Lamp-1 does not acquire the large polylactosaminoglycans characteristic of F9 cells. Romero, P.A., Way, T., Herscovics, A. Biochem. J. (1993) [Pubmed]
  17. Characterization of the intracellular survival of Mycobacterium avium ssp. paratuberculosis: phagosomal pH and fusogenicity in J774 macrophages compared with other mycobacteria. Kuehnel, M.P., Goethe, R., Habermann, A., Mueller, E., Rohde, M., Griffiths, G., Valentin-Weigand, P. Cell. Microbiol. (2001) [Pubmed]
  18. From lysosomes to the plasma membrane: localization of vacuolar-type H+ -ATPase with the a3 isoform during osteoclast differentiation. Toyomura, T., Murata, Y., Yamamoto, A., Oka, T., Sun-Wada, G.H., Wada, Y., Futai, M. J. Biol. Chem. (2003) [Pubmed]
  19. Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice. Shirahama-Noda, K., Yamamoto, A., Sugihara, K., Hashimoto, N., Asano, M., Nishimura, M., Hara-Nishimura, I. J. Biol. Chem. (2003) [Pubmed]
  20. Identification of two lysosomal membrane glycoproteins. Chen, J.W., Murphy, T.L., Willingham, M.C., Pastan, I., August, J.T. J. Cell Biol. (1985) [Pubmed]
  21. Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. Demetriou, M., Nabi, I.R., Coppolino, M., Dedhar, S., Dennis, J.W. J. Cell Biol. (1995) [Pubmed]
 
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