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Gene Review

Lamp1  -  lysosomal-associated membrane protein 1

Rattus norvegicus

Synonyms: 120 kDa lysosomal membrane glycoprotein, CD107 antigen-like family member A, LAMP-1, LGP-120, Lamp-1, ...
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Disease relevance of Lamp1


High impact information on Lamp1

  • Here, the lysosomal membrane glycoprotein LGP96 was identified as a receptor for the selective import and degradation of proteins within lysosomes [3].
  • Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat lgp120 (lamp-I) in MDCK cells [4].
  • Rat lysosomal glycoprotein 120 (lgp120; lamp-I) is a transmembrane protein that is directly delivered from the trans-Golgi network (TGN) to the endosomal/lysosomal system without prior appearance on the cell surface [4].
  • AVd were positive for cathepsin D and lgp120 [5].
  • However, unlike nascent vacuoles vet comparable to degradative vacuoles, these vacuoles were acidic and contained the lysosomal membrane protein, lgp120, at the outer limiting membrane [6].

Biological context of Lamp1

  • The autophagy induced in mitotic cells was inhibited by amino acids, and the resulting autophagosomes contained proteins LC3 and Lamp1, known to be associated with autophagosomes in interphase cells [7].
  • The deduced amino acid sequence demonstrates that lgp120 contains a putative signal peptide, 18 sites for N-linked glycosylation, a single membrane-spanning segment, and a short (11 amino acid) cytosolic tail [8].
  • To study the kinetics of appearance of endocytic tracers in MPR-and/or lgp120-containing pools in greater detail, cells were allowed to endocytose horse-radish peroxidase (HRP) for 5-90 min [1].
  • Depletion of Lamp-1 and Lamp-2 had no measurable effect on endosomal/lysosomal pH, osmotic stability, or density, and cell viability was maintained [9].
  • We used the oligonucleotide probe corresponding to the internal amino acid sequence of a lysosomal membrane glycoprotein with a molecular weight of 85 K (LGP85) and isolated and characterized cDNA clones containing the entire coding region [10].

Anatomical context of Lamp1


Associations of Lamp1 with chemical compounds

  • Prelysosomelike and lysosomelike structures in ultrathin cryosections of M cells reacted with polyclonal antibody to a membrane glycoprotein (lgp120) enriched in prelysosomes and lysosomes [13].
  • In contrast, antibodies to the receptors for asialoglycoproteins and mannose-6-phosphate or to the lysosomal membrane protein, lgp120, distributed to endosomes or lysosomes, respectively, without accumulating in the subapical area [14].
  • Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis [9].
  • One correlated to lgp120-positive (pre)lysosomes and was still observed after treatment with brefeldin A (BFA), while the other appeared to be partially associated with Golgi membranes and was BFA-sensitive [15].
  • PT cells accumulated 109Cd7MT-1 in membrane vesicles associated with the late endo/lysosomal marker LAMP1 but less with the early endosomal marker Rab5a, which was abolished by chloroquine or LY-294002 [16].

Other interactions of Lamp1


Analytical, diagnostic and therapeutic context of Lamp1

  • The reduction in detectability of MPR and lgp120 antigenicity on Western blots, due to treatment of cell homogenates with 3'3-diaminobenzidine, was followed in time [1].
  • Thapsigargin also induced the formation of large lgp120-containing vesicles, detected by both confocal and transmission electron microscopy [20].
  • Northern blot analysis also demonstrated the presence of lamp-1 transcripts in non-neural tissues [2].
  • In parallel with the changes in cathepsins, we found that the amounts of LGP120, LGP110, and LGP85, three integral lysosomal membrane proteins, declined significantly after hepatectomy, suggesting that the lysosomal levels are also diminished in regenerating liver [21].
  • Wild-type cathepsin E expressed in human embryonic kidney 293T cells was mainly found in the LAMP-1-positive endosomal organelles, as determined by immunofluorescence microscopy [22].


  1. Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles. Geuze, H.J., Stoorvogel, W., Strous, G.J., Slot, J.W., Bleekemolen, J.E., Mellman, I. J. Cell Biol. (1988) [Pubmed]
  2. Isolation of the gene encoding lamp-1, a lysosomal membrane protein, by differential screening in an animal model of status epilepticus. Sun, N., Bruce, A.J., Baudry, M., Schreiber, S.S. Brain Res. Mol. Brain Res. (1997) [Pubmed]
  3. A receptor for the selective uptake and degradation of proteins by lysosomes. Cuervo, A.M., Dice, J.F. Science (1996) [Pubmed]
  4. Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat lgp120 (lamp-I) in MDCK cells. Höning, S., Hunziker, W. J. Cell Biol. (1995) [Pubmed]
  5. The differential degradation of two cytosolic proteins as a tool to monitor autophagy in hepatocytes by immunocytochemistry. Rabouille, C., Strous, G.J., Crapo, J.D., Geuze, H.J., Slot, J.W. J. Cell Biol. (1993) [Pubmed]
  6. Studies on the mechanisms of autophagy: maturation of the autophagic vacuole. Dunn, W.A. J. Cell Biol. (1990) [Pubmed]
  7. Inhibition of autophagy in mitotic animal cells. Eskelinen, E.L., Prescott, A.R., Cooper, J., Brachmann, S.M., Wang, L., Tang, X., Backer, J.M., Lucocq, J.M. Traffic (2002) [Pubmed]
  8. Derived protein sequence, oligosaccharides, and membrane insertion of the 120-kDa lysosomal membrane glycoprotein (lgp120): identification of a highly conserved family of lysosomal membrane glycoproteins. Howe, C.L., Granger, B.L., Hull, M., Green, S.A., Gabel, C.A., Helenius, A., Mellman, I. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  9. Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis. Kundra, R., Kornfeld, S. J. Biol. Chem. (1999) [Pubmed]
  10. Isolation and sequencing of a cDNA clone encoding 85kDa sialoglycoprotein in rat liver lysosomal membranes. Fujita, H., Ezaki, J., Noguchi, Y., Kono, A., Himeno, M., Kato, K. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  11. Mannose-6-phosphate receptors for lysosomal enzymes cycle between the Golgi complex and endosomes. Brown, W.J., Goodhouse, J., Farquhar, M.G. J. Cell Biol. (1986) [Pubmed]
  12. Translocation and clustering of endosomes and lysosomes depends on microtubules. Matteoni, R., Kreis, T.E. J. Cell Biol. (1987) [Pubmed]
  13. Rat intestinal M cells contain acidic endosomal-lysosomal compartments and express class II major histocompatibility complex determinants. Allan, C.H., Mendrick, D.L., Trier, J.S. Gastroenterology (1993) [Pubmed]
  14. Apical plasma membrane proteins and endolyn-78 travel through a subapical compartment in polarized WIF-B hepatocytes. Ihrke, G., Martin, G.V., Shanks, M.R., Schrader, M., Schroer, T.A., Hubbard, A.L. J. Cell Biol. (1998) [Pubmed]
  15. Late endocytic compartments are major sites of annexin VI localization in NRK fibroblasts and polarized WIF-B hepatoma cells. Pons, M., Ihrke, G., Koch, S., Biermer, M., Pol, A., Grewal, T., Jäckle, S., Enrich, C. Exp. Cell Res. (2000) [Pubmed]
  16. Apoptosis by Cd2+ or CdMT in proximal tubule cells: different uptake routes and permissive role of endo/lysosomal CdMT uptake. Erfurt, C., Roussa, E., Thévenod, F. Am. J. Physiol., Cell Physiol. (2003) [Pubmed]
  17. Isolation and sequencing of a cDNA clone encoding 96 kDa sialoglycoprotein in rat liver lysosomal membranes. Noguchi, Y., Himeno, M., Sasaki, H., Tanaka, Y., Kono, A., Sakaki, Y., Kato, K. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  18. Effect of cholera toxin and cyclic adenosine monophosphate on fluid-phase endocytosis, distribution, and trafficking of endosomes in rat liver. Van Dyke, R.W. Hepatology (2000) [Pubmed]
  19. Ultrastructural and immunocytochemical characterization of autophagic vacuoles in isolated hepatocytes: effects of vinblastine and asparagine on vacuole distributions. Fengsrud, M., Roos, N., Berg, T., Liou, W., Slot, J.W., Seglen, P.O. Exp. Cell Res. (1995) [Pubmed]
  20. Homotypic fusion between aggregated lysosomes triggered by elevated [Ca2+]i in fibroblasts. Bakker, A.C., Webster, P., Jacob, W.A., Andrews, N.W. J. Cell. Sci. (1997) [Pubmed]
  21. Suppression of lysosomal proteolysis at three different steps in regenerating rat liver. Watanabe, K., Ishidoh, K., Ueno, T., Sato, N., Kominami, E. J. Biochem. (1998) [Pubmed]
  22. Characterization of rat cathepsin E and mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells. Tsukuba, T., Ikeda, S., Okamoto, K., Yasuda, Y., Sakai, E., Kadowaki, T., Sakai, H., Yamamoto, K. FEBS J. (2006) [Pubmed]
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