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LAMP1

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LAMP1
Identifiers
AliasesLAMP1, CD107a, LAMPA, LGP120, lysosomal associated membrane protein 1
External IDsOMIM: 153330; MGI: 96745; HomoloGene: 4061; GeneCards: LAMP1; OMA:LAMP1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3916

16783

Ensembl

ENSG00000185896

ENSMUSG00000031447

UniProt

P11279

P11438

RefSeq (mRNA)

NM_005561

NM_010684
NM_001317353

RefSeq (protein)

NP_005552

NP_001304282
NP_034814

Location (UCSC)Chr 13: 113.3 – 113.32 MbChr 8: 13.21 – 13.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Lysosomal-associated membrane protein 1 (LAMP-1) also known as lysosome-associated membrane glycoprotein 1 and CD107a (Cluster of Differentiation 107a), is a protein that in humans is encoded by the LAMP1 gene. The human LAMP1 gene is located on the long arm (q) of chromosome 13 at region 3, band 4 (13q34).

Lysosomal-associated membrane protein 1 is a glycoprotein from a family of Lysosome-associated membrane glycoproteins.[5] The LAMP-1 glycoprotein is a type I transmembrane protein[6] which is expressed at high or medium levels in at least 76 different normal tissue cell types.[7] It resides primarily across lysosomal membranes,[8] and functions to provide selectins with carbohydrate ligands.[5] CD107a has also been shown to be a marker of degranulation on lymphocytes such as CD8+ and NK cells.[9] and may also play a role in tumor cell differentiation and metastasis.

Structure

Residing primarily across lysosomal membranes, these glycoproteins consist of a large, highly glycosylated end with N-linked carbon chains on the luminal side of the membrane, and a short C-terminal tail[6] exposed to the cytoplasm.[8] The extracytoplasmic region contains a hinge-like structure which can form disulphide bridges homologous to those observed in human immunoglobulin A.[8] Other characteristics of the structure of the LAMP-1 glycoproteins include:

Function

LAMP1 and LAMP2 glycoproteins comprise 50% of all lysosomal membrane proteins,[6] and are thought to be responsible in part for maintaining lysosomal integrity, pH and catabolism.[6][11] The expression of LAMP1 and LAMP2 glycoproteins are linked, as deficiencies in LAMP1 gene will lead to increased expression of LAMP2 glycoproteins.[11] The two are therefore thought to share similar functions in vivo.[6] However, this makes the determining the precise function of LAMP1 difficult, because while the LAMP1 deficient phenotype is little different than the wild type due to LAMP2 up regulation,[6][11] the LAMP1/LAMP2 double deficient phenotype leads to embryonic lethality.[11]

Although the LAMP1 glycoproteins primarily reside across lysosomal membranes, in certain cases they can be expressed across the plasma membrane of the cell.[11] Expression of LAMP1 at the cell surface can occur due to lysosomal fusion with the cell membrane.[12] Cell surface expression of LAMP1 can serve as a ligand for selectins[13][14] and help mediate cell-cell adhesion.[15] Accordingly, cell surface expression of LAMP1 is seen in cells with migratory or invasive functions, such as cytotoxic T cells, platelets and macrophages.[16] Cell surface expression of LAMP1 and LAMP2 is also often seen in cancer cells,[16][17] particularly cancers with high metastatic potential, such as colon carcinoma and melanoma,[16] and has been shown to correlate with their metastatic potential.[11]

Role in cancer

LAMP1 expression on the surface of tumor cells has been observed for a number of different cancer types, particularly in highly metastatic cancers such as pancreatic cancer,[18][19] colon cancer[16][17] and melanoma.[16][17] The structure of LAMP1 correlates with differentiation[8][20] and metastatic potential[11] of tumor cells as it is thought to help mediate cell-cell adhesion [17] and migration.[15][18] Indeed, the adhesion of some cancer cells to the extracellular matrix is mediated by interactions between LAMP1 and LAMP2 and E-selectin and galectins, with the LAMPs serving as ligands for the cell-adhesion molecules.[17]

Cell membrane expression of LAMP-1 observed in the following cancer types:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185896 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031447 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "LAMP1 lysosomal-associated membrane protein 1". Entrez Gene.
  6. ^ a b c d e f Eskelinen EL (2006). "Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy". Molecular Aspects of Medicine. 27 (5–6): 495–502. doi:10.1016/j.mam.2006.08.005. PMID 16973206.
  7. ^ "LAMP1". The Human Protein Atlas.
  8. ^ a b c d e Carlsson SR, Fukuda M (Dec 1989). "Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement". The Journal of Biological Chemistry. 264 (34): 20526–31. PMID 2584229.
  9. ^ "LAMP1 - lysosomal-associated membrane protein1". Wikigenes.
  10. ^ a b c Carlsson SR, Roth J, Piller F, Fukuda M (Dec 1988). "Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan". The Journal of Biological Chemistry. 263 (35): 18911–9. PMID 3143719.
  11. ^ a b c d e f g h Andrejewski N, Punnonen EL, Guhde G, Tanaka Y, Lüllmann-Rauch R, Hartmann D, von Figura K, Saftig P (Apr 1999). "Normal lysosomal morphology and function in LAMP-1-deficient mice". The Journal of Biological Chemistry. 274 (18): 12692–701. doi:10.1074/jbc.274.18.12692. PMID 10212251.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  12. ^ Kima, P. E.; Burleigh, B.; Andrews, N. W. (Dec 2000). "Surface-targeted lysosomal membrane glycoprotein-1 (Lamp-1) enhances lysosome exocytosis and cell invasion by Trypanosoma cruzi". Cellular Microbiology. 2 (6): 477–486. doi:10.1046/j.1462-5822.2000.00071.x. ISSN 1462-5814. PMID 11207602.
  13. ^ Laferte S, Dennis JW (Apr 1989). "Purification of two glycoproteins expressing beta 1-6 branched Asn-linked oligosaccharides from metastatic tumour cells". The Biochemical Journal. 259 (2): 569–576. doi:10.1042/bj2590569. PMID 2719668.
  14. ^ Sawada R, Jardine KA, Fukuda M (Apr 1993). "The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon organization in two genes". The Journal of Biological Chemistry. 268 (12): 9014–9022. PMID 8517882.
  15. ^ a b Acevedo-Schermerhorn C, Gray-Bablin J, Gama R, McCormick PJ (Nov 1997). "t-complex-associated embryonic surface antigen homologous to mLAMP-1. II. Expression and distribution analyses". Experimental Cell Research. 236 (2): 510–518. doi:10.1006/excr.1997.3752. PMID 9367636.
  16. ^ a b c d e Agarwal, Akhil Kumar; Srinivasan, Nithya; Godbole, Rashmi; More, Shyam K.; Budnar, Srikanth; Gude, Rajiv P.; Kalraiya, Rajiv D. (2015-01-23). "Role of tumor cell surface lysosome-associated membrane protein-1 (LAMP1) and its associated carbohydrates in lung metastasis". Journal of Cancer Research and Clinical Oncology. 141: 1–12. doi:10.1007/s00432-015-1917-2. ISSN 0171-5216.
  17. ^ a b c d e f g h Sarafian V, Jadot M, Foidart JM, Letesson JJ, Van den Brûle F, Castronovo V, Wattiaux R, Coninck SW (Jan 1998). "Expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in human tumor cells". International Journal of Cancer. Journal International Du Cancer. 75 (1): 105–111. doi:10.1002/(sici)1097-0215(19980105)75:1<105::aid-ijc16>3.3.co;2-f. PMID 9426697.
  18. ^ a b c Jensen SS, Aaberg-Jessen C, Christensen KG, Kristensen B (2013). "Expression of the lysosomal-associated membrane protein-1 (LAMP-1) in astrocytomas". International Journal of Clinical and Experimental Pathology. 6 (7): 1294–1305. PMID 23826410.
  19. ^ a b Künzli BM, Berberat PO, Zhu ZW, Martignoni M, Kleeff J, Tempia-Caliera AA, Fukuda M, Zimmermann A, Friess H, Büchler MW (Jan 2002). "Influences of the lysosomal associated membrane proteins (Lamp-1, Lamp-2) and Mac-2 binding protein (Mac-2-BP) on the prognosis of pancreatic carcinoma". Cancer. 94 (1): 228–239. doi:10.1002/cncr.10162. PMID 11815981.
  20. ^ Lee N, Wang WC, Fukuda M (Nov 1990). "Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins". The Journal of Biological Chemistry. 265 (33): 20476–87. PMID 2243101.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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