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Aqualease Ltd t/a Complete Aquatics is authorised and regulated by the Financial Conduct Authority, register number 729918 and act as a credit broker and not a lender. 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 l ysosomal 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. Fukuda M, Viitala J, Matteson J, Carlsson SR (Dec 1988). "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences". The Journal of Biological Chemistry. 263 (35): 18920–8. doi: 10.1016/S0021-9258(18)37370-8. PMID 3198605. Endo Y, Furuta A, Nishino I. Endo Y, et al. Acta Neuropathol. 2015 Mar;129(3):391-8. doi: 10.1007/s00401-015-1385-4. Epub 2015 Jan 15. Acta Neuropathol. 2015. PMID: 25589223 Review. Zhang H, Li XJ, Martin DB, Aebersold R (Jun 2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nature Biotechnology. 21 (6): 660–6. doi: 10.1038/nbt827. PMID 12754519. S2CID 581283.

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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. PMC 3693194. PMID 23826410.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. PMC 1138546. PMID 2719668. 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). 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.

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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 [ edit ] Mattei MG, Matterson J, Chen JW, Williams MA, Fukuda M (May 1990). "Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2, are encoded by genes localized to chromosome 13q34 and chromosome Xq24-25, respectively". The Journal of Biological Chemistry. 265 (13): 7548–51. doi: 10.1016/S0021-9258(19)39148-3. PMID 2332441. Clarkson-Paredes C, Karl MT, Popratiloff A, Miller RH. Clarkson-Paredes C, et al. PNAS Nexus. 2023 Oct 12;2(10):pgad334. doi: 10.1093/pnasnexus/pgad334. eCollection 2023 Oct. PNAS Nexus. 2023. PMID: 37901440 Free PMC article.PDBe-KB provides an overview of all the structure information available in the PDB for Human Lysosome-associated membrane glycoprotein 1 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. doi: 10.1016/S0021-9258(19)47094-4. PMID 2584229. Viitala J, Carlsson SR, Siebert PD, Fukuda M (Jun 1988). "Molecular cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr approximately equal to 120,000". Proceedings of the National Academy of Sciences of the United States of America. 85 (11): 3743–7. Bibcode: 1988PNAS...85.3743V. doi: 10.1073/pnas.85.11.3743. PMC 280294. PMID 3131762. Rothaug M, Stroobants S, Schweizer M, Peters J, Zunke F, Allerding M, D'Hooge R, Saftig P, Blanz J. Rothaug M, et al. Acta Neuropathol Commun. 2015 Jan 31;3:6. doi: 10.1186/s40478-014-0182-y. Acta Neuropathol Commun. 2015. PMID: 25637286 Free PMC article.

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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. doi: 10.1016/S0021-9258(17)30529-X. PMID 2243101. Significant quantities of polylactosaminoglycan and sialic acid to traverse the trans- Golgi cisternae. [10] Raposo G, Moore M, Innes D, Leijendekker R, Leigh-Brown A, Benaroch P, Geuze H (Oct 2002). "Human macrophages accumulate HIV-1 particles in MHC II compartments". Traffic. 3 (10): 718–29. doi: 10.1034/j.1600-0854.2002.31004.x. PMID 12230470. S2CID 7055266. Fehrenbacher N, Bastholm L, Kirkegaard-Sørensen T, Rafn B, Bøttzauw T, Nielsen C, Weber E, Shirasawa S, Kallunki T, Jäättelä M. Fehrenbacher N, et al. Cancer Res. 2008 Aug 15;68(16):6623-33. doi: 10.1158/0008-5472.CAN-08-0463. Cancer Res. 2008. PMID: 18701486poly-N-acetyllactosamine groups which are involved in interactions with selectin and other glycan-binding proteins [11] 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. doi: 10.1016/S0021-9258(18)52972-0. PMID 8517882. Howe CL, Granger BL, Hull M, Green SA, Gabel CA, Helenius A, Mellman I (Oct 1988). "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". Proceedings of the National Academy of Sciences of the United States of America. 85 (20): 7577–81. Bibcode: 1988PNAS...85.7577H. doi: 10.1073/pnas.85.20.7577. PMC 282235. PMID 3174652. 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. S2CID 19192092. 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: