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. Schleutker J, Haataja L, Renlund M, Puhakka L, Viitala J, Peltonen L, Aula P (Nov 1991). "Confirmation of the chromosomal localization of human lamp genes and their exclusion as candidate genes for Salla disease". Human Genetics. 88 (1): 95–7. doi: 10.1007/BF00204936. PMID 1959930. S2CID 31520394. 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). Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

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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] 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.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: Höning S, Sandoval IV, von Figura K (Aug 1998). "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3". The EMBO Journal. 17 (5): 1304–14. doi: 10.1093/emboj/17.5.1304. PMC 1170479. PMID 9482728. 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.

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Ohno H, Stewart J, Fournier MC, Bosshart H, Rhee I, Miyatake S, Saito T, Gallusser A, Kirchhausen T, Bonifacino JS (Sep 1995). "Interaction of tyrosine-based sorting signals with clathrin-associated proteins". Science. 269 (5232): 1872–5. Bibcode: 1995Sci...269.1872O. doi: 10.1126/science.7569928. PMID 7569928. 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. 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. 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]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. The Blagdon Inpond 6000 is an instant solution for achieving a healthy, clear and beautiful pond. The pond filter has been designed for ponds up to 6000 litres in size and boasts 5 innovative features merged into one design - all of which remain unmatched when it comes to pond filters on the market right now. The innovation comes complete with 4 stunning fountain heads for a range of breathtaking effects. A low wattage LED spotlight automatically illuminates the pond during nighttime, switching on after dark to provide an eye-catching focal feature for your garden over those long summer nights. PDBe-KB provides an overview of all the structure information available in the PDB for Human Lysosome-associated membrane glycoprotein 1 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. Mane SM, Marzella L, Bainton DF, Holt VK, Cha Y, Hildreth JE, August JT (Jan 1989). "Purification and characterization of human lysosomal membrane glycoproteins". Archives of Biochemistry and Biophysics. 268 (1): 360–78. doi: 10.1016/0003-9861(89)90597-3. PMID 2912382.