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Zhang J, Sun B, Shen W, Wang Z, Liu Y, Sun Y, Zhang J, Liu R, Wang Y, Bai T, Ma Z, Luo C, Qiao X, Zhang X, Yang S, Sun Y, Jiang D, Yang K. Zhang J, et al. Vaccines (Basel). 2023 Oct 20;11(10):1620. doi: 10.3390/vaccines11101620. Vaccines (Basel). 2023. PMID: 37897022 Free PMC article. PDBe-KB provides an overview of all the structure information available in the PDB for Human Lysosome-associated membrane glycoprotein 1 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). 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]

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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. 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. 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. 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. Obviously I never heard of such a thing until tonight. Google revealed it's one of those tiktok crazes and I looked at the options.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.

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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.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. 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: 18701486 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] 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): 9014–22. doi: 10.1016/S0021-9258(18)52972-0. PMID 8517882. 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.

LAMP-1-deficient Normal Lysosomal Morphology and Function in LAMP-1-deficient

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. Immunofluorescence staining of HeLa Cells with antibody to reveal lysosomal LAMP1 in red and vimentin containing intermediate filaments in green. Nuclear DNA is seen in blue. Antibodies and image courtesy EnCor Biotechnology Inc. Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine. 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. doi: 10.1016/S0021-9258(18)37369-1. PMID 3143719.poly-N-acetyllactosamine groups which are involved in interactions with selectin and other glycan-binding proteins [11] Significant quantities of polylactosaminoglycan and sialic acid to traverse the trans- Golgi cisternae. [10] in 1 looks like you have to change the filters to get the colour you want (sunset or red sunset or rainbow etc) 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.

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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. 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. The Blagdon Inpond 5 in 1 6000 Pond filter also features a 9w UVC clarifier to ensure the best possible water clarity levels. The clarifier is integrated into the kills' of the pond filter to effectively reduce and control green water in ponds for crystal clear results. 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:Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine. Tanaka Y, Guhde G, Suter A, Eskelinen EL, Hartmann D, Lüllmann-Rauch R, Janssen PM, Blanz J, von Figura K, Saftig P. Tanaka Y, et al. Nature. 2000 Aug 24;406(6798):902-6. doi: 10.1038/35022595. Nature. 2000. PMID: 10972293