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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. Significant quantities of polylactosaminoglycan and sialic acid to traverse the trans- Golgi cisternae. [10]

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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. 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. 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).

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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.

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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. 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.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 ] 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]

LAMP1 - Wikipedia LAMP1 - Wikipedia

PDBe-KB provides an overview of all the structure information available in the PDB for Human Lysosome-associated membrane glycoprotein 1 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. 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. doi: 10.1016/S0021-9258(19)47094-4. PMID 2584229. 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. Chang MH, Karageorgos LE, Meikle PJ (2003). "CD107a (LAMP-1) and CD107b (LAMP-2)". Journal of Biological Regulators and Homeostatic Agents. 16 (2): 147–51. PMID 12144129.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. S2CID 12702437. 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. Polylactosamine attachments which protect the glyocoprotein from degradation by lysosomal proteases [10] 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.

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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: 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.

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.