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{{Infobox_gene}}
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'''Lysosomal-associated membrane protein 1''' ('''LAMP-1''') also known as '''lysosome-associated membrane glycoprotein 1''' and '''CD107a''' ('''C'''luster of '''D'''ifferentiation 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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[[File:HeLa_cells_showin_Lamp1_in_red,_vimentin_in_green_and_DNA_in_blue.jpg|thumb|328px|Immunofluorescence staining of [[HeLa | 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 | EnCor Biotechnology Inc]].]]
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Lysosomal-associated membrane protein 1
| HGNCid = 6499
| Symbol = LAMP1
| AltSymbols =; CD107a; LAMPA; LGP120
| OMIM = 153330
| ECnumber = 
| Homologene = 4061
| MGIid = 96745
| GeneAtlas_image1 = PBB_GE_LAMP1_201553_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMP1_201551_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_LAMP1_201552_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005771 |text = multivesicular body}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042383 |text = sarcolemma}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3916
    | Hs_Ensembl = ENSG00000185896
    | Hs_RefseqProtein = NP_005552
    | Hs_RefseqmRNA = NM_005561
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 13
    | Hs_GenLoc_start = 112999557
    | Hs_GenLoc_end = 113025746
    | Hs_Uniprot = P11279
    | Mm_EntrezGene = 16783
    | Mm_Ensembl = ENSMUSG00000031447
    | Mm_RefseqmRNA = NM_010684
    | Mm_RefseqProtein = NP_034814
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 13159138
    | Mm_GenLoc_end = 13175307
    | Mm_Uniprot = Q3TA96
  }}
}}
'''Lysosomal-associated membrane protein 1''' ('''LAMP1''') also known as '''CD107a''' ('''C'''luster of '''D'''ifferentiation 107a)
, is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMP1 lysosomal-associated membrane protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3916| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Lysosomal-associated membrane protein 1 is a [[glycoprotein]] from a family of [[Lysosome-associated membrane glycoproteins]].<ref name="entrez">{{cite web | title = LAMP1 lysosomal-associated membrane protein 1 | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3916 | work = Entrez Gene }}</ref> The LAMP-1 glycoprotein is a type I [[transmembrane protein]]<ref name = "Eskelinen_2006">{{cite journal | vauthors = Eskelinen EL | title = Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy | journal = Molecular Aspects of Medicine | volume = 27 | issue = 5–6 | pages = 495–502 | pmid = 16973206 | doi = 10.1016/j.mam.2006.08.005 | year=2006}}</ref> which is expressed at high or medium levels in at least 76 different normal tissue cell types.<ref name="HPA">{{cite web | work  = The Human Protein Atlas | title = LAMP1 | url = http://www.proteinatlas.org/ENSG00000185896-LAMP1/tissue }}</ref> It resides primarily across l[[lysosome|ysosomal]] membranes,<ref name="Carlsson_1989">{{cite journal | vauthors = Carlsson SR, Fukuda M | title = Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement | journal = The Journal of Biological Chemistry | volume = 264 | issue = 34 | pages = 20526–31 | date = Dec 1989 | pmid = 2584229 }}</ref> and functions to provide [[selectin]]s with [[carbohydrate]] [[Ligand (biochemistry)|ligands]].<ref name="entrez"/> CD107a has also been shown to be a marker of [[degranulation]] on [[lymphocytes]] such as [[CD8+ cell|CD8+]] and [[NK cells]].<ref name="Wikigenes">{{cite web|title=LAMP1 - lysosomal-associated membrane protein1 | work = Wikigenes | url=https://www.wikigenes.org/e/gene/e/3916.html}}</ref> and may also play a role in [[tumor]] [[cell differentiation]] and [[metastasis]].
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of a family of membrane glycoproteins.  This glycoprotein provides selectins with carbohydrate ligands.  It may also play a role in tumor cell metastasis.<ref name="entrez">{{cite web | title = Entrez Gene: LAMP1 lysosomal-associated membrane protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3916| accessdate = }}</ref>
}}


==See also==
== Structure ==
 
Residing primarily across lysosomal membranes, these glycoproteins consist of a large, highly [[Glycosylation|glycosylated]] end with N-linked carbon chains on the luminal side of the membrane, and a short C-terminal tail<ref name="Eskelinen_2006" /> exposed to the [[cytoplasm]].<ref name="Carlsson_1989" /> The extracytoplasmic region contains a hinge-like structure which can form [[disulphide bridges]] homologous to those observed in human [[immunoglobulin A]].<ref name="Carlsson_1989" /> Other characteristics of the structure of the LAMP-1 glycoproteins include:
* A [[polypeptide]] core of ~40kDa<ref name="Carlsson_1989" />
* 18 {[[N-glycosylation]]} sites to help with the addition of sugar chains<ref name="Carlsson_1988">{{cite journal | vauthors = Carlsson SR, Roth J, Piller F, Fukuda M | title = Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan | journal = The Journal of Biological Chemistry | volume = 263 | issue = 35 | pages = 18911–9 | date = Dec 1988 | pmid = 3143719 }}</ref>
* Polylactosamine attachments which protect the glyocoprotein from degradation by lysosomal [[protease]]s<ref name="Carlsson_1988" />
* Significant quantities of polylactosaminoglycan and [[sialic acid]] to traverse the trans-[[Golgi apparatus|Golgi]] [[cisterna]]e.<ref name="Carlsson_1988" />
* poly-N-acetyllactosamine groups which are involved in interactions with [[selectin]] and other [[glycan]]-binding proteins<ref name="Andrejewski_1999">{{cite journal | vauthors = Andrejewski N, Punnonen EL, Guhde G, Tanaka Y, Lüllmann-Rauch R, Hartmann D, von Figura K, Saftig P | title = Normal lysosomal morphology and function in LAMP-1-deficient mice | journal = The Journal of Biological Chemistry | volume = 274 | issue = 18 | pages = 12692–701 | date = Apr 1999 | pmid = 10212251 | doi=10.1074/jbc.274.18.12692}}</ref>
 
== Function ==
 
LAMP1 and [[LAMP2]] glycoproteins comprise 50% of all lysosomal membrane proteins,<ref name="Eskelinen_2006" /> and are thought to be responsible in part for maintaining lysosomal integrity, pH and [[catabolism]].<ref name="Eskelinen_2006" /><ref name="Andrejewski_1999" />  The expression of LAMP1 and LAMP2 glycoproteins are linked, as deficiencies in ''LAMP1'' gene will lead to increased expression of LAMP2 glycoproteins.<ref name="Andrejewski_1999" /> The two are therefore thought to share similar functions ''in vivo''.<ref name="Eskelinen_2006" /> 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,<ref name="Eskelinen_2006" /><ref name="Andrejewski_1999" /> the ''LAMP1''/''LAMP2'' double deficient phenotype leads to [[embryo]]nic lethality.<ref name ="Andrejewski_1999" />
 
Although the LAMP1 glycoproteins primarily reside across lysosomal membranes, in certain cases they can be expressed across the plasma membrane of the cell.<ref name="Andrejewski_1999" /> Expression of LAMP1 at the cell surface can occur due to lysosomal [[Lipid bilayer fusion|fusion]] with the cell membrane.<ref>{{Cite journal|title = Surface-targeted lysosomal membrane glycoprotein-1 (Lamp-1) enhances lysosome exocytosis and cell invasion by Trypanosoma cruzi|journal = Cellular Microbiology|date = Dec 2000|issn = 1462-5814|pmid = 11207602|pages = 477–486|volume = 2|issue = 6|first = P. E.|last = Kima|first2 = B.|last2 = Burleigh|first3 = N. W.|last3 = Andrews|doi=10.1046/j.1462-5822.2000.00071.x}}</ref> Cell surface expression of LAMP1 can serve as a ligand for [[selectin]]s<ref name="Dennis_1989">{{cite journal | vauthors = Laferte S, Dennis JW | title = Purification of two glycoproteins expressing beta 1-6 branched Asn-linked oligosaccharides from metastatic tumour cells | journal = The Biochemical Journal | volume = 259 | issue = 2 | pages = 569–576 | date = Apr 1989 | pmid = 2719668 | doi=10.1042/bj2590569 | pmc=1138546}}</ref><ref name="Sawada_1993">{{cite journal | vauthors = Sawada R, Jardine KA, Fukuda M | title = 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 | journal = The Journal of Biological Chemistry | volume = 268 | issue = 12 | pages = 9014–9022 | date = Apr 1993 | pmid = 8517882 }}</ref> and help mediate cell-[[cell adhesion]].<ref name="Acevedo-Schermerhorn_1997">{{cite journal | vauthors = Acevedo-Schermerhorn C, Gray-Bablin J, Gama R, McCormick PJ | title = t-complex-associated embryonic surface antigen homologous to mLAMP-1. II. Expression and distribution analyses | journal = Experimental Cell Research | volume = 236 | issue = 2 | pages = 510–518 | date = Nov 1997 | pmid = 9367636 | doi=10.1006/excr.1997.3752}}</ref> Accordingly, cell surface expression of LAMP1 is seen in cells with migratory or invasive functions, such as [[cytotoxic T cell]]s, [[platelet]]s and [[macrophage]]s.<ref name=":0">{{Cite journal|title = Role of tumor cell surface lysosome-associated membrane protein-1 (LAMP1) and its associated carbohydrates in lung metastasis|url = https://link.springer.com/article/10.1007/s00432-015-1917-2|journal = Journal of Cancer Research and Clinical Oncology|date = 2015-01-23|issn = 0171-5216|pages = 1–12|doi = 10.1007/s00432-015-1917-2|first = Akhil Kumar|last = Agarwal|first2 = Nithya|last2 = Srinivasan|first3 = Rashmi|last3 = Godbole|first4 = Shyam K.|last4 = More|first5 = Srikanth|last5 = Budnar|first6 = Rajiv P.|last6 = Gude|first7 = Rajiv D.|last7 = Kalraiya|volume=141}}</ref> Cell surface expression of LAMP1 and LAMP2 is also often seen in [[cancer]] cells,<ref name=":0" /><ref name="Sarafian_1988">{{cite journal | vauthors = Sarafian V, Jadot M, Foidart JM, Letesson JJ, Van den Brûle F, Castronovo V, Wattiaux R, Coninck SW | title = Expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in human tumor cells | journal = International Journal of Cancer | volume = 75 | issue = 1 | pages = 105–111 | date = Jan 1998 | pmid = 9426697 | doi=10.1002/(sici)1097-0215(19980105)75:1<105::aid-ijc16>3.0.co;2-f}}</ref> particularly cancers with high metastatic potential, such as colon carcinoma and melanoma,<ref name=":0" /> and has been shown to correlate with their metastatic potential.<ref name="Andrejewski_1999" />
 
== 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]],<ref name="Jensen_2013">{{cite journal | vauthors = Jensen SS, Aaberg-Jessen C, Christensen KG, Kristensen B | title = Expression of the lysosomal-associated membrane protein-1 (LAMP-1) in astrocytomas | journal = International Journal of Clinical and Experimental Pathology | volume = 6 | issue = 7 | pages = 1294–1305 | pmid = 23826410 | year=2013 | pmc=3693194}}</ref><ref name="Berberat_2002">{{cite journal | vauthors = Künzli BM, Berberat PO, Zhu ZW, Martignoni M, Kleeff J, Tempia-Caliera AA, Fukuda M, Zimmermann A, Friess H, Büchler MW | title = 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 | journal = Cancer | volume = 94 | issue = 1 | pages = 228–239 | date = Jan 2002 | pmid = 11815981 | doi=10.1002/cncr.10162}}</ref> [[colon cancer]]<ref name=":0" /><ref name="Sarafian_1988" /> and [[melanoma]].<ref name=":0" /><ref name="Sarafian_1988" /> The structure of LAMP1 correlates with [[Cell differentiation|differentiation]]<ref name="Carlsson_1989" /><ref name="Lee_1990">{{cite journal | vauthors = Lee N, Wang WC, Fukuda M | title = Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins | journal = The Journal of Biological Chemistry | volume = 265 | issue = 33 | pages = 20476–87 | date = Nov 1990 | pmid = 2243101 }}</ref> and metastatic potential<ref name="Andrejewski_1999" /> of tumor cells as it is thought to help mediate cell-cell adhesion <ref name="Sarafian_1988" /> and [[Cellular migration|migration]].<ref name="Acevedo-Schermerhorn_1997" /><ref name="Jensen_2013" /> Indeed, the adhesion of some cancer cells to the [[extracellular matrix]] is mediated by interactions between LAMP1 and LAMP2 and [[E-selectin]] and [[galectin]]s, with the LAMPs serving as ligands for the cell-adhesion molecules.<ref name="Sarafian_1988" />
 
Cell membrane expression of LAMP-1 observed in the following cancer types:
* Human [[fibrosarcoma]],<ref name="Sarafian_1988" />
* [[Colon cancer|Colon adenocarcinoma]],<ref name="Sarafian_1988" />
* [[Melanoma]],<ref name="Sarafian_1988" />
* [[Pancreatic cancer|Pancreatic adenocarcinoma]],<ref name="Berberat_2002" /> and
* [[Astrocytoma]].<ref name="Jensen_2013" />
 
== See also ==
* [[Cluster of differentiation]]
* [[Cluster of differentiation]]


==References==
== References ==
{{reflist|2}}
{{reflist|33em}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|33em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Chang MH, Karageorgos LE, Meikle PJ | title = CD107a (LAMP-1) and CD107b (LAMP-2) | journal = Journal of Biological Regulators and Homeostatic Agents | volume = 16 | issue = 2 | pages = 147–51 | year = 2003 | pmid = 12144129 | doi =  }}
| citations =
* {{cite journal | vauthors = Schleutker J, Haataja L, Renlund M, Puhakka L, Viitala J, Peltonen L, Aula P | title = Confirmation of the chromosomal localization of human lamp genes and their exclusion as candidate genes for Salla disease | journal = Human Genetics | volume = 88 | issue = 1 | pages = 95–7 | date = Nov 1991 | pmid = 1959930 | doi = 10.1007/BF00204936 }}
*{{cite journal | author=Chang MH, Karageorgos LE, Meikle PJ |title=CD107a (LAMP-1) and CD107b (LAMP-2). |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 2 |pages= 147-51 |year= 2003 |pmid= 12144129 |doi=  }}
* {{cite journal | vauthors = Carlsson SR, Fukuda M | title = The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones | journal = The Journal of Biological Chemistry | volume = 265 | issue = 33 | pages = 20488–95 | date = Nov 1990 | pmid = 2243102 | doi =  }}
*{{cite journal | author=Schleutker J, Haataja L, Renlund M, ''et al.'' |title=Confirmation of the chromosomal localization of human lamp genes and their exclusion as candidate genes for Salla disease. |journal=Hum. Genet. |volume=88 |issue= 1 |pages= 95-7 |year= 1992 |pmid= 1959930 |doi= }}
* {{cite journal | vauthors = Mattei MG, Matterson J, Chen JW, Williams MA, Fukuda M | title = 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 | journal = The Journal of Biological Chemistry | volume = 265 | issue = 13 | pages = 7548–51 | date = May 1990 | pmid = 2332441 | doi =  }}
*{{cite journal | author=Carlsson SR, Fukuda M |title=The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones. |journal=J. Biol. Chem. |volume=265 |issue= 33 |pages= 20488-95 |year= 1990 |pmid= 2243102 |doi=  }}
* {{cite journal | vauthors = Carlsson SR, Fukuda M | title = Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement | journal = The Journal of Biological Chemistry | volume = 264 | issue = 34 | pages = 20526–31 | date = Dec 1989 | pmid = 2584229 | doi =  }}
*{{cite journal | author=Mattei MG, Matterson J, Chen JW, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 13 |pages= 7548-51 |year= 1990 |pmid= 2332441 |doi=  }}
* {{cite journal | vauthors = Mane SM, Marzella L, Bainton DF, Holt VK, Cha Y, Hildreth JE, August JT | title = Purification and characterization of human lysosomal membrane glycoproteins | journal = Archives of Biochemistry and Biophysics | volume = 268 | issue = 1 | pages = 360–78 | date = Jan 1989 | pmid = 2912382 | doi = 10.1016/0003-9861(89)90597-3 }}
*{{cite journal | author=Carlsson SR, Fukuda M |title=Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement. |journal=J. Biol. Chem. |volume=264 |issue= 34 |pages= 20526-31 |year= 1990 |pmid= 2584229 |doi=  }}
* {{cite journal | vauthors = Viitala J, Carlsson SR, Siebert PD, Fukuda M | title = Molecular cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr approximately equal to 120,000 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 85 | issue = 11 | pages = 3743–7 | date = Jun 1988 | pmid = 3131762 | pmc = 280294 | doi = 10.1073/pnas.85.11.3743 }}
*{{cite journal | author=Mane SM, Marzella L, Bainton DF, ''et al.'' |title=Purification and characterization of human lysosomal membrane glycoproteins. |journal=Arch. Biochem. Biophys. |volume=268 |issue= 1 |pages= 360-78 |year= 1989 |pmid= 2912382 |doi= }}
* {{cite journal | vauthors = Howe CL, Granger BL, Hull M, Green SA, Gabel CA, Helenius A, Mellman I | title = 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 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 85 | issue = 20 | pages = 7577–81 | date = Oct 1988 | pmid = 3174652 | pmc = 282235 | doi = 10.1073/pnas.85.20.7577 }}
*{{cite journal | author=Viitala J, Carlsson SR, Siebert PD, Fukuda M |title=Molecular cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr approximately equal to 120,000. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3743-7 |year= 1988 |pmid= 3131762 |doi= }}
* {{cite journal | vauthors = Fukuda M, Viitala J, Matteson J, Carlsson SR | title = Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences | journal = The Journal of Biological Chemistry | volume = 263 | issue = 35 | pages = 18920–8 | date = Dec 1988 | pmid = 3198605 | doi =  }}
*{{cite journal | author=Howe CL, Granger BL, Hull M, ''et al.'' |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 20 |pages= 7577-81 |year= 1988 |pmid= 3174652 |doi= }}
* {{cite journal | vauthors = Ohno H, Stewart J, Fournier MC, Bosshart H, Rhee I, Miyatake S, Saito T, Gallusser A, Kirchhausen T, Bonifacino JS | title = Interaction of tyrosine-based sorting signals with clathrin-associated proteins | journal = Science | volume = 269 | issue = 5232 | pages = 1872–5 | date = Sep 1995 | pmid = 7569928 | doi = 10.1126/science.7569928 }}
*{{cite journal | author=Fukuda M, Viitala J, Matteson J, Carlsson SR |title=Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18920-8 |year= 1989 |pmid= 3198605 |doi=  }}
* {{cite journal | vauthors = Carlsson SR, Lycksell PO, Fukuda M | title = Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2 | journal = Archives of Biochemistry and Biophysics | volume = 304 | issue = 1 | pages = 65–73 | date = Jul 1993 | pmid = 8323299 | doi = 10.1006/abbi.1993.1322 }}
*{{cite journal | author=Ohno H, Stewart J, Fournier MC, ''et al.'' |title=Interaction of tyrosine-based sorting signals with clathrin-associated proteins. |journal=Science |volume=269 |issue= 5232 |pages= 1872-5 |year= 1995 |pmid= 7569928 |doi= }}
* {{cite journal | vauthors = Sawada R, Jardine KA, Fukuda M | title = 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 | journal = The Journal of Biological Chemistry | volume = 268 | issue = 12 | pages = 9014–22 | date = Apr 1993 | pmid = 8517882 | doi =  }}
*{{cite journal | author=Carlsson SR, Lycksell PO, Fukuda M |title=Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2. |journal=Arch. Biochem. Biophys. |volume=304 |issue= 1 |pages= 65-73 |year= 1993 |pmid= 8323299 |doi= 10.1006/abbi.1993.1322 }}
* {{cite journal | vauthors = Rohrer J, Schweizer A, Russell D, Kornfeld S | title = The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane | journal = The Journal of Cell Biology | volume = 132 | issue = 4 | pages = 565–76 | date = Feb 1996 | pmid = 8647888 | pmc = 2199866 | doi = 10.1083/jcb.132.4.565 }}
*{{cite journal | author=Sawada R, Jardine KA, Fukuda M |title=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. |journal=J. Biol. Chem. |volume=268 |issue= 12 |pages= 9014-22 |year= 1993 |pmid= 8517882 |doi=  }}
* {{cite journal | vauthors = Höning S, Sandoval IV, von Figura K | title = A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3 | journal = The EMBO Journal | volume = 17 | issue = 5 | pages = 1304–14 | date = Aug 1998 | pmid = 9482728 | pmc = 1170479 | doi = 10.1093/emboj/17.5.1304 }}
*{{cite journal | author=Rohrer J, Schweizer A, Russell D, Kornfeld S |title=The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. |journal=J. Cell Biol. |volume=132 |issue= 4 |pages= 565-76 |year= 1996 |pmid= 8647888 |doi= }}
* {{cite journal | vauthors = Furuta K, Yang XL, Chen JS, Hamilton SR, August JT | title = Differential expression of the lysosome-associated membrane proteins in normal human tissues | journal = Archives of Biochemistry and Biophysics | volume = 365 | issue = 1 | pages = 75–82 | date = May 1999 | pmid = 10222041 | doi = 10.1006/abbi.1999.1147 }}
*{{cite journal | author=Höning S, Sandoval IV, von Figura K |title=A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. |journal=EMBO J. |volume=17 |issue= 5 |pages= 1304-14 |year= 1998 |pmid= 9482728 |doi= 10.1093/emboj/17.5.1304 }}
* {{cite journal | vauthors = Raposo G, Moore M, Innes D, Leijendekker R, Leigh-Brown A, Benaroch P, Geuze H | title = Human macrophages accumulate HIV-1 particles in MHC II compartments | journal = Traffic | volume = 3 | issue = 10 | pages = 718–29 | date = Oct 2002 | pmid = 12230470 | doi = 10.1034/j.1600-0854.2002.31004.x }}
*{{cite journal | author=Furuta K, Yang XL, Chen JS, ''et al.'' |title=Differential expression of the lysosome-associated membrane proteins in normal human tissues. |journal=Arch. Biochem. Biophys. |volume=365 |issue= 1 |pages= 75-82 |year= 1999 |pmid= 10222041 |doi= 10.1006/abbi.1999.1147 }}
* {{cite journal | vauthors = Zhang H, Li XJ, Martin DB, Aebersold R | title = Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry | journal = Nature Biotechnology | volume = 21 | issue = 6 | pages = 660–6 | date = Jun 2003 | pmid = 12754519 | doi = 10.1038/nbt827 }}
*{{cite journal | author=Raposo G, Moore M, Innes D, ''et al.'' |title=Human macrophages accumulate HIV-1 particles in MHC II compartments. |journal=Traffic |volume=3 |issue= 10 |pages= 718-29 |year= 2003 |pmid= 12230470 |doi= }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
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==External links==
== External links ==
* {{MeshName|LAMP1+protein,+human}}
* {{MeshName|LAMP1+protein,+human}}


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[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
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Latest revision as of 11:30, 9 January 2019

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SpeciesHumanMouse
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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).

File:HeLa cells showin Lamp1 in red, vimentin in green and DNA in blue.jpg
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.

Lysosomal-associated membrane protein 1 is a glycoprotein from a family of Lysosome-associated membrane glycoproteins.[1] The LAMP-1 glycoprotein is a type I transmembrane protein[2] which is expressed at high or medium levels in at least 76 different normal tissue cell types.[3] It resides primarily across lysosomal membranes,[4] and functions to provide selectins with carbohydrate ligands.[1] CD107a has also been shown to be a marker of degranulation on lymphocytes such as CD8+ and NK cells.[5] 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[2] exposed to the cytoplasm.[4] The extracytoplasmic region contains a hinge-like structure which can form disulphide bridges homologous to those observed in human immunoglobulin A.[4] Other characteristics of the structure of the LAMP-1 glycoproteins include:

Function

LAMP1 and LAMP2 glycoproteins comprise 50% of all lysosomal membrane proteins,[2] and are thought to be responsible in part for maintaining lysosomal integrity, pH and catabolism.[2][7] The expression of LAMP1 and LAMP2 glycoproteins are linked, as deficiencies in LAMP1 gene will lead to increased expression of LAMP2 glycoproteins.[7] The two are therefore thought to share similar functions in vivo.[2] 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,[2][7] the LAMP1/LAMP2 double deficient phenotype leads to embryonic lethality.[7]

Although the LAMP1 glycoproteins primarily reside across lysosomal membranes, in certain cases they can be expressed across the plasma membrane of the cell.[7] Expression of LAMP1 at the cell surface can occur due to lysosomal fusion with the cell membrane.[8] Cell surface expression of LAMP1 can serve as a ligand for selectins[9][10] and help mediate cell-cell adhesion.[11] Accordingly, cell surface expression of LAMP1 is seen in cells with migratory or invasive functions, such as cytotoxic T cells, platelets and macrophages.[12] Cell surface expression of LAMP1 and LAMP2 is also often seen in cancer cells,[12][13] particularly cancers with high metastatic potential, such as colon carcinoma and melanoma,[12] and has been shown to correlate with their metastatic potential.[7]

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,[14][15] colon cancer[12][13] and melanoma.[12][13] The structure of LAMP1 correlates with differentiation[4][16] and metastatic potential[7] of tumor cells as it is thought to help mediate cell-cell adhesion [13] and migration.[11][14] 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.[13]

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

See also

References

  1. ↑ 1.0 1.1 "LAMP1 lysosomal-associated membrane protein 1". Entrez Gene.
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 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.
  3. ↑ "LAMP1". The Human Protein Atlas.
  4. ↑ 4.0 4.1 4.2 4.3 4.4 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.
  5. ↑ "LAMP1 - lysosomal-associated membrane protein1". Wikigenes.
  6. ↑ 6.0 6.1 6.2 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.
  7. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 7.7 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.
  8. ↑ 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.
  9. ↑ 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.
  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. PMID 8517882.
  11. ↑ 11.0 11.1 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.
  12. ↑ 12.0 12.1 12.2 12.3 12.4 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.
  13. ↑ 13.0 13.1 13.2 13.3 13.4 13.5 13.6 13.7 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. 75 (1): 105–111. doi:10.1002/(sici)1097-0215(19980105)75:1<105::aid-ijc16>3.0.co;2-f. PMID 9426697.
  14. ↑ 14.0 14.1 14.2 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.
  15. ↑ 15.0 15.1 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.
  16. ↑ 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

External links

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

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