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词条 JAM2
释义

  1. Function

  2. Interactions

  3. References

  4. Further reading

  5. External links

{{Infobox_gene}}

Junctional adhesion molecule B is a protein that in humans is encoded by the JAM2 gene.[1][2][3] JAM2 has also been designated as CD322 (cluster of differentiation 322).

Function

Tight junctions represent one mode of cell-to-cell adhesion in endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. It acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.[3]

It is purported to promote lymphocyte transendothelial migration.[4] It might also be involved with endothelial cell polarity, by associating to cell polarity protein PAR-3, together with JAM3.[5]

Interactions

JAM2 has been shown to interact with PARD3.[5]

It also interacts with the integrin dimer VLA-4 (also called α4β1).[6]

References

1. ^{{cite journal |vauthors=Palmeri D, van Zante A, Huang CC, Hemmerich S, Rosen SD | title = Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells | journal = J Biol Chem | volume = 275 | issue = 25 | pages = 19139–45 |date=Aug 2000 | pmid = 10779521 | doi = 10.1074/jbc.M003189200 }}
2. ^{{cite journal |vauthors=Cunningham SA, Arrate MP, Rodriguez JM, Bjercke RJ, Vanderslice P, Morris AP, Brock TA | title = A novel protein with homology to the junctional adhesion molecule. Characterization of leukocyte interactions | journal = J Biol Chem | volume = 275 | issue = 44 | pages = 34750–6 |date=Nov 2000 | pmid = 10945976 | doi = 10.1074/jbc.M002718200 }}
3. ^{{cite web | title = Entrez Gene: JAM2 junctional adhesion molecule 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58494| accessdate = }}
4. ^{{cite journal |vauthors=Johnson-Léger CA, Aurrand-Lions M, Beltraminelli N, Fasel N, Imhof BA | title = Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte transendothelial migration | journal = Blood | volume = 100 | issue = 7 | pages = 2479–86 |date=October 2002 | pmid = 12239159 | doi = 10.1182/blood-2001-11-0098 }}
5. ^{{cite journal |vauthors=Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D | title = The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity | journal = J. Cell Sci. | volume = 116 | issue = Pt 19 | pages = 3879–91 |date=October 2003 | pmid = 12953056 | doi = 10.1242/jcs.00704 }}
6. ^{{cite journal |vauthors=Cunningham SA, Rodriguez JM, Arrate MP, Tran TM, Brock TA | title = JAM2 interacts with alpha4beta1. Facilitation by JAM3 | journal = J. Biol. Chem. | volume = 277 | issue = 31 | pages = 27589–92 |date=August 2002 | pmid = 12070135 | doi = 10.1074/jbc.C200331200 }}

Further reading

{{refbegin | 2}}
  • {{cite journal | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327–34 |year= 2003 |pmid= 12810109 |doi=10.1016/S1471-4906(03)00117-0 }}
  • {{cite journal | author=Bazzoni G |title=The JAM family of junctional adhesion molecules. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 5 |pages= 525–30 |year= 2004 |pmid= 14519386 |doi=10.1016/S0955-0674(03)00104-2 }}
  • {{cite journal |vauthors=Hattori M, Fujiyama A, Taylor TD, etal |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311–9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
  • {{cite journal |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000 | pmc=310948 }}
  • {{cite journal |vauthors=Arrate MP, Rodriguez JM, Tran TM, etal |title=Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45826–32 |year= 2002 |pmid= 11590146 |doi= 10.1074/jbc.M105972200 }}
  • {{cite journal |vauthors=Liang TW, Chiu HH, Gurney A, etal |title=Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. |journal=J. Immunol. |volume=168 |issue= 4 |pages= 1618–26 |year= 2002 |pmid= 11823489 |doi= 10.4049/jimmunol.168.4.1618}}
  • {{cite journal |vauthors=Gardiner K, Slavov D, Bechtel L, Davisson M |title=Annotation of human chromosome 21 for relevance to Down syndrome: gene structure and expression analysis. |journal=Genomics |volume=79 |issue= 6 |pages= 833–43 |year= 2002 |pmid= 12036298 |doi= 10.1006/geno.2002.6782 }}
  • {{cite journal |vauthors=Cunningham SA, Rodriguez JM, Arrate MP, etal |title=JAM2 interacts with alpha4beta1. Facilitation by JAM3. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27589–92 |year= 2002 |pmid= 12070135 |doi= 10.1074/jbc.C200331200 }}
  • {{cite journal |vauthors=Aurrand-Lions M, Johnson-Leger C, Lamagna C, etal |title=Junctional adhesion molecules and interendothelial junctions. |journal=Cells Tissues Organs (Print) |volume=172 |issue= 3 |pages= 152–60 |year= 2004 |pmid= 12476045 |doi=10.1159/000066967 }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
  • {{cite journal |vauthors=Ebnet K, Aurrand-Lions M, Kuhn A, etal |title=The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. |journal=J. Cell Sci. |volume=116 |issue= Pt 19 |pages= 3879–91 |year= 2004 |pmid= 12953056 |doi= 10.1242/jcs.00704 |url=https://archive-ouverte.unige.ch/unige:11233/ATTACHMENT01 }}
  • {{cite journal |vauthors=Clark HF, Gurney AL, Abaya E, etal |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 }}
  • {{cite journal |vauthors=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819–24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 | pmc=2286551 }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 }}
  • {{cite journal |vauthors=Liu T, Qian WJ, Gritsenko MA, etal |title=Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070–80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 | pmc=1850943 }}
{{refend}}

External links

  • {{MeshName|JAM2+protein,+human}}
{{NLM content}}{{Clusters of differentiation}}{{membrane-protein-stub}}

1 : Clusters of differentiation

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