ICAM1

ICAM1
Рәвеш
Нинди таксонда бар H. sapiens[1]
Кодлаучы ген ICAM-1[d][1]
Молекуляр функция virus receptor activity[d][2], protein-containing complex binding[d][3][2], integrin binding[d][4][3][5], связывание с белками плазмы[d][6][7][8][…], transmembrane signaling receptor activity[d][9], integrin binding[d][10][2][11][…] һәм signaling receptor activity[d][9]
Күзәнәк компоненты мембрана өлеше[d][2], мембрана[d][3][3][12], фокальные контакты[d][13], күзәнәк мембранасы[d][2][14][2], күзәнәк мембранасы өлеше[d][15], күзәнәк өслеге[d][3][16][17], иммунологик синапс[d][2], липидный рафт[d][2], экзосома[d][18][19][20], наружная сторона клеточной мембраны[d][2], күзәнәк тышындагы мохит[d][2][21], внеклеточный матрикс[d][22], күзәнәк мембранасы өлеше[d][9][23], фокальные контакты[d][24], күзәнәк өслеге[d][2][25][26], мембрана[d][2][2][27], collagen-containing extracellular matrix[d][28] һәм экзосома[d][29][30][31]
Биологик процесс leukocyte cell-cell adhesion[d][32][2], response to ionizing radiation[d][2], establishment of endothelial barrier[d][33], negative regulation of endothelial cell apoptotic process[d][34], cellular response to organic substance[d][2], heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules[d][32], response to amino acid[d][2], response to hypoxia[d][2], positive regulation of actin filament polymerization[d][2], response to organic cyclic compound[d][2], T cell antigen processing and presentation[d][2], establishment of Sertoli cell barrier[d][2], response to sulfur dioxide[d][2], response to copper ion[d][2], interferon-gamma-mediated signaling pathway[d][2], positive regulation of nitric oxide biosynthetic process[d][2], response to amphetamine[d][2], cellular response to tumor necrosis factor[d][2], regulation of leukocyte mediated cytotoxicity[d][35], T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell[d][32], extracellular matrix organization[d][2], acute inflammatory response to antigenic stimulus[d][2], ишетү[d][2], cellular response to alkaloid[d][2], response to gonadotropin[d][2], positive regulation of cellular extravasation[d][36], positive regulation of GTPase activity[d][2], response to lipopolysaccharide[d][2], regulation of cell adhesion[d][2], агрегация клеток[d][3][3][37], cell adhesion mediated by integrin[d][2], positive regulation of NF-kappaB transcription factor activity[d][2], negative regulation of extrinsic apoptotic signaling pathway via death domain receptors[d][34], positive regulation of vasoconstriction[d][2], cellular response to interleukin-1[d][2], cellular response to nutrient levels[d][2], negative regulation of calcium ion transport[d][2], regulation of cell shape[d][2], membrane to membrane docking[d][38], positive regulation of peptidyl-tyrosine phosphorylation[d][2], ovarian follicle development[d][2], regulation of immune response[d][2], positive regulation of ERK1 and ERK2 cascade[d][34], regulation of ruffle assembly[d][2], viral entry into host cell[d][2], response to ethanol[d][2], вирусный процесс[d][2], cellular response to lipopolysaccharide[d][2], cellular response to hypoxia[d][2], leukocyte migration[d][38], cellular response to glucose stimulus[d][2], response to insulin[d][2], cellular response to interferon-gamma[d][2], cellular response to interleukin-6[d][2], cellular response to dexamethasone stimulus[d][2], establishment of endothelial intestinal barrier[d][2], positive regulation of leukocyte adhesion to vascular endothelial cell[d][2], cellular response to leukemia inhibitory factor[d][2], cell-cell adhesion[d][2][2], агрегация клеток[d][2][2][39][…], cytokine-mediated signaling pathway[d][2], T cell extravasation[d][2] һәм cellular response to amyloid-beta[d][40]
Изображение Gene Atlas
 ICAM1 Викиҗыентыкта

ICAM1 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[41][42]

Искәрмәләр

  1. ↑ 1,0 1,1 UniProt
  2. ↑ 2,00 2,01 2,02 2,03 2,04 2,05 2,06 2,07 2,08 2,09 2,10 2,11 2,12 2,13 2,14 2,15 2,16 2,17 2,18 2,19 2,20 2,21 2,22 2,23 2,24 2,25 2,26 2,27 2,28 2,29 2,30 2,31 2,32 2,33 2,34 2,35 2,36 2,37 2,38 2,39 2,40 2,41 2,42 2,43 2,44 2,45 2,46 2,47 2,48 2,49 2,50 2,51 2,52 2,53 2,54 2,55 2,56 2,57 2,58 2,59 2,60 2,61 2,62 2,63 2,64 2,65 GOA
  3. ↑ 3,0 3,1 3,2 3,3 3,4 3,5 3,6 GOA
  4. ↑ Holness C. L., Needham L. A., Gatter K. C. et al. Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytes // Nature / M. Skipper — NPG, Springer Science+Business Media, 1992. — ISSN 1476-4687; 0028-0836 — doi:10.1038/360481A0 — PMID:1448173
  5. ↑ Chiang Y., Lee F. S. CBAP functions as a novel component in chemokine-induced ZAP70-mediated T-cell adhesion and migration // PLOS ONE / PLOS ONE Editors — PLoS, 2013. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0061761 — PMID:23620790
  6. ↑ Madrid F. S., Rocha-Perugini V., Gonzalez-Granado J. M. et al. CD81 controls sustained T cell activation signaling and defines the maturation stages of cognate immunological synapses // Mol. Cell. Biol. — ASM, 2013. — ISSN 0270-7306; 1098-5549; 1067-8824 — doi:10.1128/MCB.00302-13 — PMID:23858057
  7. ↑ Gewirtz A. CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia, CD98 and Intracellular Adhesion Molecule I Regulate the Activity of Amino Acid Transporter LAT-2 in Polarized Intestinal Epithelia // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2003. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M302777200 — PMID:12716892
  8. ↑ Joachimiak A. Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation // Cell — Cell Press, Elsevier, 2003. — ISSN 0092-8674; 1097-4172 — doi:10.1016/S0092-8674(02)01257-6 — PMID:12526797
  9. ↑ 9,0 9,1 9,2 McClelland A. The major human rhinovirus receptor is ICAM-1 // Cell — Cell Press, Elsevier, 1989. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(89)90688-0 — PMID:2538243
  10. ↑ Holness C. L., Needham L. A., Gatter K. C. et al. Molecular cloning of ICAM-3, a third ligand for LFA-1, constitutively expressed on resting leukocytes // Nature / M. Skipper — NPG, Springer Science+Business Media, 1992. — ISSN 1476-4687; 0028-0836 — doi:10.1038/360481A0 — PMID:1448173
  11. ↑ Chiang Y., Lee F. S. CBAP functions as a novel component in chemokine-induced ZAP70-mediated T-cell adhesion and migration // PLOS ONE / PLOS ONE Editors — PLoS, 2013. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0061761 — PMID:23620790
  12. ↑ Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom. — Wiley, 2010. — ISSN 1076-5174; 1096-9888 — doi:10.1002/JMS.1696 — PMID:19946888
  13. ↑ Waterman C., Yates J. R. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  14. ↑ Dustin M. L. Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families // Cell — Cell Press, Elsevier, 1988. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(88)90434-5 — PMID:3349522
  15. ↑ McClelland A. The major human rhinovirus receptor is ICAM-1 // Cell — Cell Press, Elsevier, 1989. — ISSN 0092-8674; 1097-4172 — doi:10.1016/0092-8674(89)90688-0 — PMID:2538243
  16. ↑ Robinson C. M. Mycobacterium tuberculosis infection of human dendritic cells decreases integrin expression, adhesion and migration to chemokines // Immunology — Wiley-Blackwell, Wiley, 2014. — ISSN 0019-2805; 1365-2567 — doi:10.1111/IMM.12164 — PMID:23981064
  17. ↑ Teckchandani A., Toida N., Goodchild J. et al. Quantitative proteomics identifies a Dab2/integrin module regulating cell migration // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2009. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200812160 — PMID:19581412
  18. ↑ Atay S. Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells // Exp. Cell. Res. — Academic Press, Elsevier, 2011. — ISSN 0014-4827; 1090-2422 — doi:10.1016/J.YEXCR.2011.01.014 — PMID:21276792
  19. ↑ Buschow S. I., Stoorvogel W., Wauben M. MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis // Immunology & Cell Biology — Wiley, 2010. — ISSN 0818-9641; 1440-1711 — doi:10.1038/ICB.2010.64 — PMID:20458337
  20. ↑ Pisitkun T., Tchapyjnikov D., Knepper M. A. Large-scale proteomics and phosphoproteomics of urinary exosomes // Journal of the American Society of Nephrology / J. Briggs — American Society of Nephrology, 2008. — ISSN 1046-6673; 1533-3450 — doi:10.1681/ASN.2008040406 — PMID:19056867
  21. ↑ Augustin H. G. Circulating endothelial cell adhesion molecules as diagnostic markers for the early identification of pregnant women at risk for development of preeclampsia // American Journal of Obstetrics and Gynecology — Elsevier, 1997. — ISSN 0002-9378; 1097-6868; 1085-8709 — doi:10.1016/S0002-9378(97)70213-8 — PMID:9290466
  22. ↑ Mayr M., Iozzo R. V., Barallobre-Barreiro J. et al. Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation // Circulation — Lippincott Williams & Wilkins, 2016. — ISSN 0009-7322; 1524-4539 — doi:10.1161/CIRCULATIONAHA.115.016423 — PMID:27559042
  23. ↑ Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
  24. ↑ Waterman C., Yates J. R. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
  25. ↑ Robinson C. M. Mycobacterium tuberculosis infection of human dendritic cells decreases integrin expression, adhesion and migration to chemokines // Immunology — Wiley-Blackwell, Wiley, 2014. — ISSN 0019-2805; 1365-2567 — doi:10.1111/IMM.12164 — PMID:23981064
  26. ↑ Teckchandani A., Toida N., Goodchild J. et al. Quantitative proteomics identifies a Dab2/integrin module regulating cell migration // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2009. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200812160 — PMID:19581412
  27. ↑ Lippert D. Defining the membrane proteome of NK cells // J. Mass Spectrom. — Wiley, 2010. — ISSN 1076-5174; 1096-9888 — doi:10.1002/JMS.1696 — PMID:19946888
  28. ↑ Mayr M., Iozzo R. V., Barallobre-Barreiro J. et al. Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation // Circulation — Lippincott Williams & Wilkins, 2016. — ISSN 0009-7322; 1524-4539 — doi:10.1161/CIRCULATIONAHA.115.016423 — PMID:27559042
  29. ↑ Atay S. Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells // Exp. Cell. Res. — Academic Press, Elsevier, 2011. — ISSN 0014-4827; 1090-2422 — doi:10.1016/J.YEXCR.2011.01.014 — PMID:21276792
  30. ↑ Buschow S. I., Stoorvogel W., Wauben M. MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis // Immunology & Cell Biology — Wiley, 2010. — ISSN 0818-9641; 1440-1711 — doi:10.1038/ICB.2010.64 — PMID:20458337
  31. ↑ Pisitkun T., Tchapyjnikov D., Knepper M. A. Large-scale proteomics and phosphoproteomics of urinary exosomes // Journal of the American Society of Nephrology / J. Briggs — American Society of Nephrology, 2008. — ISSN 1046-6673; 1533-3450 — doi:10.1681/ASN.2008040406 — PMID:19056867
  32. ↑ 32,0 32,1 32,2 Dustin M. L. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1 // Nature / M. Skipper — NPG, Springer Science+Business Media, 1989. — ISSN 1476-4687; 0028-0836 — doi:10.1038/341619A0 — PMID:2477710
  33. ↑ Aranda J. F., Millán J., Kremer L. et al. MYADM controls endothelial barrier function through ERM-dependent regulation of ICAM-1 expression // Mol. Biol. Cell, — American Society for Cell Biology, 2013. — ISSN 1059-1524; 1939-4586; 1044-2030 — doi:10.1091/MBC.E11-11-0914 — PMID:23264465
  34. ↑ 34,0 34,1 34,2 E Pluskota, S E D'Souza Fibrinogen interactions with ICAM-1 (CD54) regulate endothelial cell survival // FEBS J. — Wiley-Blackwell, 2000. — ISSN 1742-464X; 1742-4658 — doi:10.1046/J.1432-1327.2000.01520.X — PMID:10903502
  35. ↑ Yokomori H. Expression of adhesion molecules on mature cholangiocytes in canal of Hering and bile ductules in wedge biopsy samples of primary biliary cirrhosis // World J. Gastroenterol. — Baishideng Publishing Group, 2005. — ISSN 1007-9327; 2219-2840 — doi:10.3748/WJG.V11.I28.4382 — PMID:16038038
  36. ↑ Greenwood J., Couraud P., Lyck R. et al. Intracellular domain of brain endothelial intercellular adhesion molecule-1 is essential for T lymphocyte-mediated signaling and migration // J. Immunol. — Baltimore: 2003. — ISSN 0022-1767; 1550-6606 — doi:10.4049/JIMMUNOL.171.4.2099 — PMID:12902516
  37. ↑ Ottoboni L., Meregalli M., Torrente Y. et al. VCAM-1 expression on dystrophic muscle vessels has a critical role in the recruitment of human blood-derived CD133+ stem cells after intra-arterial transplantation // Blood — American Society of Hematology, Elsevier, 2006. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2006-04-018564 — PMID:16809613
  38. ↑ 38,0 38,1 Yáñez-Mó M., Serrador J. M., Montoya M. C. et al. Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2002. — 13 p. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200112126 — PMID:12082081
  39. ↑ Ottoboni L., Meregalli M., Torrente Y. et al. VCAM-1 expression on dystrophic muscle vessels has a critical role in the recruitment of human blood-derived CD133+ stem cells after intra-arterial transplantation // Blood — American Society of Hematology, Elsevier, 2006. — ISSN 0006-4971; 1528-0020 — doi:10.1182/BLOOD-2006-04-018564 — PMID:16809613
  40. ↑ R Giri, Y Shen, M Stins et al. beta-amyloid-induced migration of monocytes across human brain endothelial cells involves RAGE and PECAM-1. // American Journal of Physiology-Cell Physiology: Cell Physiology — 2000. — ISSN 0363-6143; 1522-1563 — doi:10.1152/AJPCELL.2000.279.6.C1772 — PMID:11078691
  41. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланган. 18 сентябрь, 2017 тикшерелгән.
  42. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)

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