title: Integrin triplets of marine sponges in the murine and human MHCI-CD8 interface and in the interface of human neural receptor heteromers and subunits.
abstract: Based on our theory, main triplets of amino acid residues have been discovered in cell-adhesion receptors (integrins) of marine sponges, which participate as homologies in the interface between two major immune molecules, MHC class I (MHCI) and CD8αβ. They appear as homologies also in several human neural receptor heteromers and subunits. The obtained results probably mean that neural and immune receptors also utilize these structural integrin triplets to form heteromers and ion channels, which are required for a tuned and integrated intracellular and intercellular communication and a communication between cells and the extracellular matrix with an origin in sponges, the oldest multicellular animals.
authors.affiliation: Russian Academy of Sciences, St. Petersburg Institute for Informatics and Automation, Saint Petersburg, Russia.
authors.forename: Alexander O
authors.initials: AO
authors.lastname: Tarakanov
authors.forename: Kjell G
authors.initials: KG
authors.lastname: Fuxe
keywords: Marine sponges; Neural receptor-receptor interactions; Receptor interface; Triplet homologies
references.citation: Mol Biol Evol. 1997 Apr;14(4):391-8
references.pmid: 9100369
references.citation: Biol Psychiatry. 2012 Jan 1;71(1):84-91
references.pmid: 22035699
references.citation: J Mol Neurosci. 2010 Jun;41(2):294-303
references.pmid: 19960372
references.citation: J Neural Transm (Vienna). 2009 Aug;116(8):989-94
references.pmid: 19229585
references.citation: Curr Med Chem. 2012;19(3):356-63
references.pmid: 22335512
references.citation: Nature. 1997 Jun 5;387(6633):630-4
references.pmid: 9177355
references.citation: Biochem Biophys Res Commun. 2010 Mar 19;393(4):767-72
references.pmid: 20171159
references.citation: Biochem Soc Trans. 2009 Aug;37(Pt 4):751-5
references.pmid: 19614588
references.citation: J Neurosci. 2012 May 2;32(18):6295-303
references.pmid: 22553035
references.citation: J Recept Signal Transduct Res. 2012 Aug;32(4):202-8
references.pmid: 22712841
references.citation: Science. 1984 Sep 21;225(4668):1335-45
references.pmid: 6382611
references.citation: Cell Tissue Res. 1997 Sep;289(3):383-95
references.pmid: 9232818
references.citation: J Neural Transm Suppl. 2003;(65):1-28
references.pmid: 12946046
references.citation: IUBMB Life. 2011 Jul;63(7):463-72
references.pmid: 21698749
references.citation: J Neural Transm (Vienna). 2012 May;119(5):517-23
references.pmid: 22068823
references.citation: J Immunol. 2009 Aug 15;183(4):2554-64
references.pmid: 19625641
references.citation: J Mol Neurosci. 2012 Mar;46(3):616-21
references.pmid: 21932037
references.citation: J Mol Neurosci. 2011 Jul;44(3):173-7
references.pmid: 21416272
references.citation: Biol Chem Hoppe Seyler. 1994 Sep;375(9):583-8
references.pmid: 7840899
references.citation: J Mol Neurosci. 2012 Sep;48(1):154-60
references.pmid: 22573093
references.citation: Cell Tissue Res. 2010 Jan;339(1):269-80
references.pmid: 19693543
references.citation: Nat Neurosci. 2001 Dec;4(12):1207-16
references.pmid: 11704764
references.citation: Biochem Biophys Res Commun. 2011 Jun 17;409(4):764-8
references.pmid: 21621521
references.citation: J Mol Endocrinol. 2007 Mar;38(3):365-76
references.pmid: 17339399
references.citation: J Neurosci. 2011 Nov 9;31(45):16177-84
references.pmid: 22072669
references.citation: Trends Pharmacol Sci. 1999 Oct;20(10):396-9
references.pmid: 10498952