R Koskinen

University of Turku, Turku, Western Finland, Finland

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Publications (10)27.15 Total impact

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    ABSTRACT: CD4 has a central role in thymocyte differentiation and cell-mediated immunity. We isolated and analyzed chicken CD4. The gene spans 11.5 kb and is composed of ten exons. The promoter is TATA-less and similar to the mouse and human CD4 promoters, with two transcription start sites as determined by 5'RACE analysis. In general the introns are short, although the 5'untranslated region includes a large intron of 5.6 kb containing binding sites of the putative CD4 silencer. The single-strand conformation polymorphism technique was used to identify a polymorphism to map the gene, which lies on chicken Chromosome 1 in a position showing conserved synteny to mouse and human. This is the first report describing the organization of CD4 from a non-mammalian species. The structure and localization of chicken CD4 and many sequence motifs important in its regulation have remained conserved during evolution.
    Immunogenetics 11/2002; 54(7):520-5. · 2.89 Impact Factor
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    ABSTRACT: CD5 is a transmembrane glycoprotein on all T cells and on a subpopulation of B cells. Based on the analysis of chicken CD5-cDNA we have previously shown that the structure of the CD5 protein is conserved between species. Here we report the isolation and chromosomal mapping of the chicken CD5 gene. The gene spans 3.4 kb and is extremely compact with a high GC-nucleotide content. There are 10 exons and the introns are spliced out similarly to those in the human CD5 gene. Each of the three extracellular scavenger receptor cysteine-rich (SRCR) domains is encoded as an exon of its own, as is the proline-rich hinge region that separates the first two membrane-distal SRCR domains. The fluorescence in situ hybridization (FISH) technique was used to map the gene to chromosome five. This is the first report describing the organization of the CD5 gene from a nonmammalian species.
    Scandinavian Journal of Immunology 07/2001; 54(1-2):141-5. · 2.20 Impact Factor
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    ABSTRACT: We have cloned and sequenced the first nonmammalian CD4 cDNA from the chicken using the COS cell expression method. Chicken CD4 contains four extracellular Ig domains that, in analogy to mammalian CD4, are in the order V, C2, V, and C2. The molecule is 24% identical with both human and mouse sequences. The extracellular domains were modeled using human and rat CD4 crystal structures as templates. In the first domain there are two extra Cys residues that are at suitable distance to form an intra-beta-sheet disulfide bridge in addition to the canonical one in the V domain. The region responsible for the interaction with MHC class II is relatively nonconserved in chicken. However, there are positively charged amino acids in the C" region of the N-terminal domain that may mediate the association to the negatively charged residues of the MHC class II beta-chain. Molecular modeling also implies that the membrane-proximal domain mediates dimerization of chicken CD4 in a similar way as it does for human CD4. Furthermore, the cytoplasmic tail is highly conserved, containing the protein tyrosine kinase p56lck recognition site that is preceded by an adjacent di-leucine motif for the internalization of the molecule. Interestingly, there are no Ser residues in the cytoplasmic part, which may explain the slow down-regulation of chicken CD4 after phorbol ester stimulation.
    The Journal of Immunology 05/1999; 162(7):4115-21. · 5.52 Impact Factor
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    ABSTRACT: The chicken CD5 cDNA was isolated by COS cell expression cloning utilizing a novel mAb 2-191. The cDNA contains a 1422-nucleotide open reading frame encoding a mature protein with 32% and 30% identity to mouse and human CD5 polypeptides, respectively. The molecule consists of a 330-amino acid extracellular region with three repeats of the scavenger receptor cysteine-rich domain, a 29-amino acid hydrophobic transmembrane domain, and a 93-amino acid cytoplasmic tail. The cytoplasmic region contains motifs that are highly conserved between species, including several potential phosphorylation sites. The chicken CD5 is a 64-kDa phosphorylated glycoprotein with a protein core of 57 kDa as determined by immunoprecipitation and SDS-PAGE analysis. Alphabeta T cells express a homogeneously high level of CD5, whereas low or intermediate CD5 expression on gammadelta T cells depends on their tissue location. In contrast to human and mouse, CD5 is found at low levels on all chicken B cells. The high conservation of structural features, as well as signaling motifs, implies a conserved role for CD5 both in lymphocyte development and function.
    The Journal of Immunology 06/1998; 160(10):4943-50. · 5.52 Impact Factor
  • Immunology Letters 05/1997; 56:90-90. · 2.34 Impact Factor
  • Developmental & Comparative Immunology 03/1997; 21(2):240-240. · 3.24 Impact Factor
  • Developmental & Comparative Immunology 02/1997; 21(2):240-240. · 3.24 Impact Factor
  • Scandinavian Journal of Immunology. 01/1996; 43:694.
  • M Luhtala, R Koskinen, P Toivanen, O Vainio
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    ABSTRACT: CD8 is a heterodimeric cell surface glycoprotein expressed primarily on thymocytes and a subpopulation of mature T lymphocytes. It binds to the invariant part of the major histocompatibility complex class I molecule and participates in antigen recognition by the major histocompatibility complex class I restricted T cells. As in mammalian species, the majority of chicken thymocytes express both CD4 and CD8, whereas peripheral T cells are either CD4- or CD8-positive. We have created a panel of mouse monoclonal antibodies detecting different cell surface epitopes on chicken CD8. The antibodies precipitate a 32-34 kDa dimeric protein from surface labelled thymocytes under reducing conditions. The identical N-deglycosylation pattern confirms that these MoAb precipitate the same heterodimeric molecule from chicken thymocyte lysates. Binding of 11-38 and 11-39 MoAb to peripheral blood T cells is totally inhibited by 11-39 and previously characterized CT8 and EP72 MoAb, further confirming their CD8 specificity. CD8 alpha-chain specificity of MoAb 11-39, 11-38, 11-30 and 11-13 is conclusively proven by staining COS-cells transfected with a plasmid containing CD8 alpha cDNA. However, MoAb 11-13, 11-30 and 11-38 do not compete with MoAb 11-39 in binding to CD8. These results demonstrate recognition of different epitopes by these MoAb. Monoclonal antibodies detecting novel epitopes on chicken CD8 provide a valuable tool for further studies on T cell development.
    Scandinavian Journal of Immunology 08/1995; 42(1):171-4. · 2.20 Impact Factor
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