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  • 1.
    Aveskogh, Maria
    et al.
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Hellman, Lars
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    A single major transcript encodes the membrane-bound form of rat immunoglobulin E1995Ingår i: Scandinavian Journal of Immunology, ISSN 0300-9475, E-ISSN 1365-3083, Vol. 42, nr 5, s. 535-539Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The primary structure of the membrane-bound form of rat immunoglobulin E was determined by PCR amplification and nucleotide sequence analysis of its mRNA. The sequence was found to correspond to the previously identified membrane exons of the rat epsilon chain gene. The donor splice site in the C4 exon was mapped to a position 35 nt upstream of the stop codon for the secreted form of rat IgE. Therefore, the membrane-bound IgE lacks the 12 C-terminal amino acids present in the secreted form of the protein. Recently, five novel epsilon chain transcripts were isolated from human IgE producing B-cells or B-cell lines. Four of these transcripts encode proteins which differ in their C-terminal ends from the classical membrane or secreted forms of human IgE. To investigate if these transcripts were likely to represent functional mRNAs, their evolutionary conservation was studied by screening a rat IgE producing B-cell line for the expression of similar transcripts. By PCR amplification and cloning of transcripts, containing both the C3 and the M2 exons, approximately 10,000 independent cDNA clones were obtained. These clones were screened with probes directed against regions specific for each of the five novel human epsilon chain mRNAs. However, no evidence was found for the presence of transcripts with a similar structure, indicating that no specific function associated with these transcripts and their corresponding proteins has been conserved between human and rat. The lack of additional M2-containing transcripts in the rat suggest that the novel human IgE transcripts are byproducts of differential splicing and that they most likely encode proteins with no evolutionarily important function.

  • 2. Bergvist, Anders
    et al.
    Nilsson, Mats
    Bondeson, Kåre
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Magnusson, Göran
    Loss of DNA-binding and new transcriptional trans activation function in polymavirus large T-antigen with mulation of zinc finger motif1990Ingår i: Nucleic Acids Research, Vol. 18, nr 9, s. 2715-2720Artikel i tidskrift (Refereegranskat)
  • 3.
    Bondeson, Kåre
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Mouse polyomavirus large T-antigen: DNA-binding and related activities1995Bok (Övrigt vetenskapligt)
  • 4.
    Bondeson, Kåre
    et al.
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Frostellkarlsson, Aa
    Fagerstam, L
    Magnusson, Göran
    Lactose repressor-operator DNA interactions: kinetic analysis by a surface plasmon resonance biosensor1993Ingår i: Analytical biochemistry, Vol. 214, nr 1, s. 245-251Artikel i tidskrift (Refereegranskat)
  • 5.
    Bondeson, Kåre
    et al.
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Rönn, Ola
    Magnusson, Göran
    DNA binding of polyomavirus large T-antigen: kinetics of interactions with different types of binding sites1998Ingår i: FEBS letters, Vol. 423, nr 3, s. 307-313Artikel i tidskrift (Refereegranskat)
  • 6.
    Bondeson, Kåre
    et al.
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Rönn, Ola
    Magnusson, Göran
    Preferred DNA-binding-Sites of Polyomavirus Large T-antigen1995Ingår i: European Journal of Biochemistry, Vol. 227, nr 1-2, s. 359-366Artikel i tidskrift (Refereegranskat)
  • 7.
    Lützelschwab, Claudia
    et al.
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Pejler, Gunnar
    Aveskogh, Maria
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Hellman, Lars
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för medicinsk immunologi och mikrobiologi.
    Secretory granule proteases in rat mast cells: Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations1997Ingår i: Journal of Experimental Medicine, ISSN 0022-1007, E-ISSN 1540-9538, Vol. 185, nr 1, s. 13-29Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Two of the major rat mast cell proteases, rat mast cell protease 1 (RMCP-1) and RMCP-2, have for many years served as important phenotypic markers for studies of various aspects of mast cell (MC) biology. However, except for these proteases only fragmentary information has been available on the structure and complexity of proteases expressed by different subpopulations of rat MCs. To address these questions, cDNA libraries were constructed from freshly isolated rat peritoneal MCs and from the rat mucosal MC line RBL-1. cDNA clones for 10 different serine proteases (RMCP- 1-10), and the MC carboxypeptidase A were isolated and characterized. Six of these proteases have not been isolated previously. Based on their protease content, three separate subpopulations of MCs were identified. Connective tissue MCs (CTMCs) from the ear and peritoneum express the chymases RMCP-1 and -5, the tryptases RMCP-6, and -7 and the carboxypeptidase A. However, based on a large difference in the level of expression of RMCP-7, CTMCs of these two organs may be regarded as two separate subpopulations. RMCP-2 and the three closely related proteases of the RMCP-8 subfamily were identified as the major mucosal MC proteases in rat. In contrast to what has been reported for human MCs, no expression of cathepsin G or cathepsin G-like proteases was detected in any of the rat MC populations. To determine mRNA frequencies for the various proteases expressed by normal tissue MCs, an unamplified peritoneal MC cDNA library was screened with a panel of monospecific cDNA probes. These results showed that peritoneal MCs are highly specialized effector cells with mRNA frequencies for the major proteases in the range of several percent of the total mRNA pool.

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