Cell type-specific expression of LINE-1 open reading frames 1 and 2 in fetal and adult human tissues.
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Cell type-specific expression of LINE-1 open reading frames 1 and 2 in fetal and adult human tissues. / Ergün, Süleyman; Buschmann, Christian; Heukeshoven, Jochen; Dammann, Kristin; Schnieders, Frank; Lauke, Heidrun; Chalajour, Fariba; Kilic, Nerbil; Strätling, Wolf H; Schumann, Gerald G.
in: J BIOL CHEM, Jahrgang 279, Nr. 26, 26, 2004, S. 27753-27763.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Cell type-specific expression of LINE-1 open reading frames 1 and 2 in fetal and adult human tissues.
AU - Ergün, Süleyman
AU - Buschmann, Christian
AU - Heukeshoven, Jochen
AU - Dammann, Kristin
AU - Schnieders, Frank
AU - Lauke, Heidrun
AU - Chalajour, Fariba
AU - Kilic, Nerbil
AU - Strätling, Wolf H
AU - Schumann, Gerald G
PY - 2004
Y1 - 2004
N2 - The LINE-1 (L1) family of non-long terminal repeat retrotransposons is a major force shaping mammalian genomes, and its members can alter the genome in many ways. Mutational analyses have shown that coexpression of functional proteins encoded by the two L1-specific open reading frames, ORF1 and ORF2, is an essential prerequisite for the propagation of L1 elements in the genome. However, all efforts to identify ORF2-encoded proteins have failed so far. Here, applying a novel antibody we report the presence of proteins encoded by ORF2 in a subset of cellular components of human male gonads. Immunohistochemical analyses revealed coexpression of ORF1 and ORF2 in prespermatogonia of fetal testis, in germ cells of adult testis, and in distinct somatic cell types, such as Leydig, Sertoli, and vascular endothelial cells. Coexpression of both proteins in male germ cells is necessary for the observed genomic expansion of the number of L1 elements. Peptide mass fingerprinting analysis of a approximately 130-kDa polypeptide isolated from cultured human dermal microvascular endothelial cells led to the identification of ORF2-encoded peptides. An isolated approximately 45-kDa polypeptide was shown to derive from nonfunctional copies of ORF2 coding regions. The presence of both ORF1- and ORF2-encoded proteins in vascular endothelial cells and its apparent association with certain stages of differentiation and maturation of blood vessels may have functional relevance for vasculogenesis and/or angiogenesis.
AB - The LINE-1 (L1) family of non-long terminal repeat retrotransposons is a major force shaping mammalian genomes, and its members can alter the genome in many ways. Mutational analyses have shown that coexpression of functional proteins encoded by the two L1-specific open reading frames, ORF1 and ORF2, is an essential prerequisite for the propagation of L1 elements in the genome. However, all efforts to identify ORF2-encoded proteins have failed so far. Here, applying a novel antibody we report the presence of proteins encoded by ORF2 in a subset of cellular components of human male gonads. Immunohistochemical analyses revealed coexpression of ORF1 and ORF2 in prespermatogonia of fetal testis, in germ cells of adult testis, and in distinct somatic cell types, such as Leydig, Sertoli, and vascular endothelial cells. Coexpression of both proteins in male germ cells is necessary for the observed genomic expansion of the number of L1 elements. Peptide mass fingerprinting analysis of a approximately 130-kDa polypeptide isolated from cultured human dermal microvascular endothelial cells led to the identification of ORF2-encoded peptides. An isolated approximately 45-kDa polypeptide was shown to derive from nonfunctional copies of ORF2 coding regions. The presence of both ORF1- and ORF2-encoded proteins in vascular endothelial cells and its apparent association with certain stages of differentiation and maturation of blood vessels may have functional relevance for vasculogenesis and/or angiogenesis.
M3 - SCORING: Zeitschriftenaufsatz
VL - 279
SP - 27753
EP - 27763
JO - J BIOL CHEM
JF - J BIOL CHEM
SN - 0021-9258
IS - 26
M1 - 26
ER -