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1.
Internist (Berl) ; 50(3): 368-73, 2009 Mar.
Article in German | MEDLINE | ID: mdl-19057887

ABSTRACT

An 82 year old male patient presented with acute abdominal pain. Computer tomography revealed portomesenteric vein gas and a paralytic ileus due to an acute mesenteric ischemia. Because of the presence of peritoneal signs immediate surgical exploration was performed. The diagnosis of a non-occlusive mesenteric ischemia with bowel infarction was confirmed during surgery and pathologically. The patient survived without any severe consequences.


Subject(s)
Embolism, Air/diagnostic imaging , Embolism, Air/etiology , Ischemia/complications , Ischemia/diagnostic imaging , Mesenteric Veins/diagnostic imaging , Mesentery/blood supply , Portal Vein/diagnostic imaging , Abdominal Pain/diagnostic imaging , Abdominal Pain/etiology , Aged, 80 and over , Humans , Male , Mesentery/diagnostic imaging , Radiography
2.
EMBO J ; 20(24): 7271-83, 2001 Dec 17.
Article in English | MEDLINE | ID: mdl-11743003

ABSTRACT

The best studied nuclear export processes are mediated by classical leucine-rich nuclear export signals that specify recognition by the CRM1 export receptor. However, details concerning alternative nuclear export signals and pathways are beginning to emerge. Within the family of Herpesviridae, a set of homologous regulatory proteins that are exemplified by the ICP27 of herpes simplex virus were described recently as nucleocytoplasmic shuttling proteins. Here we report that pUL69 of the beta-herpesvirus human cytomegalovirus is a nuclear protein that is able to shuttle between the nucleus and the cytoplasm independently of virus-encoded cofactors. In contrast to proteins containing a leucine-rich export signal, the shuttling activity of pUL69 was not affected by leptomycin B, indicating that pUL69 trafficking is not mediated by the export receptor CRM1. Importantly, we identified and characterized a novel type of transferable, leptomycin B-insensitive export signal that is distinct from other export signals described previously and is required for pUL69-mediated activation of gene expression. These data suggest that pUL69 is exported via a novel nuclear export pathway, based on a so far unique nuclear export signal of 28 amino acids.


Subject(s)
Cell Nucleus/metabolism , Cytomegalovirus/metabolism , Cytoplasm/metabolism , Karyopherins/metabolism , Receptors, Cytoplasmic and Nuclear , Trans-Activators/metabolism , Viral Proteins/metabolism , Active Transport, Cell Nucleus , Amino Acid Sequence , Base Sequence , Cell Line , Humans , Microinjections , Molecular Sequence Data , Mutagenesis , Oligodeoxyribonucleotides , Protein Transport , Sequence Homology, Amino Acid , Trans-Activators/chemistry , Trans-Activators/genetics , Transcriptional Activation , Viral Proteins/chemistry , Viral Proteins/genetics , Exportin 1 Protein
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