[Deep vein thrombosis as a primary symptom of abdominal aortic aneurysm : Bilateral deep vein thrombosis caused by infrarenal abdominal aortic aneurysm (15 cm in diameter) with complete compression of the inferior vena cava]. / Tiefe Venenthrombose als Primärsymptom eines abdominellen Aortenaneurysmas : Beidseitige 4-Etagen-TVT durch infrarenales Bauchaortenaneurysma (15 cm Durchmesser) mit vollständiger Kompression der V. cava inferior.

This article presents the case of a 70-year-old obese patient with severe bilateral leg pain due to deep vein thrombosis. After unsuccessful venous recanalization, computed tomography angiography revealed an abdominal aortic aneurysm 15 cm in diameter with total compression of the inferior vena cava. For venous decompression as well as rupture prophylaxis, conventional open surgical repair was performed.

Molecular cloning of a novel phytochrome gene of the moss Ceratodon purpureus which encodes a putative light-regulated protein kinase.

The phytochrome gene (phyCer) of the moss Ceratodon purpureus was isolated and characterized. phyCer is composed of three coding exons: exon I of 2035 bp, exon II of 300 bp and exon III of 1574 bp. The deduced polypeptide encoded by exon I and II exhibits substantial sequence homology to the conserved NH2-terminal chromophore domain of known phytochromes. In contrast, the COOH-terminal polypeptide encoded by exon III shows no sequence homology to any phytochrome molecule. phyCer most likely represents a single-copy gene and is expressed in a light-independent manner. From the DNA sequence analysis it can be deduced that the PhyCer polypeptide is composed of 1303 amino acids (including the starting Met) which predicts a molecular mass for PhyCer of 145 kDa. The polypeptide encoded in exon III exhibits striking homology within the 300 carboxy-terminal amino acids to the catalytic domain of protein kinases. The carboxy terminus of PhyCer was found to be most homologous to protein-tyrosine kinases of Dictyostelium discoideum and to the products of retroviral oncogenes which belong to the Raf-Mos serine/threonine kinase family. From the hydropathy profile PhyCer appears to be a soluble protein. The predicted structure suggests that PhyCer represents a soluble light-sensor protein kinase which is linked with a cellular phosphorylating cascade.