A rare case of fever of unknown origin: inflammatory myofibroblastic tumor of the liver. Case report and review of the literature.

We present the case of a rare cause of fever of unknown origin (FUO). FUO is challenging for patients as well as for physicians as there are more than 200 differential diagnoses of FUO (1,2). Pointing out a diagnosis often requires numerous noninvasive and invasive procedures that sometimes even fail to explain the fever. Our patient was admitted twice to our hospital due to remitting fever rising up to 40 degrees C without any subjective discomfort. At the first presentation no clinical focus could be identified. This included the examination of multiple blood and urine cultures, serology, autoimmune serology, transesophageal echocardiography, CT-scan of the lung and the abdomen, and bone scintigraphy. Elevated C-reactive protein (268 mg/l) decreased spontaneously and fever disappeared after 4 weeks. However, the patient was re-admitted 4 months later with identical symptoms. Multiple blood and urine cultures, serology, bone marrow examination, CT-scan of the lung and the abdomen, esophago-gastro-duodenoscopy and colonoscopy still showed no pathological findings. MRI-scan of the abdomen identified a liver tumor of 3.3 cm in diameter in segment 6 without typical signs of an adenoma, focal nodular hyperplasia or hepatocellular carcinoma. Biopsy of the suspect liver lesion revealed an inflammatory myofibroblastic tumor (inflammatory pseudotumor). After surgical resection of the tumor elevated inflammation markers as C-reactive protein normalized and fever disappeared. One year after surgery no more episodes of fever re-occurred. An inflammatory myofibroblastic tumor of the liver can be a rare cause of fever of unknown origin. MRI-scan can be an additional imaging tool to identify previously not recognized liver tumors.

A three-step purification method of large quantities of human recombinant alpha endothelial cellular growth factor for clinical use.

The endothelial cellular growth factor alpha-ECGF is a candidate drug for the induction of therapeutic neoangiogenesis. Its use in extensive experimental and clinical trials is hampered by the fact that currently published purification procedures allow only small yields, and the absence of pyrogenic impurities is not demonstrated. The rh alpha-ECGF was expressed in E. coli. Isolation of rh alpha-ECGF from E. coli lysates to apparent homogenicity was achieved by a three step purification procedure involving ionic exchange, heparin-sepharose and polymyxin B chromatography. By this method, 200 mg of rh alpha-ECGF was purified from 15 g wet weight E. coli bacteria. The isolated protein of 18 kDa appeared as a single band after SDS gel electrophoresis and subsequent silver-staining. The biological activity was expressed in the chorion-allantois-membrane assay and in the 3H-thymidine proliferation in baby hamster kidney cells. Drug trials with rabbits revealed no increase in body temperature after intravenous injections with 1 mg rh-ECGF.