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Biomedical subjects

Wang Teng

Publications and source records attributed to Wang Teng.

4 recordsLinked to original sources

A ruptured pancreaticoduodenal artery aneurysm repaired by combined endovascular and open techniques.

Aneurysms of the pancreaticoduodenal arteries (PDA) are rare, accounting for <2% of all visceral aneurysms. An association with celiac artery stenosis has been reported. Many present with rupture, and a high mortality can be expected. Treatment is therefore challenging. Arterial ligation, anuerysmectomy, or bypass has been the mainstay of treatment. We recently treated a patient (who had no celiac axis) with a ruptured PDA aneurysm with combined open and endovascular techniques. A 46-year-old man was transferred to our hospital with a 1-day history of abdominal pain and syncope. On admission, an abdominal and pelvis computerized tomographic (CT) scan identified a large mesenteric hematoma, a 1.9 cm PDA aneurysm, and an occluded celiac axis. Mesenteric angiography revealed no active aneurysm leak and a stenotic superior mesenteric artery (SMA) origin. All hepatic blood flow originated from the stenotic SMA via markedly enlarged PDA collaterals. The patient was brought to the operating room, where absence of the celiac axis was confirmed. An aorto-to-proper hepatic and SMA bypass was performed using a bifurcated polyester graft. The next day, the patient was brought to the angiography suite, where the PDA aneurysm was coiled. Postprocedure CT scans confirmed thrombosis of the aneurysm. Ruptured mesenteric artery aneurysms are a challenging problem for the vascular surgeon. PDA aneurysms are rare and often occur in an unfavorable location. There appears to be an association with anatomic anomalies of the mesenteric circulation. Prompt invasive and noninvasive diagnostic studies aid in the definitive management of this often fatal problem. Combined endovascular and open techniques can be used for successful treatment.

Aneurysm, Ruptured↗

Pneumococcal aortitis: a difficult preoperative diagnosis.

Primary infections of the aorta are rare. We recently treated a patient who was given a diagnosis of noninfectious aortitis after an extensive work-up, but after clinical deterioration, was found to have a pneumococcal mycotic aneurysm at the time of surgery. The difficulty in distinguishing microbial aortitis from noninfectious chronic periaortitis is discussed as well as the need for frequent surveillance imaging of the aorta if immunosuppression is used to treat the latter entity. The infected aortoiliac segment was ultimately repaired with autologous femoral veins.

Aged↗

Molecular cloning, genomic organization and functional characterization of a new short-chain potassium channel toxin-like peptide BmTxKS4 from Buthus martensii Karsch(BmK).

Scorpion venom contains many small polypeptide toxins, which can modulate Na(+), K(+), Cl(-), and Ca(2+) ion-channel conductance in the cell membrane. A full-length cDNA sequence encoding a novel type of K(+)-channel toxin (named BmTxKS4) was first isolated and identified from a venom gland cDNA library of Buthus martensii Karsch (BmK). The encoded precursor contains 78 amino acid residues including a putative signal peptide of 21 residues, propeptide of 11 residues, and a mature peptide of 43 residues with three disulfide bridges. BmTxKS4 shares the identical organization of disulfide bridges with all the other short-chain K(+)-channel scorpion toxins. By PCR amplification of the genomic region encoding BmTxKS4, it was shown that BmTxKS4 composed of two exons is disrupted by an intron of 87 bp inserted between the first and the second codes of Phe (F) in the encoding signal peptide region, which is completely identical with that of the characterized scorpion K(+)-channel ligands in the size, position, consensus junctions, putative branch point, and A+T content. The GST-BmTxKS4 fusion protein was successfully expressed in BL21 (DE3) and purified with affinity chromatography. About 2.5 mg purified recombinant BmTxKS4 (rBmTxKS4) protein was obtained by treating GST-BmTxKS4 with enterokinase and sephadex chromatography from 1 L bacterial culture. The electrophysiological activity of 1.0 microM rBmTxKS4 was measured and compared by whole cell patch-clamp technique. The results indicated that rBmTxKS4 reversibly inhibited the transient outward K(+) current (I(to)), delayed inward rectifier K(+) current (I(k1)), and prolonged the action potential duration of ventricular myocyte, but it has no effect on the action potential amplitude. Taken together, BmTxKS4 is a novel subfamily member of short-strain K(+)-channel scorpion toxin.

Amino Acid Sequence↗