[Menorrhagia due to cystic degeneration of a uterine leiomyoma]. / Menorragisch bloedverlies door een cysteus gedegenereerd leiomyoom van de uterus.

A 47-year-old female patient presented with increasing menorrhagia. On ultrasound examination a smooth-walled intra-uterine enlargement with multiple clear areas was found. As these cystic changes were reported to be 'most likely blood vessels' the enlargement was expected to be a uterine leiomyoma, and drug therapy was started. Due to unsatisfactory results of this therapy and continuing growth of the mass, it was finally decided to perform a total abdominal hysterectomy. The pathology revealed cystic degeneration of uterine leiomyoma. Degeneration of uterine leiomyoma is common and can easily be confused with other abnormalities of the uterus or even other abdominal organs. Diagnosis can best be made by (transvaginal) ultrasonography, if necessary complemented by CT or MRI.

Combined off-pump coronary surgery and left lung resection through midline sternotomy with a Medtronic Starfish 2 Heart Positioner.

Concomitant lung malignancy and coronary artery disease is uncommon. When the left lung is involved, the approach is considered to be staged or through left thoracotomy. We present a patient who was operated on for left pneumonectomy and off-pump coronary surgery through a midline sternotomy with the use of a Medtronic Starfish 2 Heart Positioner.

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides.

The high molecular weight (HMW) proteins from wheat contain a repetitive domain that forms 60-80% of their sequence. The consensus peptides PGQGQQ and GYYPTSPQQ form more than 90% of the domain; both are predicted to adopt beta-turn structure. This paper describes the structural characterization of these consensus peptides and forms the basis for the structural characterization of the repetitive HMW domain, described in the companion paper. The cyclic peptides cyclo-[PGQGQQPGQGQQ] (peptide 1), cyclo-[GYYPTSPQQGA] (peptide 2), and cyclo-[PGQGQQGYYPTSPQQ] (peptide 3) were prepared using a novel synthesis route. In addition, the linear peptides (PGQGQQ)n (n = 1, 3, 5) were prepared. CD, FTIR, and NMR data demonstrated a type II beta-turn structure at QPGQ in the cyclic peptide 1 that was also observed in the linear peptides 9PGQGQQ)n. A type I beta-turn was observed at YPTS and SPQQ in peptides 2 and 3, with additional beta-turns of either type I or II at GAGY (peptide 2) and QQGY (peptide 3). The proline in YPTS showed considerable cis/trans isomerization, with up to 50% of the population in the cis-conformation; the other prolines were more than 90% in the trans conformation. The conversion from trans to cis destroys the type I beta-turn at YPTS, but leads to an increase in turn character at SPQQ and GAGY (peptide 2) or QQGY (peptide 3).

Structure characterization of the central repetitive domain of high molecular weight gluten proteins. II. Characterization in solution and in the dry state.

The structure of the central repetitive domain of high molecular weight HMW) wheat gluten proteins was characterized in solution and in the dry state using HMW proteins Bx6 and Bx7 and a subcloned, bacterially expressed part of the repetitive domain of HMW Dx5. Model studies of the HMW consensus peptides PGQGQQ and GYYPTSPQQ formed the basis for the data analysis (van Dijk AA et al., 1997, Protein Sci 6:637-648). In solution, the repetitive domain contained a continuous nonoverlapping series of both type I and type II II beta-turns at positions predicted from the model studies; type II beta-turns occurred at QPGQ and QQGY sequences and type I beta-turns at YPTS and SPQQ. The subcloned part of the HMW Dx5 repetitive domain sometimes migrated as two bands on SDS-PAGE; we present evidence that this may be caused by a single amino acid insertion that disturbs the regular structure of beta-turns. The type I beta-turns are lost when the protein is dried on a solid surface, probably by conversion to type II beta-turns. The homogeneous type II beta-turn distribution is compatible with the formation of a beta-spiral structure, which provides the protein with elastic properties. The beta-turns and thus the beta-spiral are stabilized by hydrogen bonds within and between turns. Reformation of this hydrogen bonding network after, e.g., mechanical disruption may be important for the elastic properties of gluten proteins.