Biomedical subjects

S Lehnhardt

Publications and source records attributed to S Lehnhardt.

8 recordsLinked to original sources

PubMed2003

Background suppression using magnetization preparation for contrast-enhanced 3D MR angiography of the pelvic and lower leg arteries.

PURPOSE: To develop and evaluate non-slab-selective magnetization preparation in contrast-enhanced 3D-MR angiography. METHODS: An ultrafast spoiled mr angiography sequence (FLASH) with non-selective inversion prepulses for background suppression was implemented on a 1.5 T MR system. In 11 patients gadobenate dimeglumine-enhanced mr-angiography of the pelvic and lower leg arteries was performed using the AngioSURF device. Source data was evaluated for contrast-to-noise-ratio, image quality and the extent of background suppression. RESULTS: Background suppression and selective vessel contrast was excellent in all vascular levels. The mr protocol was comfortable and easy-to-handle. Abandonment of precontrast-series acquisition simplified the examination procedure markedly. CONCLUSIONS: Magnetization preparation provides efficient suppression of the background signal in contrast-enhanced 3D mr angiography of the pelvic and lower leg arteries. Since no subtraction technique is needed, moving-bed and whole body MRA-protocols can be simplified significantly.

Adult↗

PubMed2002

Diagnosis of the hypothenar hammer syndrome by high-resolution contrast-enhanced MR angiography.

Our objective was to describe the imaging features of hypothenar hammer syndrome using minimally invasive contrast-enhanced MR angiography in comparison with oscillography study. In five patients with hypothenar hammer syndrome Gd-BOPTA-enhanced elliptically reordered 3D pulse sequence MR was compared with oscillography findings and clinical symptoms focusing on angiographic appearance of vessel injury, distribution pattern of hand vasculature and joining branches between the radial and ulnar artery supply. All patients showed segmental occlusion at the site of trauma impact with varying involvement of the superficial palmar arch, common volar digital arteries. Embolic disease was present in 50% of patients and could be clearly identified with MRA. Good correspondence was found between angiographic appearance including the presence of collaterals, clinical symptoms and oscillography. Bilateral comparison was helpful in distinguishing between vessel variants and pathology. Bilateral Gd-BOPTA-enhanced MR angiography is a minimally invasive method to depict clearly the localization and extent of vessel injury in hypothenar hammer syndrome providing valuable information about distribution pattern of hand vasculature and presence of collaterals; however, no flow data can be obtained.

Adult↗

PubMed2000

Fast functional MRA using time-resolved projection MR angiography with correlation analysis.

Most recently, time-resolved 2D MRA after injection of a contrast agent bolus for various applications has been proposed. Similar to conventional digital subtraction angiography (DSA), 2D MR DSA offers the ability to observe the dilution of the bolus in the vascular system during the passage with a temporal resolution considerably below 1 sec. The purpose of this paper is to present strategies to improve the inherent low signal-to-noise ratio of 2D angiograms while retaining some temporal resolution. This can be achieved by applying algorithms for time series analysis as used in functional MRI. The significantly improved image quality is demonstrated on examples from clinical studies from bronchial MRA as well as cardiovascular MRA. In addition to the increased signal-to-noise ratio, correlation analysis leads to suppression of background signals and to a better discrimination of overlapping vessels. Further improvements in the temporal discrimination of vessels is afforded by the use of consecutive multiple contrast agent boli as demonstrated by numerical simulations and experiments.

Artifacts↗

PubMed1999

MRI of heart morphology. Comparison of nongradient echo sequences with single- and multislice acquisition.

RATIONALE AND OBJECTIVES: A large variety of cardiac MRI sequences have been introduced for heart morphology evaluation. The aim of this study was to establish a practicable and robust examination protocol for standard high-field systems applying nongradient echo sequences with single- and multi-slice acquisition. METHODS: Fifty-one patients received electrocardiogramgated MRI of the heart with "black-blood" preparation, comparing three single-slice and three multislice sequences with a T1-weighted turbo spin echo reference sequence. Demarcation of the left ventricular myocardium and cavity and the extent of flow and motion artifacts were assessed. RESULTS: The myocardium and left ventricular cavity were depicted best with the single-slice T1- and T2-weighted turbo spin echo sequence. The nonbreath-hold multislice sequences produced marked artifacts and therefore were of poor diagnostic value. The TIRM haste sequence was best suited for fat suppression. The T2-weighted breath-hold single-shot sequence with half-Fourier imaging proved to be most appropriate for multislice imaging. CONCLUSIONS: Sufficient depiction of heart morphology with comprehensive evaluation of signal changes can be achieved using nongradient spin echo and turbo spin echo sequences with breath-holding. For rational imaging of myocardial and heart chamber morphology, multislice and single-slice sequences should be combined.

Adult↗

PubMed1991

In vivo effect of asparagine in the hydrophobic region of the signal sequence.

On the basis of the biophysical studies on the synthetic mutant (Ile-8----Asn) OmpA signal peptide in the preceding paper (Hoyt, D. C., and Gierasch, L.M. (1991) J. Biol. Chem. 266, 14406-14412), the in vivo effects of the same mutation were examined by fusing the mutant OmpA signal sequence to Staphylococcus aureus nuclease or TEM beta-lactamase. The mutation in which the isoleucine residue at position 8 of the OmpA signal sequence of Escherichia coli was replaced with a neutral polar residue, asparagine, resulted in a defective signal peptide. The mutant signal sequence was unable to be processed, and the precursor molecule accumulated in the cytoplasmic as well as in the membrane fractions, indicating that the Ile-8----Asn OmpA signal sequence is not competent for translocating nuclease A or beta-lactamase across the membrane. This result is consistent with the in vitro studies on the Ile-8----Asn OmpA signal peptide, which indicated that the mutant signal peptide was unable to penetrate into the hydrophobic core of the lipid bilayer. Other asparagine or glutamine substitution mutations in the hydrophobic region of the OmpA signal sequence were also examined. Interestingly, the OmpA signal sequence with either Ile-8----Gln, Val-10----Asn, or Leu-12----Asn mutation was completely defective as the Ile-8----Asn OmpA signal sequence, while the Ile-6----Asn and Ala-9----Asn OmpA nucleases were able to be processed to secrete nuclease, although the processing occurred at a much slower rate than the wild-type OmpA nuclease. These results indicate that the defects depend on the position of the lesion in the hydrophobic core of the OmpA signal sequence.

Amino Acid Sequence↗

PubMed1990

Enhancement of protein translocation across the membrane by specific mutations in the hydrophobic region of the signal peptide.

The hydrophobic region of the signal peptide of the OmpA protein of the Escherichia coli outer membrane was extensively altered in its hydrophobicity and predicted secondary structure by site-specific mutagenesis. The mutated signal peptides were fused to nuclease A from Staphylococcus aureus, and the function of the signal peptide was examined by measuring the rate of processing of the signal peptide. Six of the 12 mutated signal peptides in the nuclease hybrid were processed faster than the wild-type. In particular, the processing of the mutated signal peptide in which the alanine residue at position 9 was substituted with a valine residue was enhanced almost twofold over the processing of the wild-type signal peptide. In addition, the production of nuclease A fused with this mutated signal peptide also increased twofold. However, these effects were not observed when the mutated signal peptide was fused to TEM beta-lactamase. Analysis of the present mutations suggests that both overall hydrophobicity and distinct structural requirements in the hydrophobic region have important roles in signal peptide function.

Amino Acid Sequence↗

PubMed1988

Modulation of the effects of mutations in the basic region of the OmpA signal peptide by the mature portion of the protein.

Oligonucleotide-directed site-specific mutagenesis was used to study the structure-function relationship of the positively charged amino terminus of the Escherichia coli outer membrane protein OmpA signal peptide. Mutations were isolated which reduced the overall charge of the amino-terminal region from +2 (wild type) to +1, 0, and -1, as well as one mutation from Thr to Ser at position 4. DNA encoding the wild type and mutant OmpA signal peptides was then fused in-frame to DNA encoding the mature regions of Staphylococcus aureus nuclease A and TEM beta-lactamase. In the case of both the beta-lactamase and nuclease fusions, normal processing was no longer observed when the charge at the amino terminus was reduced to zero or made negative. Differences between the two hybrid proteins were observed in the case of the Thr to Ser mutation. As expected, this mutation had no effect on the beta-lactamase hybrid; however, the processing rate of the nuclease hybrid protein was reduced to nearly one-half. Furthermore, this effect was essentially reversed when a Lys residue at position 3 was deleted. A model is presented which explains the differing effects of a signal peptide mutation on the secretion of different hybrid proteins based on kinetic differences in the translocation of the nuclease and beta-lactamase proteins.

Amino Acid Sequence↗

PubMed1987

The differential effect on two hybrid proteins of deletion mutations within the hydrophobic region of the Escherichia coli OmpA signal peptide.

Oligonucleotide-directed site-specific mutagenesis was used to systematically shorten the hydrophobic region within the signal peptide of the Escherichia coli outer membrane protein OmpA. DNA encoding the wild type and mutant OmpA signal peptides were then fused in frame to DNA encoding the mature regions of Staphylococcus aureus nuclease A and TEM beta-lactamase. The ability of these signal peptides to direct processing of the resulting hybrid proteins was dependent on both their length and the protein to which they were fused. Deletion of two or more residues progressively slowed processing of pro-OmpA-nuclease. By contrast, pro-OmpA-beta-lactamase was less sensitive to the length of the hydrophobic region than to the nature of the deleted residue(s). Deletion of an Ala residue tended to reduce processing efficiency of pro-OmpA-beta-lactamase, while deletion of an Ile residue, together with the Ala residue, resulted in improvement. The loss of either 3 or 4 residues abolished processing of both hybrids. These data indicate that both the length as well as the identity of residues in the hydrophobic region are important. The relative importance of these two factors depends on the mature region of the protein being secreted.

Amino Acid Sequence↗