Anesthetic management of a patient with limb-girdle muscular dystrophy 2B:CARE-compliant case report and literature review.

BACKGROUND: Limb-girdle muscular dystrophies (LGMDs) belong to few neuromuscular disorders mainly involving pelvic and shoulder girdle muscles. Also, cardiac or pulmonary complications, increased rhabdomyolysis risk when exposed to volatile anesthetics and succinylcholine may increase anesthesia related risks. However, current reports about the anesthesia management of these patients are limited. CASE PRESENTATION: We described our anesthetic management of a 36 years old woman with LGMD 2B receiving arthroscopic knee surgery. In consideration of the high risk of rhabdomyolysis, total intravenous anesthesia (TIVA) was selected for her surgery. Considering the unpredictable respiratory depression, opioid based patient-controlled intravenous analgesia was replaced with an intra-articular cocktail therapy consisting of 20 ml of 0.2% ropivacaine. Also, we reviewed the literatures on anesthetic management of LGMD through searching PubMed, in order to provide a comprehensive and safe guidance for the surgery. CONCLUSIONS: Carefully conducted general anesthesia with TIVA technique is a good choice for LGMD patients. Neuraxial anesthesia may be used if general anesthesia needs to be avoided. To warrant safe anesthesia for surgery, any decision must be well thought out during perioperative period.

Structure of C-phycocyanin from Spirulina platensis at 2.2 A resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes.

The crystal structure of C-phycocyanin from the cyanobacterium S. platensis has been determined at 2.2 A resolution. The crystals belong to the monoclinic crystal form, which has not been previously reported for phycobiliprotein structures. The structure was solved using the molecular-replacement method with a final R value of 18.9% (R(free) = 23.7%) after model building and refinement. In the crystals used for the study, the C-phycocyanin hexamers formed by face-to-face association of two trimers are arranged in layers rather than in columns. Three different kinds of packing between adjacent hexamers in the layer were compared. The tight packing of two adjacent hexamers formed by four trimers in the asymmetric unit brings beta155 PCB chromophores close together, so it is possible that lateral energy transfer takes place through the beta155-beta155 route.

Purification, crystallization and preliminary crystallographic studies on the N-terminal fragment of human protein disulfide isomerase.

A fragment of human protein disulfide isomerase composed of the thioredoxin-like a and b domains (ab) has been expressed in Escherichia coli as a fusion protein with glutathione-S-transferase and purified after thrombin cleavage. Two forms of ab crystal were obtained with polyethylene glycol as precipitant and different additives at pH 7.5. The space group of form I is P4(1)2(1)2 or P4(3)2(1)2, with unit-cell dimensions a = 81.5, c = 259.7 A. The space group of form II is P4(1)22 or P4(3)22, with unit-cell dimensions a = 82.7, c = 86.5 A.

Purification and crystal growth of F1-ATPase from pig heart mitochondria.

A method has been evolved toward the aim of getting suitable crystals for high resolution of structural analysis of F1-ATPase by X-ray crystallography. The different conditions for crystal growth of ATPase that were isolated and purified by different methods from pig heart mitochondrial ATP synthase had been compared and screened. A simple method for purification of F1-ATPase was adopted. The F1-ATPase is released with chloroform from submitochondrial particles. Then it was treated with fractional precipitation of (NH4)2SO4 and finally was further purified by employing the sephadex G 200 column. The crystals of F1-ATPase were usually obtained after a few months. They appeared to have uniform morphology of tetrahedron. They diffracted to a resolution of 7A. The diffraction data were collected on the XRD-100 Siemens Area Detector. According to a total of 240 frames, the cell parameters obtained are a = b = 147 A, c = 208 A, alpha = beta = gamma = 90 alpha, the probable space group is P4 or its antipode. The reproducibility of this method for crystallization of F1-ATPase is good.

Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 A resolution.

The crystal structure of acidic phospholipase A2 from the venom of Agkistrodon halys pallas has been determined by molecular replacement at 2.0 A resolution to a crystallographic R-factor of 0.157. The overall structure of the molecule is very similar to those of other phospholipase A2 species of known structure. The catalytic site, the hydrophobic channel and the N-terminal region show greatest structural conservation. The Ca(2+)-binding region has a conformation that resembles closely that of bovine PLA2 rather than Crotalus atrox PLA2. Compared with other PLA2 species, the conformation of the C-terminal ridge shows significant difference due to the insertion of two residues. A unique aromatic patch appears on one face of the molecules, surrounded by two acidic residues, the relevant features of this structure and their possible biological implications are discussed.

Protein crystal growth in microgravity.

Protein crystal growth is quite important for the determination of protein structures which are essential to the understanding of life at molecular level as well as to the development of molecular biotechnology. The microgravity environment of space is an ideal place to study the complicated protein crystallization and to grow good-quality protein crystals. A number of crystal-growth experiments of 10 different proteins were carried out in August, 1992 on the Chinese re-entry satellite FSW-2 in space using a tube crystallization equipment made in China. A total of 25 samples from 6 proteins produced crystals, and the effects of microgravity on protein crystal growth were observed, especially for an acidic phospholipase A2 and henegg-white lysozyme which gave better crystals in space than earth-grown crystals in ground control experiments. The results have shown that the microgravity in space favors the improvement of the size, perfection, morphology and internal order of the grown protein crystals.

Protein crystallization in space.

The microgravity environment of space is an ideal place to study the complicated protein crystallization process and to grow good-quality protein crystals. A series of crystal growth experiments of 10 different proteins was carried out in space on a Chinese re-entry satellite FSW-2 in August, 1992. The experiments were performed for about two weeks at a temperature of 18.5 +/- 0.5 degrees C using a tube-like crystallization apparatus made in the Shanghai Institute of Technical Physics, Academia Sinica. More than half of 48 samples from 6 proteins produced crystals, and the effects of microgravity on protein crystal growth were observed, especially for hen-egg white lysozyme and an acidic phospholipase A2 from the venom of Agkistrodon halys Pallas. Analyses of the crystallization of these two enzymes in this mission showed that the microgravity environment in space may be beneficial to improve size, external perfection, morphology, internal order, and nucleation of protein crystals. Some of these positive microgravity effects were also demonstrated by the growth of protein crystals in gelled solution with the above two enzymes. A structural analysis of the tetragonal lysozyme crystal grown in space is in progress.