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Biomedical subjects

D Carrier

Publications and source records attributed to D Carrier.

32 records · Page 2Linked to original sources
PubMed1990

Protective effect of lipidic surfaces against pressure-induced conformational changes of poly(L-lysine).

Poly(L-lysine) bound to phosphatidylglycerol or phosphatidic acid bilayers was submitted to hydrostatic pressure in a diamond anvil cell to investigate whether the lipidic surfaces can protect the polypeptide against pressure-induced conformational transformations. The amide I region of the infrared spectrum of dimyristoylphosphatidic acid bound polylysine shows that most of the polypeptide retains its beta-sheet structure up to 19 kbar, while it is known to convert entirely to alpha-helix at approximately 2 kbar in the absence of the lipid [Carrier, D., Mantsch, H.H., & Wong, P.T.T. (1989) Biopolymers (in press)]. The simultaneous binding of the polypeptidic molecules to two opposing bilayers appears to be required in order to preserve the beta-sheet structure at pressures over approximately 9 kbar: a small proportion of the polypeptide, most likely the molecules at the surface of the aggregated bilayers, was found to convert to unordered and eventually to alpha-helical conformations in the pressure range 9-19 kbar. The decrease from 1612 to 1606 cm-1 of the frequency of the major beta-sheet component of the infrared amide I band as the pressure is raised to 6 kbar indicates a strengthening of the interchain hydrogen bonds. The high-pressure infrared spectra of polylysine bound to dimyristoyl- and dipalmitoylphosphatidylglycerol show that the polypeptide remains alpha-helical up to approximately 12 kbar, though the changes in the bandshape indicate an increase in hydrogen bond strength. The formation of a small amount of beta-sheet was observed during decompression and is attributed to the effect of dehydration on the polypeptidic molecules located at the surface of the aggregates.(ABSTRACT TRUNCATED AT 250 WORDS)

Glycerophospholipids↗
PubMed1990

Activity of the hypaxial muscles during walking in the lizard Iguana iguana.

The role that the hypaxial muscles play in locomotion has been largely ignored by biologists. In tetrapods, there are at least three possibilities. First, the hypaxial muscles might bend the trunk laterally to increase stride length. Second, they might stabilize the trunk against the horizontal, lateral and vertical components of the propulsive force. Alternatively, they might not be involved in locomotion. This study evaluated these three hypotheses by analyzing the activity of the hypaxial muscles of green iguanas (Iguana iguana). During walking, the rectus abdominis, obliquus externus superficialis and profundus, intercostales externi, and ventral portion of the intercostales interni on one side of the trunk acted synergistically with the lateral portion of the intercostales interni and obliquus internus on the other side of the trunk. This pattern supports the hypothesis that the hypaxial muscles act to stabilize the trunk during locomotion. Specifically, the longitudinally oriented rectus abdominis, obliquus externus profundus and ventral portion of the intercostales interni appear to stabilize the trunk against the horizontal and lateral components of the propulsive force, which tend to rotate the girdles in the horizontal plane. The obliquely oriented obliquus externus superficialis, intercostales externi, lateral portion of the intercostales interni and obliquus internus appear to stabilize the trunk against the vertical component, which induces long-axis torsion in the trunk. Thus, the demands of locomotion may provide a functional explanation for the basic organization of the hypaxial muscles of tetrapods.

Abdominal Muscles↗
PubMed1989

Dynamics and orientation of glycolipid headgroups by 2H-NMR: gentiobiose.

Deuterium nuclear magnetic resonance has been used to investigate the dynamics and determine the orientation of the headgroup of the glycolipid 1,2-di-O-tetradecyl-3-O-(6-O-beta-D-glucopyranosyl-beta-D-glucopyranosyl )-sn- glycerol (beta-DTDGL), in aqueous multilamellar dispersions. In addition, its anomeric analog, having an alpha glucose-glycerol linkage, was prepared and examined. The lipids were labelled with deuterium at specific positions in the disaccharide moiety. Analysis of the deuterium quadrupolar splittings for the first glucose ring (glycerol-linked) gave segmental order parameters of 0.43 and 0.35 for the beta and alpha isomers, respectively. Both isomers had similar orientations of the sugar ring relative to the bilayer surface, as determined for lipid in the liquid-crystalline phase. 2H-NMR results for the lipid labelled at C-6' are consistent with a single conformation about the C-5'-C-6' bond of the first glucose residue, with a dihedral angle (O-5'-C-5'-C-6'-O-6') of -17 degrees. The results obtained for the second sugar ring suggest that two conformers may be present, which are in slow exchange on the 2H-NMR timescale. Measurements of longitudinal relaxation times, T1z, gave similar values for both sugar moieties in the headgroup, suggesting that the disaccharide does not exhibit the flexibility expected about the 1----6 linkage. Since T1z for 2H in these compounds decreases with increasing temperature and increases with magnetic field strength, the motion(s) dominating relaxation is in the long-correlation-time regime [omega 0 tau c)2 greater than 1). Thus, the gentiobiosyl headgroup undergoes the slowest motion of the glycolipid headgroups studied to date.

Calorimetry, Differential Scanning↗
PubMed1988

Study of the effect of poly(L-lysine) on phosphatidic acid and phosphatidylcholine/phosphatidic acid bilayers by raman spectroscopy.

The effect of polylysine (PLL) on dimyristoylphosphatidic acid (DMPA), on dimyristoyl-phosphatidylcholine (DMPC), and on mixtures of these lipids was investigated by Raman spectroscopy. These results show that long polylysine (Mr approximately 200,000) increases the stability of the acyl chain matrix of DMPA to form a more closely packed structure with a stoichiometry of one lysine residue per PA molecule. On the other hand, short PLL (Mr 4000) destabilizes the PA bilayer, and the complex formed undergoes a gel to liquid-crystalline transition at a lower temperature than of the pure lipid. For both cases, we have observed that bound polylysine adopts a beta-sheet conformation as opposed to the alpha-helical structure previously found for dipalmitoylphosphatidylglycerol/long PLL complexes [Carrier, D., & Pézolet, M. (1984) Biophys. J. 46, 497-506]. The difference in the thermal behavior of complexes of DMPA with long and short polylysines is believed to be associated with the fact that in the complex the long polypeptide adopts the beta-sheet conformation over the whole range of temperatures investigated while the short one undergoes a change of conformation from beta-sheet of random coil upon heating. Therefore, the conformation of the lipid-bound polypeptides depends on the nature of the polar head group of the lipid, not only on its net charge, and it affects considerably the thermotropism of the lipid. On the other hand, both long and short polylysines show no affinity for phosphatidylcholine since the temperature profiles of DMPC and of DMPC/PLL complexes exhibit exactly the same behavior.(ABSTRACT TRUNCATED AT 250 WORDS)

Dimyristoylphosphatidylcholine↗
PubMed1986

Investigation of polylysine-dipalmitoylphosphatidylglycerol interactions in model membranes.

The effect of poly(L-lysine) on dipalmitoylphosphatidylglycerol bilayers has been studied by Raman and infrared spectroscopies, small-angle X-ray diffraction, and carboxyfluorescein escape experiments. The polypeptide is shown to induce a stabilization of the bilayer detected by the increase of interchain vibrational coupling and a slight decrease of the overall disorder. In addition, long polylysine (Mr 150,000) induces a positive shift of the gel to fluid transition temperature and, at lipid to lysine molar ratios greater than 1, a lateral phase separation within the bilayer. Raman and infrared spectra indicate modifications at the head group level. In contrast, short polylysine (Mr 4,000) leads to a decrease of the lipid thermotropic transition temperature, and no modification of the polar head group and no phase separation could be observed. These differences between short and long polypeptides are correlated with the conformation the polypeptide adopts upon binding to the lipid, which favors the formation of alpha-helices in the case of long polypeptides (Mr greater than or equal to 14,000). The X-ray data suggest that the basic polypeptide acts as a bridge between neighboring bilayers, thus causing their aggregation and dehydration.

Fluoresceins↗
PubMed1985

[Valve replacement associated with aorto-coronary bypass in ischemic mitral insufficiency].

26 cases of ischaemic mitral regurgitation (MR) were treated by combined surgery: mitral valve replacement (MVR) and coronary bypass grafting (CBG). This type of operation is not common (1.3 p. 100 of all operations) and is usually reserved for men (21 cases) of middle age (average 59 years). A half of the cases had suffered previous myocardial infarction (MI), an average 5 months before surgery (range 20 days to 2 years). The other half had severe angina or ECG changes of myocardial ischaemia. 23 patients were in Class IV (15 patients) or Class III (8 patients) of the NYHA classification. 6 of the cases required intraaortic balloon pumping. Mitral regurgitation was severe () in half of the cases with a raised pulmonary capillary (mean V wave = 52 mmHg) and systolic pulmonary artery pressures (mean = 47 mmHg: exceeding 60 mmHg in 7 cases). The coronary lesions were severe in 18 patients (12 cases of double and 6 of triple vessel disease including 2 cases of left main stem stenosis). Ruptured chordae were found in 11 cases and papillary muscle necrosis in 4 cases. Surgery comprised MVR with 12 bioprostheses and 14 mechanical prostheses. 33 CBG were performed (anterior wall: 15 cases, posterior wall: 11 cases). In addition, one tricuspid annuloplasty and 3 ventricular aneurysmectomies were carried out. The hospital mortality was 15.4 p. 100. The main causes of morbidity were low output states and postoperative MI (2 cases).(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗
PubMed1984

Raman spectroscopic study of the interaction of poly-L-lysine with dipalmitoylphosphatidylglycerol bilayers.

The interaction of the basic polypeptide poly-L-lysine with the negatively charged phospholipid dipalmitoylphosphatidylglycerol was studied using Raman spectroscopy. The nature of the interaction appeared to depend on the molar ratio of the constituents. At up to one lysine group per lipid molecule, the bilayer was stabilized by the polypeptide that underwent a conformational transition toward an ordered alpha-helical structure, in which the electrostatic interactions were probably maximal. The stabilization of the bilayer was detected by an increase in both the temperature of the thermotropic transition of the lipid and the interchain vibrational coupling of the methylene C-H vibrations. At higher poly-L-lysine concentration, hydrophobic interactions must have been involved to explain the binding of excess polypeptide. There seemed to be a penetration of poly-L-lysine in the bilayer that increased with the polypeptide concentration. Under these conditions, the chain-packing lattice gradually changed from hexagonal to either orthorhombic or monoclinic symmetry. We believe that this change of structure is associated with the interdigitation of the acyl chains.

Kinetics↗
PubMedDate not supplied

UCH operations improvement: emergency department benchmarking project summary.

The editors are providing this Executive Summary by the University HealthSystem Consortium of their Emergency Department Benchmarking Project. The report has been reviewed by the participating members listed at the end of the summary. The summary report provides both an interesting account of how a benchmarking project of considerable magnitude can be accomplished but also indicates how important comparative data can be used to improve individual programs.

Attitude of Health Personnel↗