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PubMedDate not supplied

[The effect of ultra small doses of thyroliberin on the structural changes in endoplasmic reticulum membranes in vitro].

Peptides are known to have the ability of modulating the activity of important regulatory cellular systems. One of them--thyroliberin, i.e. thyreotropin-releasing hormone (TRH), causes changes in the membrane structure and morphology of rat erythrocytes, as well as activates retractive activity of lymphatic vessels in ultra low concentrations (10(-10) to 10(-16) mol/l). In this study we used an electron spin resonance (ESR) method to explore the effect of TRH in a wide range of concentrations (10(-4) to 10(-18) mol/l) on thermo-induced structural transitions and microviscosity of lipid bilayer of the endoplasmic reticulum membrane of mice (C57 bI) liver cells. Two stable free radicals were used as paramagnetic probes: 2,2,6,6-tetramethil-4-capryolyl-1-oxyl and 16-doxyl-stearic acid, that are localized in superficial and deep layers of the membrane respectively. TRH caused a statistically significant change (p < 0.001) in microviscosity of the membrane surface layer. The largest effect (up to 30% decrease) was observed at TRH concentrations of 10(-10) and 10(-16) mol/l. It was also demonstrated that an addition of 10(-4), 10(-10) and 10(-16) mol/l of TRH decreases effective activation energy and temperature (by several degrees) of the thermo-induced structural transitions. The observed changes in the parameters of the membrane surface layer induced by TRH may be essential for its physiological activity, because of the obtained negative correlation (r = 0.99; p < 0.001) between the membrane microviscosity and frequency of lymphatic vessels' contraction. Complex changes in the structure of deep hydrophobic layer of the membrane caused by TRH were observed in this study as well. Higher concentrations of TRH (10(-4) and 10(-10) mol/l) produced results that were similar to the effect of TRH on the superficial lipid layer of the membrane, whereas the effect of ultra low TRH concentration (10(-16) mol/l) was reversed for microviscosity, number and activation energy of structural transitions in contrast with the case of surface layer. The results of this study suggest presence of a nonspecific factor in the effect of TRH on structural characteristics of the lipid component of biological membranes. It is possible, that the change of structural properties of biological membranes may be a part of the mechanism of TRH action at ultra low concentrations.

Animals↗

PubMed1986

[Structural changes in erythrocyte membranes during cooling studied by a spin probe method].

Peculiarities of structural changes in erythrocyte membranes during freezing (from -20 degrees to -50 degrees) were studied by electron paramagnetic resonance method using spin-labelled derivative of stearic acid-5-doxylstearate. It was established that membranes underwent a number of structural reconstructions due to the temperature decrease and water freezing-out. Differences were found in temperature dependences that characterize lipid ordering during probe insertion into membranes of native erythrocytes, white ghosts, and liposomes from total lipids of erythrocyte membranes. The data obtained indicate the impairment in the structure of lipid components and lipid-protein interactions in erythrocyte membranes during cooling.

Cold Temperature↗

PubMed1983

Fine structural changes in cat L7 ventral horn neurones after chronic sub LD50 DFP.

The fine structural changes in the ventral anterior horn of spinal segment L7, have been studied in adult cats after single and chronic sub LD50 (0.1 to 0.75 mg/kg SC with a cumulative range of 1.3 mg/kg to 10.5 mg/kg) low dose exposure to diisopropylfluorophosphate (DFP). Only the motoneurons of the chronically treated animals show an increase in the number of lysosomes, neurofilaments and vesicle-like structures. A large number of coated vesicles is observed within axons and axon terminals of both acute and chronically treated animals. Morphological evidence of axon and terminal degeneration is seen only in chronically treated animals. The present study shows that chronic sub LD50 low dose administration of DFP over periods from 5 to 21 days results in degenerative changes of presynaptic terminals and axons, with the severity of the changes being dependent on dose and duration of treatment. The data are interpreted by comparison with single high dose exposure reported in the literature with a discussion of acute and delayed neurotoxic effects of DFP, on the central nervous system.

Animals↗

PubMed2006

Structural changes and binding characteristics of the tetracycline-repressor binding site on induction.

The binding motif (pharmacophore) for induction and the changes in the structure of the binding site that accompany induction have been determined from molecular-dynamics simulations on the tetracycline-repressor signal-transduction protein. The changes and the induction mechanism are discussed and compared with conclusions drawn from earlier X-ray structures. The differences in inducer strength of tetracycline and 5a,6-anhydrotetracycline are discussed with respect to their interaction in the MD simulations.

Allosteric Regulation↗

PubMed1993

[Individual differences in the reactions to acute stress related to behavioral types. The structural changes in the brain].

Structural alterations in the brain after stress were studied in rats with different behavior type in open field and forced swimming tests. The most typical brain reaction to acute stress was a combination of reactive (hypertrophy and fission of mitochondria, hyperplasia of rough reticulum) and destructive (disintegration of mitochondria and rough reticulum) alterations which were different in rats with various behavior types. Thus, in rats with the active type of behavior showing the greatest resistance to stress (see report 1) the reactive processes were more manifest, while the the rats with the passive type of behavior showing lower resistance to stress developed destructive processes. Rats of the middle group with the least resistance to stress differed from the other two groups by vague structural alterations, i.e. by the lack of evident predominance of any definite process. It is assumed that individual differences in the resistance to acute stress are associated with individual differences in the manifestation of reactive alterations in the brain which can be regarded as a structural component of the urgent adaptation to stress.

Acute Disease↗

PubMed2000

Structural changes at cut ends of earthworm giant axons in the interval between dye barrier formation and neuritic outgrowth.

We describe structural changes at the cut ends of invertebrate myelinated earthworm giant axons beginning with the formation of a dye barrier (15 minutes posttransection or postcalcium addition) and ending with the formation of a neuritic outgrowth (2-10 days posttransection). The morphology of the cut end, and the location and morphological configuration of the dye barrier, were assessed by time-lapse confocal, fluorescence microscopy and by electron microscopy. During the interval from 15 to 35 minutes postcalcium addition, the dye barrier continuously migrated away from a cut axonal end; the dye barrier then remained stable for up to 5 hours. The size, packing density, and arrangement of membranous structures were correlated with changes in the dye barrier from 15 to 35 minutes postcalcium addition. During this interval, uptake of an externally placed hydrophilic dye by these membranous structures was also variable. After 35 minutes postcalcium addition, the membranous structures remained stable until they completely disappeared between 1 and 2 days posttransection. The disappearance of membranous structures always preceded neuritic outgrowth, which only arose from cut axonal ends. These results demonstrate that the dye barrier and associated membranous structures, which form after transection of earthworm giant axons, are very dynamic in the short term (35 minutes) with respect to their location and morphological configuration and suggest that axolemmal repair must be completed before neuritic outgrowth can occur.

Animals↗

PubMed1997

[The structural changes of cortical bone beneath plate after rigid platefixation and removal].

We investigated the structural changes of bone under the plate after plate fixation and removal. Twenty-four New Zealand white rabbits were plated on their intact left tibiae with stainless steel plates and 4 animals served as controls. The plates were removed 2 months after implantation in 20 plated animals, of which, 4 were sacrificed immediately after plate removal and the other were killed in successive groups of 4 each at 1, 2, 3 and 4 months after plate removal respectively. The remaining 4 plated animals were killed at 6 months after implantation. Bone samples were harvested and prepared for scanning microscopic observation. Internal fixation with a rigid plate may lead not only to osteopenia of the cortex under the plate, but also to disorganization of the cortex, in which the mineral column and collagen fibers were oriented in a randomized pattern. The regional osteoporosis could recover gradually after removal of the rigid plate. However, the restoration of normal bone structure occurred later than that of the bone mass. Delayed restoration of bone structure might be one of the potential causes of refracture of the plated bone.

Animals↗

PubMed1993

Structural changes in Z-disks of skeletal muscle myofibrils during growth of chicken.

Postnatal structural changes in Z-disks of skeletal muscles of chicken from 2 to 35 wk after hatching were examined to elucidate how Z-disks develop from the embryonic to the mature stage. The mechanical strength of Z-disks of breast muscle (i.e. the ratio of the number of myofibrils to the total number of myofibrils and myofibrillar fragments composed of 1-4 sarcomeres, which were formed under the mechanical forces exerted during homogenization) increased from 66% at 2 wk of age to 75% at 10 wk, and leveled off at 76% at 25 wk. The Z-disks of leg muscle were stronger than those of breast muscle throughout growth. Measurements by electron microscope showed that the width of Z-disks increased during growth from 26 to 33 nm, 48 to 53 nm, and 89 to 101 nm, in white, intermediate, and red muscle fibers, respectively. It was proved that the configuration of Z-filaments, the structural backbone of Z-disks, takes its final shape within 2 wk after hatching; the immature Z-disks are then reinforced by the accumulation of amorphous matrix materials. These results confirm that the maturation of Z-disks is brought about by physical motion in muscle tissue and the accompanying development of tension.

Animals↗

PubMed1978

Comparison of the calcium- and magnesium-induced structural changes of troponin--C. A proton magnetic resonance study.

Previous proton magnetic resonance studies of the effects of Ca(II) on the structure of rabbit skeletal muscle troponin--C have shown that Ca(II) binding to the two high affinity sites of troponin--C both directs and stabilizes the folding of much of the structure. Ca(II) binding by the two low affinity sites of troponin--C causes changes in the environment of largely hydrophobic residues. We have now examined the structural changes caused by Mg(II) and by Ca(II) in the presence of excess Mg(II). Successive addition of Mg(II) to metal-free troponin--C leads to broadly similar, but not identical, structural changes to those previously assigned to Ca(II) binding at the high affinity sites. None of the changes previously assigned to Ca(II) binding to the low affinity sites was observed. Since Mg(II) does not bind to the low affinity sites, these results confirm the previous assignments. The spectral differences between Mg(II) and Ca(II) show that the degree of backbone folding and interactions between a group of hydrophobic residues (one or more Val, Leu, Ile; two or more Phe) are different for the two cations. In the presence of excess Mg(II), at a molar ratio that may exist in vivo (approx. 40 : 1 mol ratio Mg(II): Ca(II), titration with Ca(II) leads to a displacement of Mg(II) and to all the structural changes previously observed for Ca(II) alone. However, in the presence of Mg(II) the distinction between high and low affinity sites is blurred as judged by the overlap of the spectral changes associated with each of the binding sites. This result, together with the observation that Mg(II) promotes structural changes different from Ca(II), suggests a structural basis for the observation that the Ca(II) threshold for the activation of tension in some myofibrils is increased in the presence of high Mg(II) concentrations.

Animals↗

PubMed2003

Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max)--an in situ spectroscopic study.

The thermal denaturation behaviour of glycinin solutions has been studied in situ as a function of ionic strength using various spectroscopic methods. Changes in secondary structure occurred at temperatures above 60 degrees C, well before the onset of gelation. Even after heating to 95 degrees C, much of the native beta-sheet structure of glycinin was retained, as indicated by the amide I peak maximum at 1635 cm(-1) in the Fourier transformed infrared (FT-IR) spectrum. This was accompanied by an increase in the 1625 cm(-1) band, indicative of the formation of intermolecular beta-sheet associated with protein aggregation. Nuclear magnetic resonance (NMR) spectroscopy confirmed the presence of highly mobile regions in glycinin comprising predominantly of Gln and Glu residues, corresponding to mobile regions previously identified by crystallographic studies. There was also evidence of a hydrogen-bonded structure within this mobile region, which may correspond to an alpha-helical region from Pro(256) to (or just before) Pro(269) in proglycinin. This structure disappeared at 95 degrees C, when heat-set gel formation occurred, as indicated by a sudden broadening and weakening of the NMR signal. Otherwise the NMR spectrum changed little during heating, emphasising the remarkable thermal stability of glycinin. It is proposed that during heating the core beta-barrel structure remains intact, but that the interface between the beta-domains melts, revealing hydrophobic faces which may then form new structures in a gel-network. As Cys(45), which forms the disulfide with Cys(12) linking the acidic and basic polypeptides, is found in this interface, such a rearrangement of the individual beta-domains could be accompanied by cleavage of this disulfide bond, as is observed experimentally. Such information contributes to our understanding the aggregative behaviour of proteins, and hence develops knowledge-based strategies for controlling and manipulating it.

Amino Acid Sequence↗

PubMed1998

Structural changes in blood vessels entering the growth plate during growth in rats.

We observed the structural changes in blood vessels entering the growth plates of the femur and tibia of rats during growth using scanning electron microscopy. The penetrating vessels had blind endings which were bulbous at a time when rats showed rapid skeletal development. With subsequent slowing of development, the density of the vessels decreased and the blind endings became short stumps. These changes were more prominent in the proximal femur than in the distal femur and proximal tibia. The present study indicates an intimate relation between endochondral ossification in the growth plate and the structure of the penetrating vessels.

Animals↗

PubMed1986

Analysis of structural changes during hypotonic swelling in Ehrlich ascites tumor cells.

Studies were undertaken to quantify structural changes associated with swelling of Ehrlich ascites tumor cells in hypotonic medium. Cells transferred from isotonic (294 mosmol/kg H2O) to hypotonic (98 mosmol/kg H2O) medium swelled rapidly. Subsequently, approximately 40% of the water initially gained was lost, a phenomenon referred to as volume-regulatory decrease (VRD). During the initial rapid cell swelling, blister-like protrusions or blebs were formed on the cell surface. These blebs were examined by routine light microscopy, differential interference-contrast (DIC) microscopy, and scanning and transmission electron microscopy. Microscopic observations and the distribution of ATPase antibodies indicated that the blebs were formed from plasma membrane. During VRD, the blebs coalesced to form a smooth but expanded membrane surface that appeared to be separated from the original cytoplasm by a layer of less dense ground substance. Computer-assisted morphometry from digitized DIC images of the initial swelling phase indicated that all of the volume gained was sequestered in the blebs. We suggest that bleb formation may allow increases in cell volume without disruption of cytoplasmic organization and may be a protective response to a variety of stressful stimuli. The subsequent VRD is accompanied by reduction of this expanded compartment.

Animals↗

PubMed1983

[Thermo-induced structural changes in lipoproteins of human plasma, studied with spin probes].

The thermo-induced structural changes in lipoproteins (LP) of human plasma were investigated by the electron paramagnetic resonance method, using 5-doxylstearate as a spin probe. LP were shown to undergo thermotropic transformations at temperatures specific for each LP type. Differences were found in the nature of temperature dependences of the order parameter for the probe localized in LP and for isolated lipids. The denser the LP, the more pronounced the differences. 5-Doxylstearate was shown to be localized not only in the lipid phase of LP, but also in the area of the protein--lipid contact. This indicates that 5-doxylstearate is a useful tool for the study of protein--lipid interactions in pathological processes coupled with their modifications.

Cyclic N-Oxides↗

PubMed2004

Time course of capillary structure changes in rat skeletal muscle following strenuous eccentric exercise.

AIM: We examined the time course of capillary structure changes in rat skeletal muscle at 1, 3 and 7 days after strenuous eccentric exercise. METHODS: The right gastrocnemius muscles of anaesthetized male Wistar rats were subjected to 300 controlled eccentric contractions using electrical stimulation. The contralateral gastrocnemius muscle was used as control. All morphometric parameters were determined in in situ perfused gastrocnemius muscles in red (Gr, predominantly slow-twitch fibre) and white (Gw, predominantly fast-twitch fibre) portions. RESULTS: Muscle fibre damage was evident on days 1, 3 and 7 in Gr (29.3-53.9% damaged fibres) and Gw (58.9-86.8% damaged fibres) of exercised legs. Electron micrographs of transverse sections did not display collapsed or obstructed capillaries in exercised legs, and capillary endothelial cells retained their normal structures. However, capillary luminal shapes and area were altered in exercised legs on days 1 and 3. The ratio between minimal and maximal capillary diameter in a transverse section (i.e. luminal ellipticity) significantly differed when comparing control (Gr, 0.75 +/- 0.02; Gw, 0.79 +/- 0.03) and exercised legs (Gr, 0.65 +/- 0.03; Gw, 0.66 +/- 0.04) at 1 day after exercise. The mean capillary luminal area was significantly increased in exercised legs after 1 day (Gw, +24.3%) and 3 days (Gr, +31.9%; Gw, +62.2%) compared with control. CONCLUSION: We conclude that (1) capillary endothelial cell structure was maintained in damaged muscles, (2) changes in capillary lumen shapes and distensibility occur in the degenerated muscle up to 3 days after the eccentric contraction period.

Animals↗

PubMed1985

X-ray analysis of structural changes induced by reduced nicotinamide adenine dinucleotide when bound to cysteine-46-carboxymethylated liver alcohol dehydrogenase.

The structure of the complex between Cys-46-carboxymethylated horse liver alcohol dehydrogenase (CM-LADH) and reduced nicotinamide adenine dinucleotide (NADH) has been determined by X-ray analysis. The complex represents NADH binding to the orthorhombic, "open" conformation of the enzyme. Coenzyme binding here induces a local structural change in the peptide loop 293-297, but there is no domain rotation, as observed for the "closed" conformation of the protein. This local movement of a few residues in the loop is sufficient to trap the nicotinamide ring of NADH within the active-site area close to a productive binding position. The carboxymethyl group on the zinc ligand cysteine-46 is oriented between the pyrophosphate bridge of NADH and the guanidinium group of arginine-369 and can occupy this position because the coenzyme binding cleft remains open and unchanged upon coenzyme binding. The zinc coordination sphere is distorted, and the position of the metal atom is shifted 1 A compared to native unliganded LADH. The distance between the zinc ion and the sulfur of the alkylated cysteine residue is of the order of 3 A. Alkylation experiments were performed at 0.15 and 10 mM iodoacetate, and peptide maps were examined. Gentle treatment with reagent yields an enzyme product which is substituted at only one of the two zinc binding sites per subunit of LADH (Cys-46). This enzyme species maintains its structural integrity; it binds coenzyme which induces conformational changes resolved into two steps. Thus, in addition to the orthorhombic complex, a crystalline NADH complex in the closed conformation of CM-LADH was obtained. These crystals showed enzymic activity, and single crystals were analyzed with microspectrophotometric methods. Formation of the stable crystalline abortive complex between CM-LADH-NAD+ and 4-trans-(N,N-dimethylamino)cinnamaldehyde (DACA) could be observed upon addition of excess aldehyde to the closed complex of CM-LADH-NADH. The CM-LADH-NAD+-DACA complex is characterized by an intense absorption band with a lambda max at 456 nm which corresponds to a shift in the spectrum of free DACA of approximately 60 nm. At the higher concentration of iodoacetate, three of the cysteine ligands to the second zinc atom (Cys-100, -103, and -111) are alkylated in addition to Cys-46. This enzyme product rapidly denatures and cannot be crystallized under our conditions. This is an experimental indication that the intact noncatalytic zinc binding site contributes to the structural stability of the protein.

Alcohol Dehydrogenase↗

PubMed2006

In situ monitoring of tendon structural changes by elastic scattering spectroscopy: correlation with changes in collagen fibril diameter and crimp.

The aim of this study was to monitor structural changes in loaded rabbit digital flexor tendons in situ and ex situ via elastic scattering spectroscopy (ESS). The optical setup consisted of a xenon white light source (lambda = 320-860 nm), connected to a fiber optic probe (with a source-detector separation of approximately 350 microm) and a spectrometer, controlled by a personal computer (PC). Cadaveric rabbit tendons were studied in situ under 3 tensional regimens: unloaded (no extrinsic tension applied), stretched, and 1-kg loaded and compared with excised tendons (i.e., no tension). Four times more light was detected in in situ unloaded tendons perpendicular to the tendon long axis than parallel to it. Backscatter anisotropy was expressed as the anisotropy factor (AF600nm: ratio of greatest to least backscatter intensity, measured with orthogonal probe positions). Differences in backscatter anisotropy between tendons from different digits were not significant. AF600nm had the smallest value (2.72 +/- 0.38) for the least aligned tendon preparations (excised tendons), and increased to 7.17 +/- 0.54 (1-kg loaded) as in situ loads were applied. Electron microscopy revealed that the distribution of collagen fibril diameters changed as loads were applied, with the diameter of larger fibrils decreasing approximately 33% for 1-kg loaded compared with excised tendons. Polarized light microscopy showed a characteristic crimp pattern in excised tendons, but this was hardly detectable in unloaded tendons and not detectable in tendons fixed in situ under a 1-kg load. We propose that the increase in optical anisotropy is a function of collagen fibril straightening and reducing fibril diameter as the tendon undergoes progressive loading. These findings are important for monitoring structure in vivo and in bioreactors for tissue engineers.

Animals↗

PubMed1982

Functional and structural changes in the rat kidney by long-term lithium treatment.

The relation between functional and structural renal changes induced by lithium was studied in rats during long-term treatment and after withdrawal of lithium. Administration of LiCl in the diet for up to 21 weeks caused marked polyuria associated with a significant lowering of renal concentrating ability assessed by dehydration and vasopressin tests. Plasma creatinine and plasma urea were not significantly changed by the treatment. Upon withdrawal of lithium water intake and concentrating ability were normalized within 4--8 weeks. Lithium caused focal light microscopic changes in the distal convoluted tubule and the collecting duct, consisting of nuclear and cellular polymorphism and, after prolonged treatment, dilatation of tubular lumens with tubular cell atrophy. These changes appeared later than the concentrating defect and persisted when lithium was withdrawn after prolonged treatment. No significant correlation was found between the degree of tubular changes and water intake or concentrating ability. It is concluded that the reversible diabetes insipidus induced by lithium in rats cannot be explained directly by the light microscopical changes observed in the distal part of the nephron, although the structural changes may be secondary to the polyuric state induced by lithium.

Animals↗

PubMed1999

A multi-step lipid mixing assay to model structural changes in cationic lipoplexes used for in vitro transfection.

Formation of liposome/polynucleotide complexes (lipoplexes) involves electrostatic interactions, which induce changes in liposome structure. The ability of these complexes to transfer DNA into cells is dependent on the physicochemical attributes of the complexes, therefore characterization of binding-induced changes in liposomes is critical for the development of lipid-based DNA delivery systems. To clarify the apparent lack of correlation between membrane fusion and in vitro transfection previously observed, we performed a multi-step lipid mixing assay to model the sequential steps involved in transfection. The roles of anion charge density, charge ratio and presence of salt on lipid mixing and liposome aggregation were investigated. The resonance-energy transfer method was used to monitor lipid mixing as cationic liposomes (DODAC/DOPE and DODAC/DOPC; 1:1 mole ratio) were combined with plasmid, oligonucleotides or Na(2)HPO(4). Cryo-transmission electron microscopy was performed to assess morphology. As plasmid or oligonucleotide concentration increased, lipid mixing and aggregation increased, but with Na(2)HPO(4) only aggregation occurred. NaCl (150 mM) reduced the extent of lipid mixing. Transfection studies suggest that the presence of salt during complexation had minimal effects on in vitro transfection. These data give new information about the effects of polynucleotide binding to cationic liposomes, illustrating the complicated nature of anion induced changes in liposome morphology and membrane behavior.

4-Chloro-7-nitrobenzofurazan↗