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At least 199 records · Page 11Linked to original sources
PubMed1985

An investigation of the structural changes occurring in a cetostearyl alcohol/cetrimide/water gel after prolonged low temperature (4 degrees C) storage.

Structural changes in a ternary gel prepared using the mixed emulsifier system of cetrimide and cetostearyl alcohol after prolonged low temperature (4 degrees C) storage have been studied using freeze-etch transmission electron microscopy and other techniques. The system changed from an opaque smooth gel of high viscosity, low conductivity and low free water, to a pearlescent milky lotion of low viscosity, high conductivity and high free water. Subsequent equilibration of the thinned system to room temperature (25 degrees C) over 48 h produced an opaque granular gel of similar consistency, but slightly higher conductivity and higher free water than the initial sample. Microscopical examination by both differential interference contrast and freeze-etch electron microscopy showed the system changed from one consisting of a liquid crystalline network localized around cetostearyl alcohol particles, to a system consisting of large waxy plates coexisting with some residual liquid crystalline network. A supportive mechanism for the thinning of the ternary gel at prolonged low temperature storage has been inferred by comparing data with that produced by other workers studying the fusion of phospholipid membranes considered to be morphologically similar to the liquid crystalline network observed in this ternary gel.

Cetrimonium↗
PubMed1969

Structural changes in Stigmatella aurantiaca during myxospore induction.

Suspension cultures of Stigmatella aurantiaca (Chondromyces aurantiacus) were induced to form myxospores by addition of glycerol to the growing culture. The cells were fixed at various stages during conversion, thin sections were prepared, and changes in fine structure were studied. Vegetative cells are quite similar in their ultrastructure to Myxococcus xanthus. During transformation into myxospores, three important cytological changes were observed. Granules of storage material, probably polysaccharide and polyphosphate, accumulated; a 200 to 300-mum thick capsule was laid down, and the outer triple layer of the cell wall became locally folded. These cell wall folds were often densely packed and lay in pockets formed by the cytoplasmic membrane. We have suggested the possibility that the cell may store in these folds wall material which has become superfluous by the decrease in surface area during conversion.

Bacteria↗
PubMed1975

Structural changes in the granulosa lutein cells of pregnant cows between 60 and 245 days.

The structural changes in the granulosa lutein cells in the pregnant cows between 60 and 245 days, were observed. The polyhedral or pump cells has an acidophilic cytoplasm around the spherical nucleus. The glycogen granules increased in number up to 230 days of pregnancy. The lipid globules increased in size and amount during advanced pregnancy. The mitochondria showed a wide range of variations in shape and size. The matrix of many mitochondria contained dense inclusions which replaced the entire matrix in late pregnancy. The endoplasmic reticulum was chiefly of smooth type but a few stacks of the rough variety could be seen in the early days of pregnancy. Sometimes, whorls of smooth-surfaced endoplasmic reticulum enclosing mitochondria were seen. The Golgi complex was fully developed in the granulosa cells of all cases studied. The dense granules and lipid globules increased in size and number in the older corpora lutea. The cell surface showed numerous infolding of the plasma membrane.

Animals↗
PubMed1988

[Structural changes in the small intestine wall and its lymphatic bed after gastrectomy].

Morphologically and histochemically structural changes of the small intestine wall and its lymphatic bed have been studied in 104 dogs after the stomach resection. After the operation an increase in the diameter of the lymphatic capillaries and vessels takes place. Lateral dilatations and protrusions in the capillary walls appear, new anastomoses in all the membranes are formed, they are mostly manifested in the mucous membrane. Histopathological rearrangement in the small intestine wall is demonstrated as edema of the mucous membrane, as plethora of the vessels, as lymphoid infiltration and as changes of the villi forms.

Animals↗
PubMed1987

[Analysis of cytoskeleton structural changes in the granular cells of the frog bladder during the stimulation of water transport].

Structural changes of the cytoskeleton of the frog urinary bladder granular cells were examined during low and high water permeability of the epithelium. A tight connection of the microfilaments and microtubules with vacuolar membranes and a great increase in the number of microtubules during a stimulated water flow was shown using different electron microscopic methods. Two populations of microtubules were discovered, respectively, with different diameter and different rate of stability. It is suggested that the thicker microtubules while interacting with actin microfilaments through associated electron dense globules may fulfil the transport function in the cell.

Animals↗
PubMedDate not supplied

[Structural changes to the skin in the area of gunshot wounds].

Microscopic changes in skin structures around gunshot and stabbed wounds, which may be used as features characterizing injury volume were studied. Factors influencing the significance of these changes were presented and mechanisms of their occurrence is discussed.

Cadaver↗
PubMed1995

Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding pathway.

The three-dimensional solution structure of (Cd2+)1-calbindin D9k has been determined by distance geometry, restrained molecular dynamics and relaxation matrix calculations using experimental constraints obtained from two-dimensional 1H and 15N-1H NMR spectroscopy. The final input data consisted of 1055 NOE distance constraints and 71 dihedral angle constraints, corresponding to 15 constraints per residue on average. The resulting ensemble of 24 structures has no distance or dihedral angle constraints consistently violated by more than 0.07 A and 1.8 degrees, respectively. The structure is characteristic of an EF-hand protein, with two helix-loop-helix calcium binding motifs joined by a flexible linker, and a short anti-parallel beta-type interaction between the two ion-binding sites. The four helices are well defined with a root mean square deviation from the mean coordinates of 0.35 A for the backbone atoms. The structure of the half-saturated cadmium state was compared with the previously determined solution structures of the apo and fully calcium saturated calbindin D9k. The comparisons were aided by introducing the ensemble averaged distance difference matrix as a tool for analyzing differences between two ensembles of structures. Detailed analyses of differences between the three states in backbone and side-chain dihedral angles, hydrogen bonds, interatomic distances, and packing of the hydrophobic core reveal the reorganization of the protein that occurs upon ion binding. Overall, it was found that (Cd2+)1-calbindin D9k, representing the half-saturated calcium state with an ion in site II, is structurally more similar to the fully calcium-saturated state than the apo state. Thus, for the binding sequence apo-->(Ca2+)II1-->(Ca2+)I,II2, the structural changes occurring upon ion binding are most pronounced for the first binding step, an observation that bears significantly on the molecular basis for cooperative calcium binding in calbindin D9k.

Animals↗
PubMed1976

Novel mutation that causes a structural change in a lipoprotein in the outer membrane of Escherichia coli.

A novel mutation which caused a structural change in a lipoprotein in the outer-membrane has been found in Escherichia coli K-12. The lipoprotein of the wild-type strain is known to have a peculiar amino terminal structure: glycerylcysteine with two fatty acids attached by ester linkages and one fatty acid by an amide linkage. In contrast to the wild-type lipoprotein, the mutant lipoproteins is isolated from the E. coli envelope as a dimer of molecular weight of about 15,000. The dimer can be reduced by mercaptoethanol to the lipoprotein monomer of molecular weight of about 7,500. The monomer has a free thiol group which is susceptible to monoiodacetie mutant lipoprotein is extremely low in comparison with that into the wild-type lipoprotein. These results suggest that the mutant is defective in transferring a glycerol group to the thiol group of the amino terminal cysteine residue of the lipoprotein. The gene responsible for this modification reaction has been located at 36.5 min on the E. coli chromosome.

Bacterial Proteins↗
PubMed1988

Lithium-induced structural changes in the cortical distal nephron localized by computer-assisted three-dimensional reconstruction.

Lithium treatment is known to cause tubule dilation in distal nephron segments both in rat and in man. However, due to the heterogeneous cell composition of the distal nephron and the cellular changes following lithium treatment, it has been difficult to identify the structurally changed segments. In this study we have therefore applied computer-assisted reconstruction of cortical distal nephron segments. Tubule dilation was demonstrated in connecting and initial collecting tubules and in the first part of cortical collecting ducts (CCD) whereas it was absent from distal straight and distal convoluted tubules. Principal cells (P cells) in the CCD showed swelling of the cytoplasm, accumulation of actin-like microfilaments, and abnormal arrangements of basolateral membranes. Connecting tubule cells (CNT cells) showed similar but less pronounced changes. Intercalated cells (I cells) showed an accumulation of vesicles in the apical cytoplasm and a reduced luminal surface area. Lesions in P and CNT cells may, at least in part, explain the diabetes insipidus and sodium loss found during lithium treatment. Proton secretion in I cells is probably mediated by an ATPase present in the luminal membrane. The reduction in area of this membrane may explain why lithium-treated animals have a lowered ability to excrete an acid load.

Animals↗
PubMed1995

Photoinduced structural changes in the collagen/gelatin binding domain of fibronectin.

Prolonged exposure of human plasma fibronectin (pFn) and its 40- and 21-kDa collagen/gelatin binding fragments (GBFs) to 280-nm irradiation decreased their affinity for gelatin and for TR-CB7, a fluorescently labeled CNBr fragment of the alpha-1 chain of type I collagen. Fluorescence polarization binding assays of TR-CB7 with pFn and the 40-kDa GBF yielded progressively higher Kd's with increased time of exposure to 280-nm light at 25 degrees C. Binding of nonirradiated and irradiated pFn and fragments to gelatin-Sepharose correlated with the polarization data, confirming diminished gelatin binding following exposure to 280-nm light. Fluorescence spectra of intrinsic tryptophans in the 21- and 40-kDa GBFs exhibited changes indicative of photoinduced conformational changes; the maximum fluorescence wavelength red-shifted from between 340 and 350 nm to 360 nm, with concomitant increases in fluorescence intensity. Exposure of 21- and 40-kDa GBFs and pFn to 280-nm light also generated approximately two, four, and six free sulfhydryl groups per molecule, respectively. No sulfhydryl release was observed in other Trp- and disulfide-containing proteins under the same conditions. We propose that the fluorescence changes as well as the changes in affinity for gelatin or the collagen fragment result from structural changes secondary to the breakage of disulfide bonds, as a consequence of energy transfer from nearby tryptophans in one or more of the Fn type I repeats in the gelatin binding region of fibronectin.

Collagen↗
PubMed1987

Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.

Electron microscopy has been used to study the structural changes that occur in the myosin filaments of tarantula striated muscle when they are phosphorylated. Myosin filaments in muscle homogenates maintained in relaxing conditions (ATP, EGTA) are found to have nonphosphorylated regulatory light chains as shown by urea/glycerol gel electrophoresis and [32P]phosphate autoradiography. Negative staining reveals an ordered, helical arrangement of crossbridges in these filaments, in which the heads from axially neighboring myosin molecules appear to interact with each other. When the free Ca2+ concentration in a homogenate is raised to 10(-4) M, or when a Ca2+-insensitive myosin light chain kinase is added at low Ca2+ (10(-8) M), the regulatory light chains of myosin become rapidly phosphorylated. Phosphorylation is accompanied by potentiation of the actin activation of the myosin Mg-ATPase activity and by loss of order of the helical crossbridge arrangement characteristic of the relaxed filament. We suggest that in the relaxed state, when the regulatory light chains are not phosphorylated, the myosin heads are held down on the filament backbone by head-head interactions or by interactions of the heads with the filament backbone. Phosphorylation of the light chains may alter these interactions so that the crossbridges become more loosely associated with the filament backbone giving rise to the observed changes and facilitating crossbridge interaction with actin.

Actin Cytoskeleton↗
PubMed1989

Left ventricular structural changes in young men at increased risk of developing essential hypertension. Assessment by echocardiography.

Left ventricular structural changes were assessed by echocardiography in young men at increased risk of developing essential hypertension. Four groups were investigated: 28 normotensive offspring of hypertensives (NTO), 20 borderline hypertensive offspring of hypertensives (BHO), 12 borderline hypertensives with normotensive parents (BH) and 28 normotensive subjects with normotensive parents (NT). The septum-posterior wall ratio was increased in the risk groups (NT, BHO, BH). The increased ratio could be explained by both heredity and elevated blood pressure. Left ventricular mass index (LVMI) correlated strongly with physical activity in the NT group, so LVMI was adjusted accordingly. The adjusted LVMI was significantly increased in the risk groups. The increase in the adjusted LVMI could best be explained by the elevated blood pressure and not by heredity. Multivariate analysis of variance showed that physical activity is an independent predictor of LVMI only in the NT group and that systolic blood pressure is an independent predictor of LVMI only in the risk groups.

Adolescent↗
PubMed1982

Evidence of early structural change in the artery wall of two-kidney one-clip Goldblatt hypertensive rats.

Vascular structural changes were studied during the development of two-kidney one-clip renal hypertension. The weight of the arteries and the concentration and total amount of ribonucleic acid, deoxyribonucleic acid, alkali-soluble proteins, collagen and elastin of the vascular wall were measured. Tritiated thymidine uptake was also determined 15 and 30 days after clipping. Hypertension developed in 58% of the animals while the rest remained normotensive. A significant increase in artery weight and in the total amount of nucleic acids and proteins was found in hypertensive rats. The uptake of 3H thymidine by the arteries of hypertensive rats was significantly increased 15 days after clipping. This increment showed a significant correlation with blood pressure levels. Present data seem to indicate that the increase in vessel wall dimensions observed is partly due to an increase in the number of smooth muscle cells during the acute phase; this alteration appears to be mainly due to the rise in blood pressure.

Animals↗
PubMed1981

[Structural changes in the soleus muscle of rats on the Kosmos-series biosatellites and in hypokinesia].

Structural changes in the soleus muscle of rats used in flight and synchronous experiments of the Cosmos program and hypokinetic studies have been investigated. It is hypothesized that focal edema and dystrophic changes observed in flight, synchronous and hypokinetic rats can be caused by circulation disorders of different etiology. In flight and synchronous rats they develop two days postflight due to the deconditioning of the muscle tissue and intraorgan vascular system which fail to meet the requirements after transition from 0 g to 1 g. In hypokinetic rats circulation disorders occur on the first experimental day due to mechanical causes (paws are pressed against the cage floor impeding venous outflow) and muscle pump deficiency. In all cases circulation disorders seem to be associated with peculiar features of angioarchitectonics of the soleus muscle.

Animals↗
PubMed1981

Structural changes in BHK cell plasma membrane caused by the binding of vesicular stomatitis virus.

Spin label electron spin resonance techniques using a nitroxide derivative of stearic acid were used to detect changes in plasma membrane structure caused by the binding of vesicular stomatitis virus (VSV) to cell plasma membranes of intact BHK-21 cells. The results indicate that binding of VSV to cell surface receptors causes an increase in the observed rigidity of the plasma membrane lipid bilayer. This change in membrane structure, which appears to be caused by the cross-linking of receptors in the plane of the plasma membrane, could be prevented by treating the cells with colchicine before addition of virus and could be reversed by treating the cells with colchicine after addition of virus. Cells treated with a monovalent, water-soluble derivative of VSV G-protein (Gs) did not show an increase in plasma membrane bilayer rigidity. However, addition of anti-VSV G-protein immunoglobulin G to cells pretreated with G8 caused an increase in plasma membrane bilayer rigidity. This increased rigidity could also be reversed by the addition of colchicine. Fluorescence microscopy was used to determine the distribution of fluorescein-labeled VSV particles on the cell surface after addition of virus. Approximately 30 min after addition of virus, discrete areas on the cell surface showed fluorescent staining, which coalesced to apical regions of the cell after approximately 40 min.

Animals↗
PubMed1989

Structural changes in myosin subfragment 1 by mild denaturation and proteolysis probed by antibodies.

The perturbations in the structure of myosin subfragment 1 (S1) by mild denaturation or proteolysis were investigated by measuring the inhibition of the binding of antibodies to immobilized S1 by treated S1 in a solution-phase competitive immunochemical assay. The structural changes in S1 were probed by using anti-50-kDa segment, anti-N-terminus, anti-27-kDa segment, and anti-A1 light chain monoclonal antibodies (MAbs). Methanol and heat denaturation increased MAb binding to the 50-kDa segment. MAb binding to regions in the 27-kDa segment was also promoted, slightly by methanol and more drastically by heat. Proteolysis also induced structural alterations in 50- and 27-kDa segments as shown by increased MAb binding to these regions in cleaved S1. These results indicate that mild denaturation and proteolysis induce structural perturbations which alter the epitope accessibility in 50- and 27-kDa segments of S1 and that antibody binding studies afford a sensitive probe to such perturbations.

Animals↗
PubMed1995

Immunochemical analysis of the structure of diphtheria toxin shows all three domains undergo structural changes at low pH.

Diphtheria toxin is a bacterial protein that undergoes a physiologically critical conformational change at low pH. This change involves a partial unfolding event forming a molten globule-like structure, which exposes hydrophobic regions and which allows the toxin to insert into, and translocate across, membranes. In this report, antibody binding was used to examine the regions of the toxin that undergo structural changes at low pH. Monoclonal antibodies specific to the catalytic (C), transmembrane (T), and receptor-binding (R) domains of diphtheria toxin were prepared and isolated. In addition, the binding of anti-peptide antibodies raised against peptides in the C and T domains to toxin was examined. Anti-C monoclonals and antipeptide antibodies were found to bind preferentially to low pH-treated toxin relative to native toxin. Anti-T and anti-R monoclonal binding ranged between preference for native toxin and preference for low pH-treated toxin. These results suggest that the C domain becomes more exposed to solution at low pH, and that both the T and R domains of the B chain undergo major conformational changes at low pH. Based on these results, a model in which low pH induces several coordinated changes in intra- and inter-domain interactions is suggested. The participation of the R domain in these changes is of particular significance because it suggests that the R domain plays a more important role in low pH-induced changes than previously realized.

Animals↗
PubMed1991

Structural changes in aging bone: osteopenia in the proximal femurs of female mice.

A computerized image analysis system was used to quantitate age-related changes in the structure of the proximal femur in CW-1 female mice, ranging from 3 to 32 months of age. Morphological findings revealed a progressive thinning of bone trabeculae within the femoral head, accompanied by the development of marrow cavities in the cortical bone of the femoral neck and in the subchondral bone. As a result, the compact bone in senescent mice acquired an appearance similar to trabecular bone. Quantitative image analysis revealed a similarity in the pattern of changes in the three types of bone: cortical, trabecular, and subchondral. Bone density increased from 3 to 12 months of age and subsequently declined. A similar pattern was noted for the changes in the thickness of the cortical and the subchondral bone. Regression analysis revealed that the changes with age fitted a second-order model; thus it was possible to predict the age of maximal values for each parameter. Hence, the age of maximal bone density for cortical, trabecular, and subchondral bone was 12.3, 14.8, and 18.0 months, respectively. The rate of bone loss after 12 months was most prominent for trabecular bone (1.47% per month), so that by 32 months of age its overall mass had declined by 57% in comparison to peak values seen at 12 months of age (p less than 0.001). The density of the subchondral and cortical bones decreased at a slower rate (0.6% to 0.8% per month) and at the age of 32 months their values had decreased by 12% to 18% in comparison to those at 12 months (p less than 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)

Aging↗