Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011570 (depression)
 172,036 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It was discovered that the product of a mix containing the enzyme creatine phosphokinase (CPK) and either glutathione (GSH) or cysteine caused platelets to adhere together in vitro. This platelet adhesive factor (PAF) was formed as CPK enzyme activity declined. An alternative method for the destruction of enzyme activity--heat at 56 degrees C--also resulted in the formation of an in-vitro active PAF which was both less stable and active than its chemically produced counterpart. Assay of the platelet adhesive potency of the CPK-GSH mix, using human platelets, revealed a wide variation in the response of different individuals' platelets to standard quantities of PAF. The nature of this preparation of PAF was investigated by both biochemical and biophysical means, including ion exchange chromatography, electrophoresis, amino acid analysis and analytical ultracentrifuge studies. Evidence is presented that PAF is the product of the disruption of the dimeric structure of the CPK molecule. PAF was found to adhere to paper, under the conditions of electrophoresis imposed, and also to cause sephadex beads to bind together, characteristics which suggested that the platelet adhesion reaction was probably a biophysical process. Red and white cells were not similarly affected. The feasibility of this novel concept for the initiation of platelet adhesion, as a naturally occurring process, was supported by the results of animal experiments in which a statistically depression of platelets in the systemic circulation followed the intravascular administration of PAF. The possible relevance to man of this basic mechanism in relation to exercise and disease processes, including ideopathic and post-traumatic thrombosis, atherogenesis, and dysbaric aseptic necrosis of bone, is discussed.
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PMID:The formation of a platelet adhesive factor by disruption of the creatine phosphokinase molecule. 1 Mar 63

In our previous study (Onishi, H., Susuki, H., Nakamura, k., and Watanabe, S. J. Biochem. 83, 835-847, 1978), we found it to be characteristic of chicken gizzard myosin that thick filaments of gizzard myosin are readily disassembled by a stoichiometric amount of ATP (3 mol of ATP per mol of myosin), and that the ATPase activity of gizzard myosin in the ATP-disassembled state is much lower than that of gizzard myosin disassembled by a high concentration of KCl. We now report the following findings: (1) Thick filaments of (unphosphorylated) gizzard myosin can be in a bipolar structure or in a non-polar structure, depending on the method of preparing the thick filaments. (2) Thick filaments of (unphosphorylated) gizzard myosin in either the bioplar or the non-polar structure are readily disassembled by ATP. (3) Addition of rabbit skeletal C-protein does not confer ATP resistance on thick filaments of (unphosphorylated) gizzard myosin. (4) Unphosphorylated) gizzard myosin in the ATP-disassembled state is in a dimeric form as determined by ultracentrifugation. Moreover, 0.2 M KCl-dissociated gizzard myosin in monomeric form is converted to a dimeric form by ATP. (5) The Mg-ATPase activity of (unphosphorylated) gizzard myosin is much lower in its dimeric form (less than one-tenth) than in its monomeric form. The activity depression observed around 0.15 M KCl is therefore due to the formation of myosin dimers. (6) Skeletal L-meromyosin can increase the very low activity of (unphosphorylated) gizzard myosin ATPase at low ionic strength (0.13 M KCl) by forming ATP-resistant hybrid filaments with (unphosphorylated) gizzard myosin, preventing the formation of myosin dimers. (7) Gizzard myosin in which one of the light-chain components is phosphorylated by myosin light-chain kinase can form thick filaments which are resistant to the disassembling action of ATP. (8) Even in the presence of ATP, thick filaments of phosphorylated gizzard myosin do not disassembled into myosin dimers. Accordingly, the ATPase activity of phosphorylated gizzard myosin does not show activity depression at low ionic strength.
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PMID:Structure and function of chicken gizzard myosin. 15 5

The effects of slow (10 min) i.v. infusions of contrast media (CM, 1,600 mg I/kg b.w.) on single nephron glomerular filtration rate (SNGFR) in the rat kidney were investigated using a micropuncture technique. Diatrizoate, iohexol, or ioxaglate did not change SNGFR, although a tendency towards a transient suppression was seen during the infusion phase. Iotrolan infusion, however, decreased SNGFR (p < 0.05) and the value still remained below the control value 25 min after the start of infusion. Iotrolan is a nonionic dimeric CM and has a lower osmotic effect in the tubules than the ionic dimeric CM and the monomeric CM when given in iodine equivalent doses. These characteristics of iotrolan have probably some influence on the depression of SNGFR after iotrolan injection.
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PMID:Influence of contrast media on single nephron glomerular filtration rate in rat kidney. A comparison between diatrizoate, iohexol, ioxaglate, and iotrolan. 144 88

The molecular structures of phosphorylase b and phosphorylase kinase have been visualized by scanning tunneling microscopy (STM). STM is a near field technique that can resolve structures at the nanometer level and thus can image individual molecules. Phosphorylase b can be seen in dimeric and tetrameric forms as well as linear and globular aggregates. The linear arrays consist of side by side dimers with the long axis of the dimer perpendicular to the aggregated chain. Individual molecules of phosphorylase kinase appear to be planar, bilobate structures with a 2-fold axis of symmetry and a central depression.
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PMID:Direct observation of phosphorylase kinase and phosphorylase b by scanning tunneling microscopy. 251 65

The Interaction of the cro protein of lambda phage with a synthetic OR3 operator having 17 base pairs in length and with its 9 bp fragment has been studied using the circular dichroism (CD) method. In both cases, a considerable change in the CD of the samples was found in the region 260-300 nm upon the addition of the cro protein. The stoichiometry obtained by the CD titration was identical for OR3 and its 9 bp fragment: one duplex per dimeric cro. NaCl addition makes the complexes dissociate so that the 9 bp fragment becomes free at [NaCl] greater than 0.2 M while the whole OR3 becomes free at [NaCl] greater than 0.5 M. The CD spectra of both the free duplexes show a typical B-form conservative pattern with a positive CD band (270 nm) and a negative one (250 nm). The specific complexing of both the duplexes results in a substantial CD depression in the positive band. The most pronounced effect occurs at 280 nm. This spectral change is quite distinct from those in the B to A transition and in the non-cooperative winding of the DNA within the B-family of forms. The interaction of the cro protein with the non-operator DNAs, calf thymus DNA and a synthetic 10 bp duplex, reveals no visible CD changes at all. An inference is drawn that the CD change in the specific complexes is mainly due to the induced CD in tyr-26 upon its interaction with a specific base pair in the operator or its fragment, the operator DNA conformation being conserved in a B-like form as a whole.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The absence of non-local conformational changes in OR3 operator DNA on complexing with the cro repressor. 297 19

The chemistry of low-osmolality contrast agents is reviewed, the effects of these agents on vascular and organ physiology are compared with the effects of conventional ionic contrast media, and guidelines for intravascular use of the low-osmolality agents in selected high-risk patients are presented. Three low-osmolality contrast agents, the nonionic media iohexol (Omnipaque, Winthrop-Breon) and iopamidol (Isovue, Squibb) and the dimeric medium ioxaglate meglumine-sodium (Hexabrix, Mallinckrodt) have recently been introduced into the contrast-media market. Compared with conventional ionic contrast media, these new agents demonstrate approximately one third of the osmolality per given iodine concentration (degree of roentgenographic opacification). Therefore, the risks of hyperosmolarity-induced reactions to contrast media are lower with the new agents. The low-osmolality agents may be associated with a reduced incidence of contrast-media-induced hypersensitivity reactions. Because of their lower osmolality, these agents produce less vessel dilation, vascular endothelial damage, and associated pain and discomfort than equi-iodine concentrations of the conventional ionic media. They also demonstrate a reduction in the incidence and severity of contrast-media-induced renal vasoconstriction and proteinuria, hemodynamic alterations, negative chronotropic effects, depression of myocardial contractility, and neurotoxicity in the presence of an altered blood-brain barrier. These low-osmolality agents produce fewer undesirable physiological effects than conventional contrast agents, but the cost of the new products can be more than 10 times as great. Therefore, the new products should be used selectively in patients known to be at increased risk for reactions to intravascular contrast media. A scoring system was developed to permit rapid recognition of documented single or multiple risk factors and subsequent determination of whether to administer a low-osmolality agent.
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PMID:Evaluation of intravascular low-osmolality contrast agents. 378 Jan 59

The refined high resolution crystal structure of the bovine phospholipase A2 was compared with its counterpart from the venom of Crotalus atrox, the western diamondbacked rattlesnake. The strong similarity in their backbone conformations forms the basis of a common numbering system for the amino acid sequence. The three common major helices and much of the extended chain form a nearly identical "homologous core" structure. The variations in conformation usually arise from deletions/insertions or en bloc shifts of structural units. The exception to this is part of the highly conserved calcium-binding loop; however, this is to be expected as 1) there is no calcium ion sequestered in the venom dimer as there is in the case of the bovine enzyme and 2) two side chains in that segment form dimer-stabilizing interactions between the subunits of the C. atrox enzyme. The absolutely conserved catalytic network of hydrogen-bonded side chains formed by His 48, Tyr 52, Tyr 73, and Asp 99, as well as the hydrophobic wall that shields it, are virtually superimposable in the two structures. However, the details of the structural relationship between the amino terminus and the catalytic network differ in the two species and the ordered water molecules thought to be either functionally or structurally important in the pancreatic enzymes are not found in the crystal structure of the phospholipase A2 from C. atrox. The most striking difference from a functional standpoint is the fact that the surface depression in the region of the catalytic network that has been commonly considered the active site is shielded substantially in forming the intersubunit contact surface of the dimeric venom enzyme.
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PMID:A comparison of the crystal structures of phospholipase A2 from bovine pancreas and Crotalus atrox venom. 404 72

The electroneutral exchange of chloride and bicarbonate across the human erythrocyte membrane is facilitated by Band 3, a 911 amino acid glycoprotein consisting of a 43 kDa N-terminal cytosolic domain that binds the cytoskeleton, haemoglobin and glycolytic enzymes and a 52 kDa C-terminal membrane domain that mediates anion transport. Electron microscopy and three-dimensional image reconstruction of negatively stained two-dimensional crystals of the dimeric membrane domain revealed a U-shaped structure with dimensions of 60 x 110 A, and a thickness of 80 A. The structure is open on the top and at the sides, with the monomers in close contact at the base. The basal domain is 40 A thick and probably spans the lipid bilayer. The upper part of the dimer consists of two elongated protrusions measuring 25 x 80 A in projection, with a thickness of 40 A. The protrusions form the sides of a canyon, enclosing a wide space that narrows down and converges into a depression at the centre of the dimer on the top of the basal domain. This depression may represent the opening to a transport channel located at the dimer interface. Based on the available protein-chemical data, the two protrusions face the cytosolic side of the membrane and they appear to be dynamic.
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PMID:Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3. 804 53

Since the first animal coronary arteriogram in 1933 there have been many innovations in techniques and contrast media. From 1933 through the late 1950s the procedures used involved nonselective aortic injections and the use of acetylcholine to slow the heart. The first selective coronary arteriogram in animals was performed by West, Kobayashi & Guzman in 1958 (45) and in 1959 Guzman & West (7) observed ventricular fibrillation with some media but not others. In 1967 Judkins (14) described the catheter designs for right and left coronary catheterizations that we still use today. In the 1970s and 80s many authors observed the ionic monomeric contrast media reduced plasma calcium causing fibrillation and myocardial depression. Supplementation of ionic media with calcium was shown to moderate these adverse effects. Almen's vision of low osmolality contrast media and the creation of metrizamide (1) stimulated the rapid development of monomeric and dimeric nonionic contrast media. The ionic dimeric medium ioxaglate also provided low osmolality. Digital frame grabbers and computers lead to the development of digital subtraction angiography and new applications of arteriography, frequently using dilute media. Unexpectedly, during prolonged right coronary arteriography in animals, dilute nonionic media were found to produce increased fibrillation as compared to dilute ionic media. The addition of sodium to nonionic media significantly reduced the incidence of fibrillation. Animal studies with the nonionic medium iodixanol supplemented with sodium and calcium (Visipaque) have demonstrated minimal incidences of fibrillation and myocardial depression.
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PMID:A review of coronary arteriography- and contrast media-induced ventricular fibrillation. 861 May 3

The tertiary and quaternary structure of the lectin I from Ulex europaeus (UE-I) has been determined to 2.2 A resolution. UE-I is a dimeric metalloglycoprotein that binds the H-type 2 human blood group determinant [alpha-L-Fucalpha(1-->2)-beta-D-Galbeta(1-->4)-beta-D-Glc NAcalpha-]. Nine changes from the published amino acid sequence were necessary to account for the electron density. The quaternary structural organization of UE-I is that of the most commonly occurring legume lectin dimer. The tertiary structure of the monomeric subunits is similar to that in the conventional lectin subunit; however, some structural differences are noted. These differences include a four-stranded anti-parallel "S" sheet in UE-I versus the five-stranded S sheet in other lectin monomers. The Ala residue of the Ala-Asp cis-peptide bond present in the carbohydrate-binding site of the conventional lectin monomer is replaced with a Thr in the UE-I structure. Also, a novel disulfide bridge linking Cys115 and Cys150 is present. There are two metallic ions, one calcium and the other manganese, per subunit. N-linked oligosaccharides are at residues 23 and 111 of each subunit. One molecule of R-2-methyl-2, 4-pentanediol (R-MPD) is present in a shallow depression on the surface of each subunit. In order to examine the binding of the H-type 2 blood group determinant by UE-I, its beta-methyl glycoside (H-type 2-OMe) was docked into the binding site of R-MPD. The epitope previously identified for H-type 2-OMe by chemical mapping proved, with only minor adjustment of amino acid residues, to be complementary to the shallow cavity occupied by R-MPD in the structure. Several key interactions have been proposed between the H-type 2-OMe and UE-I.
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PMID:The 2.2 A resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus. 1109 Feb 84


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