• Title/Summary/Keyword: Plasma proteins

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Effects of Dietary Casein, Soy, and Methionine-Supplemented Soy on Serum Lipids Level in Rats

  • Choi, Mi-Ja;Jung, So-Hyung
    • Preventive Nutrition and Food Science
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    • v.7 no.3
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    • pp.278-281
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    • 2002
  • The objective of the current study was to determine the influences of dietary proteins and methionine on plasma lipid concentrations. Thirty growing male Sprague-Dawley rats were fed diets similar in all respects except that dietary protein was from either casein, soy protein isolate, or soy protein isolate supplemented with L-methionine (0.24 %). The animals were fed experimental diets ad libitum for nine weeks. Plasma total-cholesterol concentrations were unaffected by the protein source or methionine supplementation. Plasma triglyceride concentrations were lower in rats of methionine supplemented soy protein diets (76 mg/dL) than in the rats fed casein or soy diet (120 mg/dL, 109 mg/dL, respectively). These results indicate that soy protein reduces plasma triglycerides relative to casein in rats fed cholesterol free diets, and that methionine-supplemented soy diets decrease plasma triglyceride concentrations more than soy protein alone.

An Anticoagulant/Fibrinolytic Protease from Lumbricus rubellus

  • Jeon, Ok-Hee;Moon, Woong-Joon;Kim, Doo-Sik
    • BMB Reports
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    • v.28 no.2
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    • pp.138-142
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    • 1995
  • An anticoagulant/fibrinolytic protease was purified to homogeneity from the earthworm Lumbricus rubellus. The protein was a single chain glycoprotein of 32 kDa that exhibited strong proteolytic activity on human thrombin and fibrin clots. Proteolytic degradation of these plasma proteins by the purified enzyme occurred at a neutral pH range. Among several human plasma proteins tested as possible substrates for the protease reaction, the 32 kDa enzyme specifically hydrolyzed both thrombin and fibrin polymers without affecting other proteins, such as serum albumin, immunoglobulin, and hemoglobin. Treatment of the purified enzyme at neutral pH with either phenylmethylsulfonylfluoride or soybean trypsin inhibitor resulted in a loss of catalytic activity. The enzyme hydrolyzed the chromogenic substrate H-D-Phe-L-Pipecolyl-L-Arg-p-nitroanilide with a $K_m$ value of 1.1 ${\mu}M$ at a neutral pH. These results suggest that the anticoagulant/fibrinolytic enzyme from Lumbricus rubellus is a member of the serine protease family having a trypsin-like active site, and one of the potential clevage sites for the enzyme is the carbonyl side of arginine residues in polypeptide chains.

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Inhibitory Effects of Bovine Serum Albumin on Cytotoxicity and Mutagenicity of 6-Sulfooxymethylbenzo[a]pyrene

  • Cho, Young-Sik;Cho, Kyung-Joo;Chung, An-Sik
    • Toxicological Research
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    • v.16 no.3
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    • pp.221-227
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    • 2000
  • A 6-sulfooxymethylbenzo[a]pyrene (SMBP), the ultimate metabolite of methyl-substituted benzo[a]pyrene (BP), has been found to be carcinogenic in mice. These properties may be attributable to its strong reactivity with cellular macromolecules such as DNA. However, serum and its major constituent albumin attenuated significantly the cytotoxicity and mutagenicity of 5MBP in bacterial and mammalian cell systems. This inhibitory activity of serum against 5MBP-induced cytotoxicity and mutagenicity in Chinese hamster V79 cells appears to be caused by the reduced macromolecular adducts such as DNA and proteins, but serum failed to reduce 5MBP binding to naked calf thymus DNA. A number of proteins in the serum could act as nucleophiles that are able to intercept reactive chemicals through covalent binding. Albumin present in the plasma seems to be one of major components responsible for direct binding with 5MBp, thereby reducing its reactivity to genetic materials. We here determined which fraction is preferential for 5MBP binding through fractionation of 5MBP-treated serum with ammonium sulfate. The albumin-containing fraction had slightly more affinity for 5MBP than the immunoglobulin-containing fraction. Our results indicate that the covalent modification of plasma proteins may reduce 5MBP-induced damage.

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Effects of Insulin-like Growth Factor-I (IGF-I) on Body Weight and the Cocentration of Serum IGF Binding Proteins in Korean Rockfish (Sebastes schlegeli) (Insulin-like growth factor-I(IGE-I)이 조피볼락의 체중 및 혈액중 IGF binding proteins에 미치는 영향)

  • NAM Taek-Jeong;LEE Sang-Mi;PYEUN Jae-Hyeung
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.5
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    • pp.774-778
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    • 1998
  • The effect of insulin-like growth factor-I (IGF-I) on circulating insulin-like growth factor binding proteins (IGFBPs) in the Korean rockfish, Sebastes schlegeli, was assessed after injected of recombinant human IGF-I (6 $\mu$g/100 g body weight). Growth and metabolic status of each fish were assessed by determing body length and body weight changes, and serum glucose concentration. Serum IGF binding proteins concentrations were assessed by the Western ligand blot procedure using $^{125}I$-labeled human IGF-I tracer. The fish received IGF-I were Heavier than the saline-injected control fish after 2 weeks of treatment. Plasma IGFBP-3 concentration inclosed, but plasma IGFBP-1 and glucose levels decreased significantly after administration. Taken together, the findings of this study suggest that human IGF-I is biologically active in Korean rockfish and may be of significance in metabolic and growth-related processes.

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Sodium/chloride-Dependent Transporters: Elucidation of Their Properties Using the Dopamine Transporter

  • Caron, Marc G.
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.88-93
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    • 1994
  • The mechanisms controlling the intensity and duration of synaptic transmission are numerous. Once an action potential reaches a nerve terminal, the stored neurotransmitters are released in a quantum fashion into the synaptic cleft. At that point neurotransmitters can act on post-synaptic receptors to elicit an action on the post-synaptic cell or net at so-called auto-receptors that are located on the presynaptic side and which often regulate the further release of the neutotransmitter. Whereas the action of the neurotransmitter receptors is regulated by desensitization phenomenon, the major mechanism by which the intensity and duration of neurotransmitter action is presumably regulated by either its degradation or its removal from the synaptic cleft. In the central nervous system, specialized proteins located in fe plasma membrane of presynaptic terminals function to rapidly remove neurotransmitters from the synaptic cleft in a sodium chloride-dependent fashion. These proteins have been referred to as uptake sites or neurotransmitter transporters. Once taken up by the plasma membrane transporters, neurotransmitters are repackaged into secretory vesicles by distinct transporters which depend on a proton gradient.

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The Unique Mechanism of SNX9 BAR Domain for Inducing Membrane Tubulation

  • Park, Joohyun;Zhao, Haiyan;Chang, Sunghoe
    • Molecules and Cells
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    • v.37 no.10
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    • pp.753-758
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    • 2014
  • Sorting nexin 9 (SNX9) is a member of the sorting nexin family of proteins and plays a critical role in clathrinmediated endocytosis. It has a Bin-Amphiphysin-Rvs (BAR) domain which can form a crescent-shaped homodimer structure that induces deformation of the plasma membrane. While other BAR-domain containing proteins such as amphiphysin and endophilin have an amphiphatic helix in front of the BAR domain which plays a critical role in membrane penetration, SNX9 does not. Thus, whether and how SNX9 BAR domain could induce the deformation of the plasma membrane is not clear. The present study identified the internal putative amphiphatic stretch in the $1^{st}$ ${\alpha}$-helix of the SNX9 BAR domain and proved that together with the N-terminal helix ($H_0$) region, this internal putative amphiphatic stretch is critical for inducing membrane tubulation. Therefore, our study shows that SNX9 uses a unique mechanism to induce the tubulation of the plasma membrane which mediates proper membrane deformation during clathrinmediated endocytosis.

Effects of Polycyclic Aromatic Hydrocarbons on DNA Damage and Plasma Protein Expression in Mouse

  • Oh, Sang-Nam;Oh, Eun-Ha;Im, Ho-Sub;Jo, Gyu-Chan;Sul, Dong-Geun;Kim, Young-Whan;Lee, Eun-Il
    • Molecular & Cellular Toxicology
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    • v.1 no.1
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    • pp.32-39
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    • 2005
  • Polycyclic aromatic hydrocarbons (PAHs) are an important class of environmentally prevalent xenobiotics that exert complex effects on the biological system and characterized as probably carcinogenic materials. Single cell gel electrophoresis assays were performed in order to evaluate DNA damage occurring in the T-and B lymphocytes, spleens (T/B-cell), bone marrow, and livers of mouse exposed to mixture of PAHs (Benzo(a)pyrene, Benzo(e)pyrene, Fluoranthene, Pyrene) at dose of 400, 800, or 1600 mg/kg body weight for 2 days. DNA damage of the cells purified from mice was increased in dose dependent manner. In the blood cells and organs, DNA damage was also discovered to vary directly with PAHs. Especially T-cells had been damaged more than B-cell. Plasma proteomes were separated by 2-dimensional electrophoresis with pH 4-7 ranges of IPG Dry strips and many proteins showed significant up-and -down expressions with the dose dependent manner. Of these, significant 4 spots were identified using matrix-assisted laser desorption/ionization-time of fight (MALDI-TOF) mass spectrometry. Identified proteins were related to energy metabolism and signal transduction.

Plasma Protein Adsorption to Anion Substituted Poly(vinyl alcohol) Membranes

  • Ryu, Kyu-Eun;Hyangshuk Rhim;Park, Chong-Won;Chun, Heung-Jae;Hong, Seung-Hwa;Kim, Jae-Jin;Lee, Young-Moo
    • Macromolecular Research
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    • v.11 no.6
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    • pp.451-457
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    • 2003
  • Anion-substituted poly(vinyl alcohol) (PVA) membranes, carboxymethylated PVA (C-PVA), and sulfonated PVA (S-PVA) were prepared and the effects of these substitutions on the plasma protein adsorption were studied by one- and two-dimensional gel electrophoresis and immunoblotting. When Cuprophane was used as a negative control, the amount of total proteins bound to samples decreased in the order Cuprophane > PVA > C-PVA > S-PVA, which we attribute to the effects of the surface characteristics of the samples, such as their surface tensions and electrostatic properties, on the adsorption of proteins to the surfaces of the materials. The results revealed that albumin was the most abundant protein in all the samples. The proportion of adsorbed fibrinogen to S-PVA exceeded those of PVA and C-PVA, whereas S-PVA exhibited the lowest IgG adsorption affinity among the samples we studied.

High fat diet confers vascular hyper-contractility against angiotensin II through upregulation of MLCK and CPI-17

  • Kim, Jee In
    • The Korean Journal of Physiology and Pharmacology
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    • v.21 no.1
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    • pp.99-106
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    • 2017
  • Obesity is a critical risk factor for the hypertension. Although angiotensin II (Ang II) in obese individuals is known to be upregulated in obesity-induced hypertension, direct evidence that explains the underlying mechanism for increased vascular tone and consequent increase in blood pressure (BP) is largely unknown. The purpose of this study is to investigate the novel mechanism underlying Ang II-induced hyper-contractility and hypertension in obese rats. Eight-week old male Sprague-Dawley rats were fed with 60% fat diet or normal diet for 4 months. Body weight, plasma lipid profile, plasma Ang II level, BP, Ang II-induced vascular contraction, and expression of regulatory proteins modulating vascular contraction with/without Ang II stimulation were measured. As a result, high fat diet (HFD) accelerated age-dependent body weight gaining along with increased plasma Ang II concentration. It also increased BP and Ang II-induced aortic contraction. Basal expression of p-CPI-17 and myosin light chain (MLC) kinase was increased by HFD along with increased phosphorylation of MLC. Ang II-induced phosphorylation of CPI-17 and MLC were also higher in HFD group than control group. In conclusion HFD-induced hypertension is through at least in part by increased vascular contractility via increased expression and activation of contractile proteins and subsequent MLC phosphorylation induced by increased Ang II.