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Journal articles on the topic 'Rat plasma'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

Ramaswamy, Manisha, Thomas L. Wallace, Paul A. Cossum, and Kishor M. Wasan. "Species Differences in the Proportion of Plasma Lipoprotein Lipid Carried by High-Density Lipoproteins Influence the Distribution of Free and Liposomal Nystatin in Human, Dog, and Rat Plasma." Antimicrobial Agents and Chemotherapy 43, no. 6 (1999): 1424–28. http://dx.doi.org/10.1128/aac.43.6.1424.

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ABSTRACT The objective of this study was an interspecies comparison of free nystatin (NYS) and liposomal NYS (Nyotran) distribution in plasma. NYS and liposomal NYS at concentrations of 5, 10, and 20 μg of NYS/ml were incubated in human, dog, and rat plasma for 5, 60, and 180 min at 37°C. Following these incubations, plasma samples were separated into their high-density lipoprotein (HDL), triglyceride-rich lipoprotein, low-density lipoprotein, and lipoprotein-deficient plasma (LPDP) fractions by density-gradient ultracentrifugation, and each fraction was assayed for NYS by high-pressure liquid

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Ono, Mayumi, Hiroyuki Fujiwara, Takaaki Okafuji, Tomoko Enjoh, and Katsuhiko Nawa. "Recombinant Rat Protein C: Comparative Studies of Structure, Function and Synthesis with Plasma Protein C." Thrombosis and Haemostasis 71, no. 01 (1994): 054–61. http://dx.doi.org/10.1055/s-0038-1642384.

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SummaryIn order to elucidate the role of protein C (PC) in the rat, we expressed, purified, and characterized recombinant rat PC. The purified recombinant rat PC was 70–90% two-chain (41 kDa heavy chain; 22 and 23 kDa light chain) and 10–30% single-chain (61 kDa). Amino acid analysis confirmed the presence of 10 moles of γ-carboxyglutamic acid residues per mol of protein. For comparison, plasma rat PC was purified from a barium citrate precipitate using similar method. Plasma rat PC was a two-chain form (41 kDa heavy chain; 22 kDa light chain) with no detectable single-chain nor 23 kDa light c

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Kim, Shokei, Masayuki Hosoi, Kiichiro Nakajima, and Kenjiro Yamamoto. "Biochemical and immunological differences between plasma inactive renin from normal and nephrectomized rats." Canadian Journal of Physiology and Pharmacology 69, no. 9 (1991): 1350–54. http://dx.doi.org/10.1139/y91-199.

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Using immunological techniques, we have demonstrated that about half the trypsin-activatable renin in normal rat plasma is prorenin, while the other is not, and that inactive renin in nephrectomized rat plasma is not prorenin. In the present study, the trypsin-induced angiotensin I generating activity not related to prorenin from normal rat plasma disappeared after HPLC on G3000SW. HPLC analysis of trypsin-treated plasma showed the generation of active renin by trypsin for normal rat plasma, while it did not for nephrectomized rat plasma. These results indicate that trypsin treatment of crude

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Ioannou, P., A. Y. Loh, and D. H. Osmond. "Activation and measurement of plasma prorenin in the rat." Canadian Journal of Physiology and Pharmacology 69, no. 9 (1991): 1331–40. http://dx.doi.org/10.1139/y91-197.

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Prorenin determination in rat plasma has been problematic from the outset. Consequently, its existence is questioned by some and its quantity by others, making it difficult for knowledge to advance as to its function relative to the renin system. The present study examines major variables in the determination of rat plasma prorenin and renin, notably different prorenin activation protocols involving blood samples obtained under various conditions from animals under different anesthetics. We found that a trypsin activation step with 5 mg/mL plasma, 60 min at 23 °C, followed by a PRA step of 10

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Vohra, Prerna, and Kuldeep Singh Khera. "Effect of imidacloprid on plasma and tissue biochemistry of albino rat." Indian Journal of Applied Research 3, no. 12 (2011): 554–56. http://dx.doi.org/10.15373/2249555x/dec2013/169.

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6

Yurt, R. W., and B. A. Pruitt. "Base-line and postthermal injury plasma histamine in rats." Journal of Applied Physiology 60, no. 5 (1986): 1782–88. http://dx.doi.org/10.1152/jappl.1986.60.5.1782.

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Although plasma histamine concentration has been reported to increase after thermal injury in the rat to as much as 100-fold over normal human plasma levels, the pathophysiological significance and relevance to human disease is questionable. Lack of confidence in the rat as a model of histamine-mediated disease is based on reports that normal rat base-line plasma histamine concentration exceeds that of human plasma by 20- to 70-fold. The present study confirms that high concentrations of histamine (20–68.9 ng/ml) are found in rat plasma obtained in an uncontrolled manner; but concentrations ar

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Barrett, Jack D., and Peter Eggena. "Trypsin activation of inactive renin: plasma blanks and angiotensin I radioimmunoassay." Canadian Journal of Physiology and Pharmacology 69, no. 9 (1991): 1315–20. http://dx.doi.org/10.1139/y91-194.

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Divergent conclusions exist as to whether inactive renin is present in nephrectomized rat plasma. A major factor contributing to this conflict may be related to significant changes in the "plasma blank" when trypsin-treated plasma is subjected to angiotensin I (AI) radioimmunoassay (RIA). In normal, but not nephrectomized rat plasma, AI-like substances are present in direct proportion to active renin. These substances are destroyed by trypsin. However, trypsin generates additional AI-like material, in both normal and nephrectomized rat plasma. This material, which is present in proportion to t

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8

Wasan, Kishor M., Manisha Ramaswamy, Samson P. Ng, et al. "Differences in the Lipoprotein Distribution of Free and Liposome-Associated All-trans-Retinoic Acid in Human, Dog, and Rat Plasma Are Due to Variations in Lipoprotein Lipid and Protein Content." Antimicrobial Agents and Chemotherapy 42, no. 7 (1998): 1646–53. http://dx.doi.org/10.1128/aac.42.7.1646.

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ABSTRACT The objective of the proposed study was to determine the distribution in plasma lipoprotein of free all-transretinoic acid (ATRA) and liposomal ATRA (Atragen; composed of dimyristoyl phosphatidylcholine and soybean oil) following incubation in human, rat, and dog plasma. When ATRA and Atragen at concentrations of 1, 5, 10, and 25 μg/ml were incubated in human and rat plasma for 5, 60, and 180 min, the majority of the tretinoin was recovered in the lipoprotein-deficient plasma fraction. However, when ATRA and Atragen were incubated in dog plasma, the majority of the tretinoin (>40%)

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9

Weissgerber, Tracey L., Andrea McConico, Bruce E. Knudsen, et al. "Methodological differences account for inconsistencies in reported free VEGF concentrations in pregnant rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 306, no. 11 (2014): R796—R803. http://dx.doi.org/10.1152/ajpregu.00544.2013.

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Free vascular endothelial growth factor (VEGF) is undetectable in plasma during human pregnancy. However, studies examining pregnant rats have reported both low (8–29 pg/ml) and high (527–1,030 pg/ml) free VEGF. These discrepancies cast uncertainty over the use of rat models to study angiogenic factors in pregnancy and preeclampsia. This study investigates methodological factors that may explain these discrepancies. Plasma VEGF in nonpregnant, day 7 pregnant, and day 19 pregnant rats was measured using rat and mouse ELISAs (R&D Systems). The rat ELISA detected VEGF in plasma from nonpregna

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Aletti, Federico, Elisa Maffioli, Armando Negri, et al. "Peptidomic Analysis of Rat Plasma." SHOCK 45, no. 5 (2016): 540–54. http://dx.doi.org/10.1097/shk.0000000000000532.

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11

Beguin, Y., H. A. Huebers, B. Josephson, and C. A. Finch. "Transferrin receptors in rat plasma." Proceedings of the National Academy of Sciences 85, no. 2 (1988): 637–40. http://dx.doi.org/10.1073/pnas.85.2.637.

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Shisheva, Assia C., Ognian C. Ikonomov, and Luben M. Sirakov. "Comments on spectrofluorometric assay of angiotensin-converting enzyme activity in blood plasma of different species." Collection of Czechoslovak Chemical Communications 51, no. 10 (1986): 2280–84. http://dx.doi.org/10.1135/cccc19862280.

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The activity of the angiotension -converting enzyme (ACE) in human, dog, rabbit, and rat blood plasma was assayed by spectrofluorometric determination of the product liberated by enzymatic cleavage (L-His-L-Leu). In parallel experiments the hydrolysis of L-His-L-Leu by blood plasma was examined. The hydrolytic activity of rat blood plasma was high and therefore lower values of ACE activity were obtained; the use of the spectrofluorometric assay with rat blood plasma is therefore problematic. By contrast, L-His-L-Leu was not degraded by human, dog, and rabbit blood plasma and the spectrofluorom

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Ngo, Thu-Hoa, S. Verheyen, I. Knockaert, and P. J. Declerck. "Monoclonal Antibody-based Immunoassays for the Specific Quantitation of Rat PAI-1 Antigen and Activity in Biological Samples." Thrombosis and Haemostasis 79, no. 04 (1998): 808–12. http://dx.doi.org/10.1055/s-0037-1615069.

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SummaryTwo enzyme-linked immunosorbent assays (ELISAs) for the quantitation of rat plasminogen activator inhibitor-1 (PAI-1) antigen and activity, respectively, in biological fluids were developed using monoclonal antibodies raised against recombinant rat PAI-1. These assays had a lower limit of sensitivity in plasma of 0.3 and 0.15 ng/ml, respectively. The intra-assay, inter-assay and inter-dilution coefficients of variation were 9, 14 and 9%, respectively, for the antigen assay and 8, 17 and 13%, respectively for the activity assay. Assay recoveries of recombinant rat PAI-1 (5 to 20 ng/ml) a

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14

Poulsen, Knud, Arne Høj Nielsen, and Arne Johannessen. "Measurement of inactive renin in normal, nephrectomized, and adrenalectomized rats." Canadian Journal of Physiology and Pharmacology 69, no. 9 (1991): 1381–84. http://dx.doi.org/10.1139/y91-205.

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In a new method for measurement of inactive rat plasma renin, the trypsin generated angiotensin I immunoreactive material, which was HPLC characterized as similar to tetradecapeptide renin substrate, is removed by a cation exchange resin before the renin incubation step. The method also corrects for trypsin destruction of endogenous angiotensinogen by the addition of exogenous angiotensinogen. When measured with this method inactive renin in rat plasma decreased after nephrectomy and increased after adrenalectomy. This is in accordance with findings in humans. A sexual dimorphism of prorenin (

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Calvo, M. S., C. M. Gundberg, H. Heath, and J. Fox. "Homologous amino-terminal radioimmunoassay for rat parathyroid hormone." American Journal of Physiology-Endocrinology and Metabolism 261, no. 2 (1991): E262—E268. http://dx.doi.org/10.1152/ajpendo.1991.261.2.e262.

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Existing radioimmunoassays for parathyroid hormone (PTH) in rat plasma are based on cross-reactivity of rat PTH (rPTH) with heterologous antisera. We used the synthetic NH2-terminal fragment of rPTH [rPTH-(1-34)] to develop a homologous radioimmunoassay for circulating PTH. An antiserum to rPTH-(1-34) was raised in a goat (G-813), and the same peptide was used as radioligand (125I) and standard. Purification of the label by high-performance liquid chromatography (HPLC) increased specific binding greater than twofold and sensitivity by 50-100%. With a final antiserum dilution of 1:70,000, maxim

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Shen, Xin-Yi, and Aubie Angel. "Identification of high density lipoprotein binding proteins in mature adipocyte plasma membranes." Biochemistry and Cell Biology 71, no. 7-8 (1993): 348–54. http://dx.doi.org/10.1139/o93-052.

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High density lipoprotein (HDL) binding proteins were identified in nonreduced detergent extracts of plasma membranes or crude membrane fractions of rat adipocytes by ligand blotting. Using 125I-labelled human apolipoprotein-E-free HDL ([125I]HDL3), two binding proteins in adipocyte membranes were detected with apparent molecular masses of 122 and 88 kilodaltons (kDa), respectively. The binding of HDL3 to both binding proteins was abolished by pronase treatment and was inhibited by excess unlabelled HDL3. Excessive unlabelled low density lipoprotein reduced the binding of [125I]HDL3 to the 122-

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Waller, Amanda, Katelyn Wolfgang, Zachary Stevenson, and Bryce Kerlin. "Hypoalbuminemia Increases Clot Fibrin Network Density and Reduces Fibrinolytic Susceptibility through a Paraoxonase 1 Dependent Mechanism." Blood 144, Supplement 1 (2024): 3963. https://doi.org/10.1182/blood-2024-211888.

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Introduction Hypoalbuminemia is a predictor for thrombotic cardiovascular disease. Albumin is a negative acute phase reactant and may thus be a biomarker for thrombo-inflammation, but some data suggest a mechanistic role for albumin in fibrinolysis. The aim of this study was to investigate the mechanistic role of albumin in fibrinolysis. We hypothesized that albumin modifies clot structure and fibrinolytic susceptibility in two well-established rodent models of hypoalbuminemia and analbuminemia. Methods Blood or plasma from a hypoalbuminemic nephrotic syndrome rat model and an albumin knockout

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18

Millett, J. A., S. M. Holland, J. Alaghband-Zadeh, and H. E. de Wardener. "Na-K-ATPase-inhibiting and glucose-6-phosphate dehydrogenase-stimulating activity of plasma and hypothalamus of the Okamoto spontaneously hypertensive rat." Journal of Endocrinology 108, no. 1 (1986): 69–73. http://dx.doi.org/10.1677/joe.0.1080069.

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ABSTRACT The plasma of normal man and the rat, and an acetone extract of hypothalamus from the rat, have an ability to inhibit Na-K-ATPase which is related directly to salt intake. The ability of the plasma to inhibit Na-K-ATPase is raised in essential hypertension. The ability of plasma and of an acetone extract of hypothalamus from six spontaneously hypertensive (SHR) rats and six normotensive control (WKY) rats to inhibit Na-K-ATPase of fresh guinea-pig kidney was studied using cytochemical bioassay techniques. With a validated assay, which measures the capacity of biological samples to sti

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NANJUNDAN, Meera, and Fred POSSMAYER. "Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling platforms." Biochemical Journal 358, no. 3 (2001): 637–46. http://dx.doi.org/10.1042/bj3580637.

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Lipid phosphate phosphohydrolase (LPP) has recently been proposed to have roles in signal transduction, acting sequentially to phospholipase D (PLD) and in attenuating the effects of phospholipid growth factors on cellular proliferation. In this study, LPP activity is reported to be enriched in lipid-rich signalling platforms isolated from rat lung tissue, isolated rat type II cells and type II cell-mouse lung epithelial cell lines (MLE12 and MLE15). Lung and cell line caveolin-enriched domains (CEDs), prepared on the basis of their detergent-insolubility in Triton X-100, contain caveolin-1 an

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Landt, Michael, Ronald L. Gingerich, Peter J. Havel, et al. "Radioimmunoassay of rat leptin: sexual dimorphism reversed from humans." Clinical Chemistry 44, no. 3 (1998): 565–70. http://dx.doi.org/10.1093/clinchem/44.3.565.

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Abstract Adipose tissue secretes leptin, which interacts with receptors in the hypothalamus. In rodent models of obesity, leptin increases metabolism and decreases food intake, which helps to maintain normal body composition. Accurate and precise methods to quantitate circulating leptin concentrations are needed for physiological studies. We developed an RIA to measure leptin in rat plasma, serum, or adipocyte culture fluids. The working range of the assay, defined by the detection limit and the highest calibrator, was 0.5–50 μg/L. Recovery of 1.6–11.6 μg/L leptin added to serum was 92–103%. T

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Romans, Barua, and Olson. "Pharmacokinetics of All-trans Retinoyl beta-Glucuronide in Rats following Intraperitoneal and Oral Administration." International Journal for Vitamin and Nutrition Research 73, no. 4 (2003): 251–57. http://dx.doi.org/10.1024/0300-9831.73.4.251.

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The purpose of this study was to examine the pharmacokinetics of a single dose (6.3 mumol, 3 mg) of all-trans retinoyl beta-glucuronide (RAG), when given either orally in corn oil or by intraperitoneal (IP) injection in dimethylsulfoxide (DMSO) to adult Sprague-Dawley rats. Following dosing, serial blood samples were collected at various times up to 48 hours from each rat via saphenous vein puncture. Retinoids were extracted from plasma samples and analyzed by high-performance liquid chromatography. In the plasma of IP-dosed rats (n = 6), a derivative of RAG, tentatively identified as the lact

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Ballermann, B. J. "A highly sensitive radioreceptor assay for atrial natriuretic peptide in rat plasma." American Journal of Physiology-Renal Physiology 254, no. 1 (1988): F159—F163. http://dx.doi.org/10.1152/ajprenal.1988.254.1.f159.

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To enable serial measurements of plasma atrial natriuretic peptide (ANP) concentrations in the rat, a microradioreceptor assay (RRA) for this hormone was developed. Glomerular microsomes bearing ANP receptors were used to bind ANP. The smallest quantity of ANP detectable by this method was 0.2 fmol/sample. By contrast, a radioimmunoassay for ANP was sensitive to 2.4 fmol/sample. The intra- and interassay coefficients of variation for the RRA were 4.1 and 11.6%, respectively. Recovery of 10, 20, 50, and 100 pM synthetic ANP added to unextracted rat plasma was essentially 100%. Biologically inac

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Saxena, U., J. Francis-Collins, J. Hall, et al. "Removal of apoprotein-B-containing lipoproteins by plasmapheresis using immobilized phosphorylcholine-binding protein affinity adsorbent." Biochemistry and Cell Biology 68, no. 1 (1990): 255–59. http://dx.doi.org/10.1139/o90-035.

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Rat serum phosphorylcholine binding protein was earlier shown to bind lipoproteins containing apoproteins B and E from human very low and low density lipoproteins. The present studies were undertaken to show the effectiveness of rat serum phosphorylcholine-binding protein immobilized on Sepharose affinity column to remove apoprotein-B-containing lipoproteins from normal and hypercholesterolemic rabbit plasma, when used in a plasmapheresis system. The maximum in vitro binding of very low and low density lipoproteins from hypercholesterolemic rabbit plasma to the affinity adsorbent was Ca2+ depe

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Hazri, M. "Analisis Malware PlasmaRAT dengan Metode Reverse Engineering." Jurnal Rekayasa Teknologi Informasi (JURTI) 4, no. 2 (2020): 192. http://dx.doi.org/10.30872/jurti.v4i2.4131.

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Software untuk me-remote sistem dari jarak jauh sangat memudahkan pengguna khususnya untuk perusahaan besar. Akan tetapi tidak sedikit dari software tersebut menyisipkan malware didalam program yang mereka buat yang kemudian dimanfaatkan untuk kepentingan pribadi maupun kelompok. Penting untuk melakukan analisis terhadap program remote sistem tersebut untuk mengetahui hal tidak normal apa yang dilakukan pada sistem ketika program tersebut berjalan. Dengan metode analisis dan tool yang bisa mengekstrak program tersebut. salah satu metode yang bisa digunakan adalah reverse engineering. Sebuah te

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Hazri, M. "Analisis Malware PlasmaRAT dengan Metode Reverse Engineering." Jurnal Rekayasa Teknologi Informasi (JURTI) 4, no. 2 (2020): 192. http://dx.doi.org/10.30872/jurti.v4i2.4131.

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Software untuk me-remote sistem dari jarak jauh sangat memudahkan pengguna khususnya untuk perusahaan besar. Akan tetapi tidak sedikit dari software tersebut menyisipkan malware didalam program yang mereka buat yang kemudian dimanfaatkan untuk kepentingan pribadi maupun kelompok. Penting untuk melakukan analisis terhadap program remote sistem tersebut untuk mengetahui hal tidak normal apa yang dilakukan pada sistem ketika program tersebut berjalan. Dengan metode analisis dan tool yang bisa mengekstrak program tersebut. salah satu metode yang bisa digunakan adalah reverse engineering. Sebuah te

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Bradley, Nicolette S., Laelie A. Snook, Swati S. Jain, George J. F. Heigenhauser, Arend Bonen, and Lawrence L. Spriet. "Acute endurance exercise increases plasma membrane fatty acid transport proteins in rat and human skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 302, no. 2 (2012): E183—E189. http://dx.doi.org/10.1152/ajpendo.00254.2011.

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Fatty acid transport proteins are present on the plasma membrane and are involved in the uptake of long-chain fatty acids into skeletal muscle. The present study determined whether acute endurance exercise increased the plasma membrane content of fatty acid transport proteins in rat and human skeletal muscle and whether the increase was accompanied by an increase in long-chain fatty acid transport in rat skeletal muscle. Sixteen subjects cycled for 120 min at ∼60 ± 2% V̇o2 peak. Two skeletal muscle biopsies were taken at rest and again following cycling. In a parallel study, eight Sprague-Dawl

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Lowe, N. M., I. Bremner, and M. J. Jackson. "Plasma 65Zn Kinetics in the rat." British Journal of Nutrition 65, no. 3 (1991): 445–55. http://dx.doi.org/10.1079/bjn19910103.

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The amount of 65Zn in the plasma of rats after intravenous injection was found to decline following closely two-compartment kinetics over a period of 90 min. Comparative analysis of the amount of 65Zn present in the two kinetic pools at various time-intervals post-injection with the actual physiological location of the 65Zn, revealed that the initial pool (Qa) is primarily the blood plasma, while the second pool (Qb) is primarily within the liver. The plasma Zn concentration and Qa were both found to fall reproducibly during Zn depletion, whereas Qa and Qb increased following injection of Esch

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TAMAI, Toshitaka, Tsuguhiko NAKAI, Susumu MIYABO, Wolfgang PATSCH, and Gustav SCHONFELD. "Rat Plasma Lipoprotein Catabolism in a Rat Hepatoma Cell Line." Journal of Japan Atherosclerosis Society 13, no. 3 (1985): 707–12. http://dx.doi.org/10.5551/jat1973.13.3_707.

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ICHIKAWA, TSUTOMU, SHIRO ISHIDA, YOKO SAKIYA, and YASUFUMI SAWADA. "Binding of glycyrrhizin to rat plasma and rat serum albumin." CHEMICAL & PHARMACEUTICAL BULLETIN 33, no. 7 (1985): 3031–33. http://dx.doi.org/10.1248/cpb.33.3031.

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Galan, Xavier, Julia Peinado-Onsurbe, Josep Julve, et al. "Inactive hepatic lipase in rat plasma." Journal of Lipid Research 44, no. 12 (2003): 2250–56. http://dx.doi.org/10.1194/jlr.m300131-jlr200.

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Arntzen, Finn Cato, Kjell Briseid, and Ellen-Karine Qvigstad. "Determination of Prekininogenase in Rat Plasma." Acta Pharmacologica et Toxicologica 36, no. 2 (2009): 145–54. http://dx.doi.org/10.1111/j.1600-0773.1975.tb00780.x.

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Yellon, D. M., C. Boi-Doku, S. Subrayan, et al. "238 RAT PLASMA EXOSOMES ARE CARDIOPROTECTIVE." Heart 99, suppl 2 (2013): A127.2—A127. http://dx.doi.org/10.1136/heartjnl-2013-304019.238.

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Yang, LIN, XIAO-YU Guo, LI-YI Pan, et al. "Metabolites of scutellarein in rat plasma." Journal of Asian Natural Products Research 10, no. 1 (2008): 59–64. http://dx.doi.org/10.1080/10286020701275804.

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Feng, Qianru, Shunjun Xu, Jiejing Yu, Shuai Sun, and Liu Yang. "Determination of Epimedin B in Rat Plasma and Tissue by LC-MS/MS: Application in Pharmacokinetic and Tissue Distribution Studies." Journal of Analytical Methods in Chemistry 2017 (2017): 1–9. http://dx.doi.org/10.1155/2017/7194075.

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A simple, sensitive, and specific liquid chromatography tandem mass-spectrometric method was developed and validated for the determination of epimedin B in rat plasma and tissue samples. After being processed with a protein precipitation method, these samples were separated on an Agilent Eclipse XDB-C18 column with an isocratic mobile phase consisting of acetonitrile and 0.1% formic acid aqueous solution (32 : 68, v/v). The calibration curve of epimedin B was linear over the concentration range from 1 to 500 ng/mL in plasma and tissue homogenate. The method was then applied to pharmacokinetic

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Agarwal, Kailash C., Beth A. Zielinski, and Ranjan S. Maitra. "Significance of Plasma Adenosine in the Antiplatelet Activity of Forskolin: Potentiation by Dipyridamole and Dilazep." Thrombosis and Haemostasis 61, no. 01 (1989): 106–10. http://dx.doi.org/10.1055/s-0038-1646536.

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SummaryForskolin, a plant (Coleus forskohlii) diterpene, inhibits ADP- induced (human: IC50, 2.3±1.0 μ;M; rat: IC50, 1.2±0.5 μM) and collagen-induced (human: IC50, 2.4±1.2 μM; rat: 0.6±0.2 μM) platelet aggregation in human and rat platelet-rich plasma (PRP). Human blood levels of adenosine (Ado) are low (100-300 nM) as compared to levels in rat plasma (7.55 ± 0.51 μM). Ado is a natural antiplatelet and vasodilatory agent produced by vascular endothelium, heart and other body tissues. If the plasma Ado is degraded by pretreatment of PRP with adenosine deaminase (ADA), forskolin inhibition on pl

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Thapa, Subindra Kazi, Mahesh Upadhyay, Tae Hwan Kim, Soyoung Shin, Sung-Joo Park, and Beom Soo Shin. "Liquid Chromatography-Tandem Mass Spectrometry of Desoxo-Narchinol a and Its Pharmacokinetics and Oral Bioavailability in Rats and Mice." Molecules 24, no. 11 (2019): 2037. http://dx.doi.org/10.3390/molecules24112037.

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Desoxo-narchinol A is one of the major active constituents from Nardostachys jatamansi, which has been reported to possess various pharmacological activities, including anti-inflammatory, antioxidant, and anticonvulsant activity. A simple and sensitive liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was developed and validated for the quantification of desoxo-narchinol A in two different biological matrices, i.e., rat plasma and mouse plasma, using sildenafil as an internal standard (IS). The method involved simple protein precipitation with acetonitrile and the analyte was se

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Lord, A. P. D., S. E. P. Bastian, L. C. Read, P. E. Walton, and F. J. Ballard. "Differences in the association of insulin-like growth factor-I (IGF-I) and IGF-I variants with rat, sheep, pig, human and chicken plasma-binding proteins." Journal of Endocrinology 140, no. 3 (1994): 475–82. http://dx.doi.org/10.1677/joe.0.1400475.

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Abstract Associations between labelled insulin-like growth factors (IGFs) and IGF-binding proteins in plasma have been compared in the rat, sheep, human, pig and chicken. The IGFs tested were recombinant human IGF-I, the truncated variant, des(1–3)IGF-I, and LR3IGF-I, an extended form that had been engineered so as to minimize interactions with IGF-binding proteins. Marked species differences were demonstrated, notably that the IGF-I variants which exhibited extremely weak binding in rat plasma bound significantly in plasma from the other species. This result was shown both by size-exclusion c

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Pappas, G. D., and V. Kriho. "Nerve terminal plasma membrane localization of Ca++-Mg++ ATPase." Proceedings, annual meeting, Electron Microscopy Society of America 45 (August 1987): 772–73. http://dx.doi.org/10.1017/s0424820100128171.

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Depolarization of the frog neuromuscular junction results In an Influx of calcium from the extracellular space. The cell calcium concentration is increased several fold and release of neurotransmitter results. Following depolarization, a necessity exists for an outwardly directed calcium pump to return the intracellular Ca++ concentration to resting levels. A calcium pump such as this has been described In the erthrocyte plasma membrane as well as In synaptosomal plasma membrane from guinea pig, synaptic membrane fractions from rat cerebral cortex and the plasma membrane of mouse neuroblastoma

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MAUNSBACH, ARVID B., HENRIK VORUM, TAE-HWAN KWON, et al. "Immunoelectron Microscopic Localization of the Electrogenic Na/HCO3 Cotransporter in Rat and Ambystoma Kidney." Journal of the American Society of Nephrology 11, no. 12 (2000): 2179–89. http://dx.doi.org/10.1681/asn.v11122179.

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Abstract. Immunofluorescence analysis has revealed that electrogenic Na+/HCO3- (NBC1) is expressed in the proximal tubule of rat kidney and in the proximal and distal tubules of the salamander Ambystoma tigrinum kidney. The present study was undertaken to define the detailed subcellular localization of the NBC1 in rat and Ambystoma kidney using high-resolution immunoelectron microscopy. For this purpose, two rabbit polyclonal antibodies raised against amino acids 928 to 1035 and amino acids 1021 to 1035 of the C-terminus of rat kidney (rkNBC1) were developed. The affinity-purified antibodies r

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Regoeczi, Erwin, Paul A. Chindemi, John R. Rudolph, Geneviève Spik, and Jean Montreuil. "The chromatographic heterogeneity of rat transferrin on immobilized concanavalin A and lentil lectin." Biochemistry and Cell Biology 65, no. 11 (1987): 948–54. http://dx.doi.org/10.1139/o87-123.

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A procedure was developed for the isolation of the microheterogeneous forms of rat transferrin consisting of anion-exchange and serial lectin affinity chromatographies. By deploying this technique, four to five different anionic species of the protein were detected in plasma. The two major components obtained, which encompassed 92–94% of the plasma transferrin, were further studied by sequential lectin chromatography. The larger of the two, representing 60–63% of plasma transferrin, was bound by concanavalin A – Sepharose, while the smaller one (30–32% of plasma transferrin) resolved into an u

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Nieuwenhuys, Cécile M., Marion A. Feijge, Suzette Béguin, and Johan W. Heemskerk. "Monitoring Hypocoagulant Conditions in Rat Plasma: Factors Determining the Endogenous Thrombin Potential of Tissue Factor-Activated Plasma." Thrombosis and Haemostasis 84, no. 12 (2000): 1045–51. http://dx.doi.org/10.1055/s-0037-1614169.

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SummaryAutomated human plasma, continuous monitoring of the formation and inactivation of thrombin during the coagulation process provides an adequate way to detect hypo- and hypercoagulant conditions. Here, we describe an analogous procedure to determine the endogenous thrombin potential (ETP), i. e. the free thrombin concentration-time integral, of coagulating rat plasma. When activated with tissue factor, the ETP of plasma from Wistar rats was comparable to the ETP of human plasma, in spite of a relatively short half-life time of free thrombin in rat plasma. The ETP was highly sensitive to

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Wada, L., R. Daly, D. Kern, and B. Halloran. "Kinetics of 1,25-dihydroxyvitamin D metabolism in the aging rat." American Journal of Physiology-Endocrinology and Metabolism 262, no. 6 (1992): E906—E910. http://dx.doi.org/10.1152/ajpendo.1992.262.6.e906.

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To determine whether postmaturational aging influences the kinetics of 1,25-dihydroxyvitamin D [1,25(OH)2D] metabolism in the rat, we measured the metabolic clearance (MCR) and production (PR) rates of 1,25(OH)2D in 6-, 12-, 18-, and 24-mo-old Fischer 344 rats using the constant infusion method. Plasma calcium, phosphorus, and parathyroid hormone (PTH), urinary calcium and phosphorus, and glomerular filtration rate (GFR) were also measured. MCR and PR increased 57 and 91%, respectively (when expressed per rat), and 32 and 39%, respectively (when expressed per kg body wt), between 6 and 24 mo o

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Blakely, P., D. A. Vaughn, and D. D. Fanestil. "Amylin, calcitonin gene-related peptide, and adrenomedullin: effects on thiazide receptor and calcium." American Journal of Physiology-Renal Physiology 272, no. 3 (1997): F410—F415. http://dx.doi.org/10.1152/ajprenal.1997.272.3.f410.

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We previously reported that salmon calcitonin, but not rat calcitonin, increased renal thiazide receptor (TZR) density and decreased renal calcium [urinary calcium excretion (U(Caex))] in the rat. Since calcitonins, islet amyloid polypeptide (amylin), calcitonin-gene related peptide (CGRP), and adrenomedullin interact with a family of calcitonin-related receptors, we examined the effects of these peptides on 1) TZR density, as quantitated by binding of [3H]metolazone to renal membranes; 2) plasma ionic composition; and 3) urinary electrolyte excretion. Subcutaneous amylin both increased TZR de

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Bang, Angela S., Steven G. Soule, Tim G. Yandle, A. Mark Richards, and Chris J. Pemberton. "Characterisation of proghrelin peptides in mammalian tissue and plasma." Journal of Endocrinology 192, no. 2 (2007): 313–23. http://dx.doi.org/10.1677/joe-06-0021.

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Ghrelin is a 28 amino acid stomach peptide, derived from proghrelin(1–94), that stimulates GH release, appetite and adipose deposition. Recently, a peptide derived from proghrelin(53–75) – also known as obestatin – has been reported to be a physiological antagonist of ghrelin in the rat. Using four specific RIAs, we provide the first characterisation of proghrelin(1–94) peptides in human plasma, their modulation by metabolic manipulation and their distribution in mammalian tissues. ghrelin(1–28) immunoreactivity (IR) in human plasma and rat plasma/stomach consisted of major des-octanoyl and mi

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Radhakrishnan, Jeejabai, Rovi Origenes, Gina Littlejohn, et al. "Plasma Cytochrome c Detection Using a Highly Sensitive Electrochemiluminescence Enzyme-Linked Immunosorbent Assay." Biomarker Insights 12 (January 1, 2017): 117727191774697. http://dx.doi.org/10.1177/1177271917746972.

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Background: Cytochrome c is an intermembrane mitochondrial protein that is released to the bloodstream following mitochondrial injury. Methods and results: We developed an electrochemiluminescence immunoassay to measure cytochrome c in human and rat plasma, which showed high sensitivity with broad dynamic range (2-1200 ng/mL in humans and 5-500 ng/mL in rat) and high assay reproducibility (inter-assay coefficient <6% in humans and <10% in rat). In patients after blunt trauma, plasma cytochrome c directly correlated with injury severity. In rats after cardiac resuscitation, plasma cytochr

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Grases-Pintó, Blanca, Mar Abril-Gil, Paulina Torres-Castro, et al. "Rat Milk and Plasma Immunological Profile throughout Lactation." Nutrients 13, no. 4 (2021): 1257. http://dx.doi.org/10.3390/nu13041257.

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The composition of bioactive factors with immune activity in human breast milk is widely studied. However, the knowledge on rat milk immune factors during the whole lactation period is still scarce. This study aimed to analyze rat breast milk’s immunoglobulin (Ig) content and some critical adipokines and growth factors throughout the lactation period, and to assess relationships with corresponding plasma levels. During lactation, milk concentration of the transforming growth factor (TGF)-β2 and -β3 showed a punctual increase in the first week, whereas adiponectin and leptin remained stable. In

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Umezawa, Tsutomu, Yukiko Ohsawa, Yutaka Miura, Hisanori Kato, and Tadashi Noguchi. "Effect of protein deprivation on insulin-like growth factor-binding proteins in rats." British Journal of Nutrition 66, no. 1 (1991): 105–16. http://dx.doi.org/10.1079/bjn19910014.

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The effect of protein deprivation on plasma concentration of insulin-like growth factor-binding proteins (IGFBP) was studied in rats. A significant decrease in the concentration of IGFBP of molecular weight (mass) approximately 40 kDa was observed in protein-deprived rats. There was no prominent effect of protein deprivation on the concentration of IGFBP with molecular weights of about 30 kDa or 22–24 kDa. The binding capacity to plasma IGFBP of exogenously-added 125I-labelled insulin-like growth factor-1 (125I-IGF-1) was also studied. IGFBP of molecular weight about 30 and 22–24 kDa (the nati

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Gomez-Sanchez, Elise P., Naveed Ahmad, Damian G. Romero, and Celso E. Gomez-Sanchez. "Origin of Aldosterone in the Rat Heart." Endocrinology 145, no. 11 (2004): 4796–802. http://dx.doi.org/10.1210/en.2004-0295.

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Abstract Aldosterone has been demonstrated in the perfusate of the ex situ rat heart and heart homogenates; however, the origin of aldosterone in the heart is controversial, with some reporting a primary role for extraadrenal synthesis within the heart, and others finding that all of the aldosterone in the heart is sequestered from the circulation. In an attempt to resolve this controversy, we measured the aldosterone and corticosterone contents of plasma and hearts of rats on a normal salt (NS), low salt (LS), or high salt (HS) diet, adrenalectomized (ADX+HS), and ADX with aldosterone replace

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Dumke, C. L., J. Kim, E. B. Arias, and G. D. Cartee. "Role of kallikrein-kininogen system in insulin-stimulated glucose transport after muscle contractions." Journal of Applied Physiology 92, no. 2 (2002): 657–64. http://dx.doi.org/10.1152/japplphysiol.00854.2001.

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Serum proteins [molecular weight (MW) > 10,000] are essential for increased insulin-stimulated glucose transport after in vitro muscle contractions. We investigated the role of the kallikrein-kininogen system, including bradykinin, which is derived from kallikrein (MW > 10,000)-catalyzed degradation of serum protein kininogen (MW > 10,000), on this contraction effect. In vitro electrical stimulation of rat epitrochlearis muscles was performed in 1) rat serum ± kallikrein inhibitors; 2) human plasma (normal or kallikrein-deficient); 3) rat serum ± bradykinin receptor-2 inhibitors; or 4

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Burk, R. F., and K. E. Hill. "Reduced glutathione release into rat plasma by extrahepatic tissues." American Journal of Physiology-Gastrointestinal and Liver Physiology 269, no. 3 (1995): G396—G399. http://dx.doi.org/10.1152/ajpgi.1995.269.3.g396.

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The liver is the only tissue that has been demonstrated directly to secrete glutathione into the plasma. The present experiments were carried out to determine whether extrahepatic tissues secrete the reduced form of glutathione (GSH) as well. Phorone, a compound that depletes glutathione through glutathione S-transferase-dependent conjugation with GSH, was administered to fasted rats in a dose of 250 mg/kg. Two hours later, glutathione concentrations were reduced to the following: liver, 2%; plasma, 17%; and skeletal muscle, 63%. This showed that plasma and muscle glutathione were not depleted

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