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1.
Neuropsychologia ; 44(10): 1752-64, 2006.
Article in English | MEDLINE | ID: mdl-16650879

ABSTRACT

We used a computerized delayed-reaching task with a simple reaction time (RT) to investigate the visuo-motor and spatio-temporal performance of right brain-damaged (RBD) patients with unilateral spatial neglect (USN). Fifty-three RBD patients (22 with and 31 without USN) and 25 controls performed the tasks. We recorded the following data: the first RT (RT-1), which is thought to reflect the detection of the target position (the perceptual factor); the second RT (RT-2), which represents the initiation of reaching (the motor initiation aspect of premotor factors); the movement time (MT), which is hypothesized to reflect the "pure" motor component of the task. RBD patients with both USN and hemianopia demonstrated significantly longer RTs towards the left than towards the right for both the RT-1 and the RT-2. Among the RBD patients without hemianopia, the laterality index (left side/right side) of the RT-1 in those with USN was significantly greater than in those without USN or the controls. Among the three groups, there were no significant differences between the laterality indices of either the RT-2s or the MTs. These results suggest that the impairment of leftward movement in RBD patients with USN might be caused primarily by a perceptual impairment rather than an impairment in motor initiation, and is certainly not a "pure" motor impairment.


Subject(s)
Functional Laterality/physiology , Perceptual Disorders/physiopathology , Psychomotor Performance/physiology , Reaction Time/physiology , Space Perception/physiology , Adult , Aged , Brain Damage, Chronic/complications , Case-Control Studies , Female , Humans , Male , Middle Aged , Neuropsychological Tests/statistics & numerical data , Perceptual Disorders/etiology
2.
Masui ; 50(11): 1242-5, 2001 Nov.
Article in Japanese | MEDLINE | ID: mdl-11758335

ABSTRACT

A 29-year-old man with severe pyloric stenosis confessed that he had been a chronic amphetamine abuser just after awakening from anesthesia for partial gastrectomy. Anesthesia was maintained with thoracic epidural bupivacaine combined with continuous i.v. infusion of propofol. Decreased arterial blood pressure was observed 10 min after starting epidural anesthesia, and remained stable at 80-90 mmHg of systolic blood pressure in spite of massive fluid resuscitation in addition to repeated i.v. administration of ephedrine/methoxamine and continuous i.v. infusion of dopamine at a rate of 8 micrograms.kg-1.min-1. Finally, arterial blood pressure rose gradually after i.v. administration of methylpredonisolone 500 mg. We speculate that the down-regulation of beta-adrenoceptor induced by the sympathomimetic action of amphetamine, might be a major cause of refractory hypotension.


Subject(s)
Amphetamine/adverse effects , Receptors, Adrenergic, beta/drug effects , Substance-Related Disorders , Adult , Down-Regulation , Gastrectomy , Humans , Hypotension/drug therapy , Hypotension/etiology , Male , Methylprednisolone/therapeutic use , Receptors, Adrenergic, beta/metabolism
3.
Biosci Biotechnol Biochem ; 64(10): 2083-8, 2000 Oct.
Article in English | MEDLINE | ID: mdl-11129579

ABSTRACT

Natural rubber serum powder, which is a by-product obtained in the production of latex rubber, has a strong growth-stimulating activity for Bifidobacterium bifidum JCM 1254. The retained fraction obtained by ultrafiltration (molecular weight cutoff 1000) showed a growth-stimulating activity in a dose-dependent manner on B12 assay medium with ammonium sulfate. One of the growth stimulators was purified from the retained fraction by acetone precipitation, solid-phase extraction with a hydrophobic pretreatment column, and multistage reversed-phase HPLC. An increase of 53-fold in the specific activity, and a recovery of 1.3% were obtained. The amino acid composition and N-terminal sequence analysis of this growth stimulator provided the structure of Ala-Thr-Pro-Glu-Lys-Glu-Glu-Pro-Thr-Ala. The molecular mass was 1075 by MALDI-TOF MS analysis. These results showed that this growth stimulator was a decapeptide with the sequence shown above. This is the first report that clarified the structure of an active peptide for the growth of Bifidobacterium.


Subject(s)
Bifidobacterium/chemistry , Growth Substances/isolation & purification , Peptides/isolation & purification , Rubber/chemistry , Amino Acid Sequence , Chromatography, Gel , Growth Substances/chemistry , Peptides/chemistry , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
5.
Biosci Biotechnol Biochem ; 63(4): 627-31, 1999 Apr.
Article in English | MEDLINE | ID: mdl-10361675

ABSTRACT

Natural rubber serum powder, rich in crude protein and carbohydrates, had a strong growth-stimulating activity for Bifidobacterium bifidum JCM 1254, which was unable to grow in a fully synthetic medium, B12 assay medium. Natural rubber serum powder was fractionated by ultrafiltration (molecular weight cutoff 1000). The active ultrafiltrate was further concentrated and desalted with an adsorptive microconcentrator, which adsorbs virtually all amino acids and peptides. Through this purification step, it was found that the adsorbed fraction obtained did not stimulate growth independently but acted complementarily with a small amount of ammonium sulfate. The adsorbed fraction was subsequently analyzed on reversed-phase high pressure liquid chromatography, and the activities of the eluates were measured on B12 assay medium with ammonium sulfate. Consequently, it was proved that several peptidic ingredients in the adsorbed fraction increased the growth of B. bifidum.


Subject(s)
Ammonium Sulfate/pharmacology , Bifidobacterium/growth & development , Bifidobacterium/metabolism , Carbohydrates/pharmacology , Proteins/pharmacology , Bifidobacterium/drug effects , Chromatography, High Pressure Liquid , Culture Media , Molecular Weight , Powders , Rubber , Stimulation, Chemical , Ultrafiltration , Vitamin B 12/pharmacology
7.
Eisei Shikenjo Hokoku ; (114): 48-9, 1996.
Article in Japanese | MEDLINE | ID: mdl-9037865

ABSTRACT

Preliminary screening of antiviral AIDS drugs has been carried out using three different in vitro assay systems. Among 138 samples tested, two were found to inhibit the growth of HIV in vitro. Neither of the positive samples has hopeful signs, as the ranges of effective doses of the samples are very narrow.


Subject(s)
Anti-HIV Agents/pharmacology , HIV-1/drug effects , Drug Evaluation, Preclinical/methods , Drug Resistance, Microbial , Microbial Sensitivity Tests/methods
8.
Kidney Int ; 45(3): 794-802, 1994 Mar.
Article in English | MEDLINE | ID: mdl-8196281

ABSTRACT

We examined acute and chronic effects of thromboxane (TX) A2 inhibition on the renal hemodynamics at early and late stage of untreated streptozotocin (STZ)-induced diabetic rats. Two weeks and 28 weeks after the induction of diabetes, renal blood flow (RBF) under anesthesia was measured with an electromagnetic flowmeter before and after TXA2 inhibition. In two-week-old diabetic rats, a specific TXA2 synthetase inhibitor, OKY-046, or a specific TXA2 receptor antagonist, Sulotroban, increased renal vascular resistance (RVR) and ameliorated the hyperperfusion. The renal vasoconstrictive effect of OKY-046 was blunted by an angiotensin converting enzyme (ACE) inhibitor, MK422, or an angiotensin II receptor antagonist, Saralasin. On the contrary, OKY-046 ameliorated the renal hypoperfusion by decreasing RVR in 28-week-old diabetic rats. Chronic oral administration of OKY-046 ameliorated not only the renal hyperperfusion but increased urinary albumin excretion (UAE) at two weeks, but also the renal hypoperfusion, filtration fraction and UAE at 24 weeks. It is suggested that TXA2 might, at least in part, play important roles in the hyperperfusion by modulating activity of the renin-angiotensin system at an early stage of untreated diabetic rats and in the hypoperfusion at the late stage of untreated diabetic rats, and that TXA2 is also involved in the increase of UAE. These results support roles for TXA2 in the progression of renal injury in STZ-induced diabetic rats.


Subject(s)
Diabetes Mellitus, Experimental/physiopathology , Hemodynamics/drug effects , Kidney/physiopathology , Thromboxane A2/physiology , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Kidney/drug effects , Male , Methacrylates/pharmacology , Rats , Rats, Sprague-Dawley , Receptors, Thromboxane/antagonists & inhibitors , Renal Circulation , Streptozocin , Sulfonamides/pharmacology , Thromboxane-A Synthase/antagonists & inhibitors , Vascular Resistance/physiology , Vasoconstriction/drug effects
9.
Diabetologia ; 36(6): 475-80, 1993 Jun.
Article in English | MEDLINE | ID: mdl-8335167

ABSTRACT

To elucidate the diabetogenic effect of growth hormone on glucose metabolism the regulation of glucose transporter (GLUT) gene expression was examined in rat skeletal muscles. Female Wistar-Furth rats were implanted subcutaneously with growth-hormone-producing pituitary tumour (GH3) cells. Animals were killed 4 or 9 weeks after GH3 cell injection. Although body weight, serum growth hormone and insulin-like growth factor I levels were remarkably elevated during the 4-9 week period, serum blood glucose levels were within normal range. Muscles were obtained from the quadriceps muscle, diaphragm and heart, respectively. Northern blot analysis and Western blot analysis were performed using specific cDNA probes and antibodies. During the 4-9 week period, the levels of muscle GLUT1 and 4 mRNA (corrected by beta-actin mRNA level) in each muscle from the rats injected with tumour cells were not significantly different from those of control rats. Chronic elevation of growth hormone in these rats did not cause any change in GLUT 1 and 4 expression compared to the controls during the euglycaemic period. These results provide the first evidence that chronic growth hormone elevation itself does not affect a key gene of in vivo glucose metabolism.


Subject(s)
Gene Expression , Growth Hormone/physiology , Monosaccharide Transport Proteins/biosynthesis , Muscles/metabolism , Myocardium/metabolism , Pituitary Neoplasms/metabolism , RNA, Messenger/metabolism , Animals , Blood Glucose/metabolism , Blotting, Northern , Blotting, Western , Female , Growth Hormone/blood , Growth Hormone/metabolism , Insulin/blood , Insulin-Like Growth Factor I/metabolism , Monosaccharide Transport Proteins/isolation & purification , Neoplasm Transplantation , Organ Specificity , RNA, Messenger/analysis , Rats , Rats, Inbred WF , Reference Values
10.
Biochem Biophys Res Commun ; 182(1): 34-8, 1992 Jan 15.
Article in English | MEDLINE | ID: mdl-1310015

ABSTRACT

Two isoforms of calcineurin beta subunit(beta 1 and beta 2) were identified in rat testis by a monoclonal antibody Va1. Both beta 1 and beta 2 were recovered in calmodulin binding protein fraction and showed calcium shift on SDS-polyacrylamide gel electrophoresis which is the specific character for EF-hand calcium binding protein. beta 2 showed same apparent molecular weight on SDS-PAGE as that of brain calcineurin beta and was found in wide variety of tissues. beta 1 was shown to have six amino acid polypepeptide sequence and it showed higher molecular weight than brain beta and was specific for testis.


Subject(s)
Calmodulin-Binding Proteins/analysis , Isoenzymes/analysis , Phosphoprotein Phosphatases/analysis , Testis/enzymology , Amino Acid Sequence , Animals , Antibodies, Monoclonal , Calcineurin , Calmodulin-Binding Proteins/isolation & purification , Electrophoresis, Polyacrylamide Gel , Immunoblotting , Macromolecular Substances , Male , Molecular Sequence Data , Oligopeptides/chemical synthesis , Oligopeptides/isolation & purification , Rats
11.
Biochem Biophys Res Commun ; 180(3): 1476-82, 1991 Nov 14.
Article in English | MEDLINE | ID: mdl-1659420

ABSTRACT

We have cloned and sequenced rat testis cDNAs coding for a calcium binding polypeptide similar to calcineurin beta subunit, the Ca(2+)-binding subunit of the Ca2+/calmodulin stimulated protein phosphatase. Rat testis cDNA library was screened with a monoclonal antibody Va1 raised against bovine brain calcineurin beta subunit. The deduced amino acid sequence is similar to that of human brain calcineurin beta subunit with respect to containing four putative calcium binding sites. However, distinct differences were found: 1) The cloned cDNA had six amino acids polypeptide tail at carboxy-terminal which is absent in human brain calcineurin beta subunit. This amino acids tail makes the carboxy-terminal highly hydrophilic in contrast to the human brain beta subunit which is hydrophobic at carboxy-terminal; 2) eleven amino acids at the N terminal of the cloned cDNA were completely different from the corresponding region of the brain calcineurin beta subunit.


Subject(s)
Calcium-Binding Proteins/genetics , Calmodulin-Binding Proteins/genetics , DNA/genetics , Phosphoprotein Phosphatases/genetics , Testis/metabolism , Amino Acid Sequence , Animals , Base Sequence , Brain/metabolism , Calcineurin , Calcium-Binding Proteins/isolation & purification , Cloning, Molecular , Codon , DNA/isolation & purification , Escherichia coli/genetics , Gene Library , Humans , Macromolecular Substances , Male , Molecular Sequence Data , Protein Conformation , Rats , Recombinant Proteins/isolation & purification , Restriction Mapping , Sequence Homology, Nucleic Acid
12.
Biochem Int ; 24(6): 1119-25, 1991 Aug.
Article in English | MEDLINE | ID: mdl-1723595

ABSTRACT

Calcineurin (calcium- and calmodulin-stimulated phosphatase) alpha subunit purified from bovine brain was found to be composed of two polypeptides, 61 KDa (alpha 1) and 59 KDa (alpha 2). The two peptides were separated and extracted from polyacrylamide gel. The immuno-peptide mapping of the purified peptides by partial proteolysis showed that the 59-KDa polypeptide was not a degradative product of the 61-KDa polypeptide. The interaction of the enzyme with two monoclonal antibodies, Vj6 and Vd3, raised against bovine brain calcineurin revealed that the 61-KDa polypeptide was recognized by both Vj6 and Vd3, whereas the 59-KDa one was recognized only by Vj6. These results indicate that there are at least two isoforms of calcineurin alpha subunits in bovine brain.


Subject(s)
Brain Chemistry , Calmodulin-Binding Proteins/chemistry , Phosphoprotein Phosphatases/chemistry , Animals , Antibodies, Monoclonal/immunology , Blotting, Western , Calcineurin , Calmodulin-Binding Proteins/analysis , Calmodulin-Binding Proteins/immunology , Cattle , Electrophoresis, Polyacrylamide Gel , Peptide Mapping , Peptides/analysis , Phosphoprotein Phosphatases/analysis , Phosphoprotein Phosphatases/immunology , Staining and Labeling
13.
Brain Res ; 557(1-2): 103-8, 1991 Aug 23.
Article in English | MEDLINE | ID: mdl-1747744

ABSTRACT

The role of intracellular Zn2+ in the translocation of protein kinase C from cytosol to membrane fractions was examined by the [3H]phorbol 12,13-dibutyrate (PDBu) binding method in guinea pig cerebral synaptoneurosomes. N-methyl-D-aspartate (NMDA, 100 microM) and calcium ionophore A23187 (0.3-30 microM) decreased the binding activity in the cytosol with a concomitant increase in the membrane fractions. Pretreatment of synaptoneurosomes with a heavy metal chelator, N,N,N',N'-tetrakis-(2-pyridylmethyl)ethylenediamine (TPEN), inhibited the NMDA- and A23187-induced changes of the distribution of [3H]PDBu binding sites in cytosol and membrane fractions. The inhibitory effect of TPEN was negated by a preincubation of TPEN with equimolar Zn2+ but not by that with Ca2+. The addition of 500 microM Zn2+ to the lysate of synaptoneurosomes induced an increase of [3H]PDBu binding activity in the membrane fraction with a concomitant decrease in the cytosol fraction, as did 100 microM Ca2+. Low concentrations of Zn2+ (10 microM), which alone had no effect on the distribution of the binding, significantly enhanced the effect of 10 microM Ca2+ in the lysate. Under those conditions TPEN inhibited the Zn(2+)-potentiated Ca(2+)-dependent changes in the binding. These results suggest that intracellular Zn2+ is essential for the agonist-induced translocation of protein kinase C in guinea pig synaptoneurosomes.


Subject(s)
Chelating Agents/pharmacology , N-Methylaspartate/antagonists & inhibitors , Protein Kinase C/metabolism , Zinc/physiology , Animals , Calcimycin/pharmacology , Calcium Radioisotopes , Cations, Divalent/pharmacology , Cerebral Cortex/drug effects , Cerebral Cortex/enzymology , Cytosol/enzymology , Egtazic Acid/pharmacology , Ethylenediamines/pharmacology , Guinea Pigs , In Vitro Techniques , Male , N-Methylaspartate/pharmacology , Neurons/drug effects , Neurons/enzymology , Phorbol 12,13-Dibutyrate/pharmacology , Synaptosomes/drug effects , Synaptosomes/enzymology , Zinc/pharmacology
14.
Jpn J Pharmacol ; 56(3): 287-96, 1991 Jul.
Article in English | MEDLINE | ID: mdl-1895575

ABSTRACT

N-methyl-D-aspartate (NMDA)-induced translocation of protein kinase C from the cytosol to membrane fractions was examined by the [3H]phorbol 12,13-dibutyrate (PDBu) binding method in guinea pig cerebral synaptoneurosomes. Pretreatment of synaptoneurosomes with NMDA, but not that with quisqualate or kainate, induced changes in the distribution of [3H]PDBu binding in the cytosol and membrane fractions in a dose-dependent manner. The NMDA-induced changes of the binding were completely dependent on Ca2+ and inhibited by NMDA receptor antagonists Mg2+, 2-amino-5-phosphonovaleric acid and ketamine, but not by Zn2+. Glycine slightly potentiated the NMDA-induced changes of [3H]PDBu binding. NMDA stimulated Ca2+ uptake but not the phosphoinositide hydrolysis in the synaptoneurosomes. These results suggest that NMDA enhances Ca2+ influx through receptor-operated Ca2+ channels, increasing intracellular calcium concentration and thereby induces translocation of protein kinase C.


Subject(s)
Brain/drug effects , N-Methylaspartate/pharmacology , Protein Kinase C/analysis , Synaptosomes/drug effects , Animals , Brain/enzymology , Calcium/metabolism , Cytosol/drug effects , Cytosol/enzymology , Guinea Pigs , In Vitro Techniques , Phorbol 12,13-Dibutyrate/metabolism , Synaptosomes/enzymology
15.
Neurosci Lett ; 126(2): 119-22, 1991 May 27.
Article in English | MEDLINE | ID: mdl-1922921

ABSTRACT

N-Methyl-D-aspartate (NMDA)-induced translocation of protein kinase C (PKC) from cytosol to membrane fractions was examined by the methods of [3H]phorbol 12,13-dibutyrate binding and western blotting in rat hippocampal slices. NMDA and L-glutamate induced translocation of PKC from cytosol to membrane fractions in immature rat hippocampal slices, but not in mature ones. The NMDA-induced translocation of PKC was dependent on Ca2+. It was inhibited by the NMDA receptor antagonists, 2-amino-5-phosphonovaleric acid and ketamine, but not by Mg2+ and Zn2+. These results suggest that stimulation of NMDA receptors enhances Ca2+ influx and thereby induces translocation of PKC in immature rat hippocampus.


Subject(s)
Hippocampus/metabolism , N-Methylaspartate/pharmacology , Protein Kinase C/metabolism , Aging/metabolism , Animals , Animals, Newborn , Biological Transport , Cell Membrane/metabolism , Chemical Fractionation , Cytosol/metabolism , Immunoblotting , In Vitro Techniques , Phorbol 12,13-Dibutyrate/metabolism , Rats
16.
Biochem Int ; 23(1): 137-43, 1991 Jan.
Article in English | MEDLINE | ID: mdl-1863266

ABSTRACT

A promyelocytic leukemia cell line, HL-60, was induced to differentiate into monocyte-macrophage lineage cells by treatment with active vitamin D3 and phorbol esters, and into granulocyte lineage ones by retinoic acid and dimethylsulfoxide. The changes in intracellular concentration of free calcium ions ([Ca2+]i) were measured and analyzed by calcium-imaging analysis with Fura 2-AM. A significant and transient increase in [Ca2+]i was observed in active vitamin D3 and phorbol ester systems; however, no change was detected with retinoic acid and dimethylsulfoxide. This increase was due to the influx of calcium ions from outside of the cells, and L-type calcium channels were shown to mainly contribute to this influx. Protein kinase C was also shown to be involved in the increase in [Ca2+]i.


Subject(s)
Calcitriol/analogs & derivatives , Calcitriol/pharmacology , Calcium/metabolism , Macrophages/metabolism , Tetradecanoylphorbol Acetate/pharmacology , Calcium/analysis , Cell Differentiation , Dimethyl Sulfoxide/pharmacology , Fura-2/analogs & derivatives , Granulocytes/metabolism , Humans , Leukemia, Promyelocytic, Acute , Monocytes/metabolism , Protein Kinase C/metabolism , Spectrophotometry, Ultraviolet , Tretinoin/pharmacology , Tumor Cells, Cultured
17.
Exp Hematol ; 18(11): 1152-7, 1990 Dec.
Article in English | MEDLINE | ID: mdl-1699772

ABSTRACT

It has been demonstrated that purified recombinant interleukin 5 (rIL-5) supports the terminal differentiation and proliferation of eosinophilic precursors in vitro and plays an important role in increasing the functional activities of eosinophils. In this study, we examined the hemopoietic changes and analyzed murine (m) IL-5 mRNA expression in eosinophilic mice infected with the helminth Toxocara canis. In eosinophilic mice, eosinophils increased in number in both bone marrow and spleen. However, the number of eosinophilic precursors increased markedly in spleen cells of eosinophilic mice but remained relatively constant in the bone marrow. In the presence of granulocyte colony-stimulating factor (G-CSF), the number of granulocytic precursors increased in the spleen cells of eosinophilic mice. From these findings, the condition of eosinophilopoiesis in eosinophilic mice is accompanied by an increase in granulocyte-macrophage progenitors as well as eosinophil progenitors. Using Northern blot analysis, a weak but definite band corresponding to mIL-5 mRNA was detected in spleen cells of mice 4 and 5 days after helminthic infection. In addition, these data were confirmed by in vitro polymerase chain reaction (PCR) amplification of mRNA obtained from these spleen cells. Finally, injections of a monoclonal antibody against mIL-5 completely suppressed the blood eosinophilia in mice infected with T. canis. In conclusion, IL-5 is suggested to play a major role in eosinophilopoiesis in vivo.


Subject(s)
Eosinophilia/pathology , Gene Expression , Hematopoietic Stem Cells/pathology , Interleukin-5/genetics , Toxocariasis , Animals , Antibodies, Monoclonal/pharmacology , Bone Marrow/pathology , Eosinophilia/metabolism , Eosinophils/pathology , Female , Granulocyte Colony-Stimulating Factor/pharmacology , Granulocytes/pathology , Hematopoiesis , Interleukin-5/immunology , Macrophages/pathology , Mice , Mice, Inbred BALB C , Nucleic Acid Hybridization , Polymerase Chain Reaction , RNA, Messenger/genetics , Spleen/pathology
19.
Br J Pharmacol ; 100(3): 564-8, 1990 Jul.
Article in English | MEDLINE | ID: mdl-2117981

ABSTRACT

1. The effects of a novel anti-asthmatic drug, 3-isobutyryl-2-isopropylpyrazolo [1,5-a]pyridine (ibudilast, KC-404) on leukotriene D4 (LTD4)-induced formation of inositol phosphates were studied in slices of guinea-pig lung and hippocampus. 2. In guinea-pig lung, ibudilast inhibited LTD4 (0.01-1 microM)-induced formation of inositol monophosphate (IP1) in a concentration-dependent manner (IC50 = 10 microM) without affecting LTD4 receptor binding. 3. Ibudilast (10 microM) inhibited histamine (0.1-1 mM)-induced formation of IP1 in guinea-pig lung slices but not in hippocampal slices. 4. Inhibition of agonist-induced formation of IP1 by ibudilast was non-competitive. 5. Ibudilast had no effect on either GTP- or calcium-stimulated phosphatidylinositol specific-phospholipase C activity of lung membranes. 6. These results suggest that ibudilast has no direct effect on LTD4 receptors, GTP binding proteins (G proteins) or phospholipase C, but inhibits inositol phosphate formation, possibly by interfering with the coupling between receptors and G proteins.


Subject(s)
Inositol Phosphates/metabolism , Lung/metabolism , Pyridines/pharmacology , SRS-A/antagonists & inhibitors , Vasodilator Agents/pharmacology , Animals , Calcium Chloride/pharmacology , GTP-Binding Proteins/metabolism , Guanosine Triphosphate/pharmacology , Guinea Pigs , Hippocampus/drug effects , Hippocampus/metabolism , In Vitro Techniques , Inositol/metabolism , Lung/drug effects , Male , Membranes/drug effects , Membranes/metabolism , SRS-A/metabolism
20.
Acta Med Okayama ; 44(1): 1-8, 1990 Feb.
Article in English | MEDLINE | ID: mdl-2330841

ABSTRACT

Peptides and proteins in the extracellular space in the central nervous system were investigated in vivo using an intracerebral microdialysis probe. The molecular cut-off of the hollow fiber which was used for the probe was approximately 100 kDa. We examined recovery rates of several compounds in vitro. The recovery rates of proteins and peptides were between 7-28%, with the exceptions of substance P and insulin-like growth factor I. The recovery rates of monoamines and their metabolites were 22-40%. In in vivo studies, two major proteins with apparent molecular weights of 62 kDa and 12 kDa, and several minor proteins (28 kDa, 43 kDa, 52 kDa and 70 kDa) were detected by SDS-polyacrylamide gel electrophoresis in the dialysate from a probe implanted in the striatum of anesthetized rats. These results suggest that the newly developed, intracerebral microdialysis probe might be useful for investigating the dynamic changes of peptides and proteins in the central nervous system.


Subject(s)
Brain Chemistry , Extracellular Space/analysis , Proteins/analysis , Animals , Dialysis/instrumentation , Electrophoresis, Polyacrylamide Gel , Equipment Design , Peptides/analysis , Rats , Rats, Inbred Strains
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