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  • 1
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    Larval ontogeny of a percichthyid fish, Synagrops philippinensis (Günther) in Kagoshima Bay, southern Japan (2021)
    In:  http://aquaticcommons.org/id/eprint/16354 | 12051 | 2015-03-27 10:15:08 | 16354 | Bangladesh Fisheries Research Institute
    Details
    Publication Date: 2021-07-04
    Description: The larval ontogeny of a developmental series (1.2-8.3mm body length, BL) of Synagrops philippinensis from Kagoshima Bay, southern Japan is described and illustrated. The yolk was completely absorbed in larva of ≥1.5 mm BL. Notochord flexion commenced at about 3.5mm BL and was completed by about 4.0-4.5mm BL. S. philippinensis larvae were distinguished from their congeners based on melanophore patterns, head spination and fin spines and rays. Larvae of 7.5-8.3 mm BL were characterized by anteriorly serrated pelvic spine, two anal spines, nine inner preopercular spines and no melanophore on lateral side of the caudal peduncle; 7.0 to 7.5mm BL larvae by the above characters except serration on pelvic spine; and yolk-sac, pre-flexion, flexing and post-flexion larvae up to 7.0mm BL by unique melanophores on lower lobe of pectoral finfold/fin.
    Keywords: Biology ; Synagrops philippinensis ; larval ontogeny ; Kagoshima Bay ; Japan
    Repository Name: AquaDocs
    Type: article
    Format: application/pdf
    Format: application/pdf
    Format: 17-24
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  • 2
    Electronic Resource
    Electronic Resource
    Oxidation of ruthenium(II) and ruthenium(III) porphyrins. Crystal structures of .mu.-oxo-bis[(p-methylphenoxo)(meso-tetraphenylporphyrinato)ruthenium(IV)] and ethoxo(meso-tetraphenylporphyrinato)(ethanol)ruthenium(III)-bisethanol (1984)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 106 (1984), S. 5151-5163 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00330a020
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of the mutant gene for L-gulono-γ-lactone oxidase in scurvy-prone rats (1989)
    Springer
    Cellular and molecular life sciences 45 (1989), S. 126-129 
    Details
    ISSN: 1420-9071
    Keywords: L-gulono-γ-lactone oxidase ; ascorbic acid deficiency ; enzyme defect ; rat ; nuclei acid hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A mutant strain of Wistar rats with L-gulono-γ-lactone oxidase deficiency has recently been established. To investigate this deficiency by DNA and RNA blot hybridization analyses, a fragment of a previously cloned cDNA encoding rat L-gulono-γ-lactone oxidase was used as a probe. When genomic DNA of the mutant rat was digested with several restriction enzymes, the probe hybridized to fragments of the same sizes as those produced from DNA of normal rats. Poly(A)+RNA from the liver of the mutant rat was found to contain an L-gulono-γ-lactone oxidase-specific mRNA of a normal size at a comparable level to that of normal rats. An in vitro translation experiment revealed that the mRNA programmed the synthesis of an enzyme protein which had the same molecular weight as that of the translational product of the normal mRNA, although the amount synthesized was markedly reduced as compared with that synthesized with the normal mRNA. In accordance with this observation, a very low but definite degree of L-gulono-γ-lactone oxidase activity was detected in the microsomes of the mutant rat by a newly developed, highly sensitive method.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01954844
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  • 4
    Electronic Resource
    Electronic Resource
    Intracellular pH regulation in the mouse lacrimal gland acinar cells (1988)
    Springer
    The journal of membrane biology 101 (1988), S. 73-81 
    Details
    ISSN: 1432-1424
    Keywords: intracellualr pH ; lacrimal gland ; amiloride ; DIDS ; Na+/H+ antiport ; Cl−/HCO 3 − ; antiport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Intracellular pH (pH i ) of the acinar cells of the isolated, superfused mouse lacrimal gland has been measured using pH-sensitive microelectrodes. Under nonstimulated condition pH i was 7.25, which was about 0.5 unit higher than the equilibrium pH. Alterations of the external pH by ±0.4 unit shifted pH i only by ±0.08 unit. The intracellular buffering value determined by applications of 25mm NH 4 + and bicarbonate buffer solution gassed with 5% CO2/95% O2 was 26 and 46mm/pH, respectively Stimulation with 1 μm acetylcholine (ACh) caused a transient, small decrease and then a sustained increase in pH i . In the presence of amiloride (0.1mm) or the absence of Na+, application of ACh caused a significant decrease in pH i and removal of amiloride or replacement with Na+-containing saline, respectively, rapidly increased the pH i . Pretreatment with DIDS (0.2mm) did not change the pH i of the nonstimulated conditions; however, it significantly enhanced the increase in pH i induced by ACh. The present results showed that (i) there is an active acid extrusion mechanism that is stimulated by ACh; (ii) stimulation with ACh enhances the rate of acid production in the acinar cells; and (iii) the acid extrusion mechanism is inhibited by amiloride addition to and Na+ removal from the bath solution. We suggest that both Na+/H+ and HCO 3 − /Cl− exchange transport mechanisms are taking roles in the intracellular pH regulation in the lacrimal gland acinar cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01872822
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of Ryanodine-sensitive Ca2+ Release from Microsomal Vesicles of Rat Parotid Acinar Cells: Regulation by Cyclic ADP-ribose (1997)
    Springer
    The journal of membrane biology 156 (1997), S. 231 -239 
    Details
    ISSN: 1432-1424
    Keywords: Key words:45Ca2+ efflux — Caffeine — Ruthenium red — Heparin — Endoplasmic reticulum — Thapsigargin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. We have measured ryanodine (caffeine)-sensitive 45Ca2+ release from isolated microsomal vesicles of endoplasmic reticulum prepared from rat parotid acinar cells. After a steady state of ATP-dependent 45Ca2+ uptake, the addition of caffeine (40 mm), ryanodine (10∼500 μm) or an NAD+ metabolite, cyclic ADP-ribose (cADPR, 4 μm) released about 10% of the 45Ca2+ that had been taken up. The 45Ca2+ release was not inhibited by heparin, an antagonist of IP3 receptor. The effects of caffeine, ryanodine and cADPR on 45Ca2+ release were also tested in the presence of thapsigargin (TG), an inhibitor of microsomal Ca2+-ATPase. When caffeine (10∼40 mm), ryanodine (10 μm) or cADPR (1∼10 μm) was added in the medium with 100 nm TG, a significant 45Ca2+ release was seen, while higher concentrations of ryanodine (〉100 μm) did not cause any 45Ca2+ release in the presence of TG. The initial rate of caffeine (40 mm)-induced 45Ca2+ release was increased by a pretreatment with 10 μm ryanodine, whereas the caffeine-induced 45Ca2+ release was strongly inhibited by the presence of a higher concentration (500 μm) of ryanodine. cADPR-induced 45Ca2+ release was also inhibited by 500 μm ryanodine. Caffeine (40 mm)- or cADPR (4 μm)-induced 45Ca2+ release was abolished by a presence of ruthenium red (50∼100 μm). The presence of a low concentration (0.5 μm) of cADPR shifted the dose-response curve of caffeine-induced 45Ca2+ release to the left. These results indicate the presence of a ryanodine sensitive Ca2+ release mechanism in the endoplasmic reticulum of rat parotid acinar cells that is distinct from the IP3-sensitive Ca2+ channel and is activated by caffeine, cADPR and a low concentration (10 μm) of ryanodine, but is inhibited by higher concentrations (〉100 μm) of ryanodine and ruthenium red. The properties of the ryanodine-sensitive mechanism are similar to that of the ryanodine receptor as described in muscle cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002329900203
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of two different Ca2+ uptake and IP3-sensitive Ca2+ release mechanisms in microsomal Ca2+ pools of rat pancreatic acinar cells (1995)
    Springer
    The journal of membrane biology 144 (1995), S. 111-120 
    Details
    ISSN: 1432-1424
    Keywords: Thapsigargin ; Vanadate ; Ca2+ pump ; Ca2+ ATPase ; SERCA ; Endoplasmic reticulum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have examined the effect of the Ca2+ (Mg2+)-ATPase inhibitors thapsigargin (TG) and vanadate on ATP-dependent 45Ca2+ uptake into IP3-sensitive Ca2+ pools in isolated microsomes from rat pancreatic acinar cells. The inhibitory effect of TG was biphasic. About 40–50% of total Ca2+ uptake was inhibited by TG up to 10 nm (apparent Ki≈4.2 nm, Ca2+ pool I). An additional increase of inhibition up to 85–90% of total Ca2+ uptake could be achieved at 15 to 20 nm of TG (apparent Ki≈12.1 nm, Ca2+ pool II). The rest was due to TG-insensitive contaminating plasma membranes and could be inhibited by vanadate (apparent Ki≈10 μm). In the absence of TG, increasing concentrations of vanadate also showed two phases of inhibition of microsomal Ca2+ uptake. About 30–40% of total Ca2+ uptake was inhibited by 100 μm of vanadate (apparent Ki≈18 μm, Ca2+ pool II). The remaining 60–70% could be inhibited either by vanadate at concentrations up to 1 mm (apparent Ki≈300 μm) or by TG up to 10 nm (Ca2+ pool I). The amount of IP3-induced Ca2+ release was constant at ≈25% over a wide range of Ca2+ filling. About 10–20% remained unreleasable by IP3. Reduction of IP3 releasable Ca2+ in the presence of inhibitors showed similar dose-response curves as Ca2+ uptake (apparent Ki≈ 3.0 nm for IP3-induced Ca2+ release as compared to ≈4.2 nm for Ca2+ uptake at TG up to 10 nm) indicating that the highly TG-sensitive Ca2+ pump fills the IP3-sensitive Ca2+ pool I. At TG concentrations 〉10 nm which blocked Ca2+ pool II the apparent Ki values were ≈11.3 and ≈12.1 nm, respectively. For inhibition by vanadate up to 100 μm the apparent Ki values were ≈18 μm for Ca2+ uptake and ≈7 μm for Ca2+ release (Ca2+ pool II). At vanadate concentrations up to 1 mm the apparent Ki values were ≈300 and ≈200 μm, respectively (Ca2+ pool I). Both Ca2+ pools I and II also showed different sensitivities to IP3. Dose-response curves for IP3 in the absence of inhibitors (control) showed an apparent Km value for IP3 at 0.6 μm. In the presence of TG (inhibition of Ca2+ pool I) the curve was shifted to the left with an apparent Km for IP3 at 0.08 μm. In the presence of vanadate (inhibition of Ca2+ pool II), the apparent Km for IP3 was 2.1 μm. These data allow the conclusion that there are at least three different Ca2+ uptake mechanisms present in pancreatic acinar cells: TG- and IP3 insensitive but highly vanadate-sensitive Ca2+ uptake occurs into membrane vesicles derived from plasma membranes. Two Ca2+ pools with different TG-, vanadate- and IP3-sensitivities are most likely located in the endoplasmic reticulum at different cell sites, which could have functional implications for hormonal stimulation of pancreatic acinar cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232797
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  • 7
    Electronic Resource
    Electronic Resource
    DNA MUTATION INDUCED IN THE SEQUENCE UPSTREAM OF THE SECRETED MYU C-TERMINAL CODING SEQUENCE BY ULTRAVIOLET IRRADIATION IN THE CELL LINE OF BLOOM'S SYNDROME (1995)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 22 (1995), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Selective IgM deficiency is commonly found in Bloom's syndrome (BS). We reported that membrane-bound μ (μ m) mRNA was well transcribed but secreted μ (μ s) mRNA was not, although there was no mutation or deletion in the sequence including the (is C-terminal coding sequence in the patients with BS. Furthermore, we have shown previously, preferential damage to IgM production by ultraviolet (UV) irradiation of the cells of the patient. In the study described here, mutation in the sequence which is upstream of the 5’ end of the μ s C-terminal coding sequence was induced by UV irradiation in the lymphoblastoid cell line (LCL) of BS patient. These results suggest that abnormal repair of DNA damage is present in this LCL, and that preferential damage to IgM production by UV irradiation in this LCL may be due to the abnormal repair of DNA damage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1995.tb00226.x
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  • 8
    Electronic Resource
    Electronic Resource
    A WILD-TYPE μs C-TERMINAL GENE IS EXPRESSED IN BLOOM'S SYNDROME CELLS (1994)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 21 (1994), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Selective IgM deficiency is found commonly in patients with Bloom's syndrome (BS). Serum IgM concentrations were low though serum IgG and IgA concentrations were normal in both patients with BS included in the study. In a previous study the authors showed that selective IgM deficiency in BS is due to an abnormality in the maturation of surface IgM-bearing cells into IgM-secreting cells and a failure of secreted μ (μ s) mRNA synthesis. The membrane-bound μ (μ m) and μ s mRNA are produced from transcripts of a single immunoglobulin μ gene by alternative RNA processing pathways. The control of μ s mRN A synthesis depends on the addition of poly(A) to μ s C-terminal segment. The study described here demonstrated that there was no mutation or deletion in the sequence including μ s C-terminal coding sequence, the RNA splice site (GG/TAAAC) at the 5’ end of μ s C-terminal segment, and the AATAAA poly(A) signal sequence, and second GT-rich element immediately down-stream of the cleavage site in both patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1994.tb00184.x
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  • 9
    Electronic Resource
    Electronic Resource
    Occurrence in humans and guinea pigs of the gene related to their missing enzyme l-gulono-γ-lactone oxidase
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 267 (1988), S. 842-846 
    Details
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-9861(88)90093-8
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  • 10
    Electronic Resource
    Electronic Resource
    Monovalent cations and inorganic phosphate alter branched-chain α-ketoacid dehydrogenase-Kinase activity and inhibitor sensitivity
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 266 (1988), S. 210-218 
    Details
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-9861(88)90252-4
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