Sinzi Matuoka

Sapporo Medical University, Sapporo, Hokkaidō, Japan

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Publications (22)58.76 Total impact

  • [Show abstract] [Hide abstract]
    ABSTRACT: Structures and phase behavior of multilamellar vesicles of 1,2-dipalmitoyl-L-phosphatidylcholine (DPPC) containing various amount of ganglioside GM3 with a C18:1 sphingoid base and a 24:0 acyl chain (GM3(18,24)) were investigated by small-angle X-ray diffraction. Below 3.5 mol% GM3 content, the phase behavior was similar to that of pure DPPC except for a slight increase of lamellar repeat distance in the L(beta'), the P(beta') and the L(alpha) phases and a decrease of the pretransition temperature. In the range of 4-12 mol% GM3 content, another phase which has larger repeat distances coexisted with the phase observed below 3.5 mol% GM3 content. This has been interpreted that the phase separation into GM3-poor phase (denoted as A-phase) and GM3-rich phase (denoted as B-phase) took place. Above 13 mol% GM3 content, the B-phase became dominant. This phase separation may be related to the formation of GM3-enriched microdomains that had been observed on the cell surfaces which express large amounts of GM3, such as murine B16 melanoma (J. Biol. Chem. 260 (1985) 13328).
    No preview · Article · Apr 2003 · Chemistry and Physics of Lipids
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    ABSTRACT: In order to investigate the relationship between the structural change and the endothermic heat at the main transition in dipalmitoylphosphatidylcholine (DPPC)-water systems with three different water concentrations (60, 25 and 15 wt%), we have performed simultaneous differential scanning calorimetry (DSC) and time-resolved X-ray diffraction. The changes of wide-angle X-ray diffraction pattern for the hydrocarbon chain packing were compared quantitatively with the endothermic heat at the main transition. In contrast to the fully hydrated sample with water concentration 60 wrt%, a broad and asymmetric curve was observed in the DSC thermogram in the samples with the water content, 15 and 25 wt%. On the other hand, the wide-angle X-ray diffraction patterns recorded simultaneously suggest that the gel and the liquid-crystalline phases coexist in the transition region. The fraction of the liquid-crystalline phase is estimated from the wide-angle X-ray diffraction profiles in the coexistence region. This fraction agrees with the normalized integrated DSC curves. Therefore, the endothermic heat at the main transition of DPPC correlates largely with the melting of the hydrocarbon chains.
    No preview · Article · May 1995 · Chemistry and Physics of Lipids
  • I. Hatta · H. Takahashi · S. Matuoka · Y. Amemiya
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    ABSTRACT: Regarding phase transitions, it is important to study both the thermodynamic behavior and the microscopic structure. To learn about the detailed mechanism of phase transitions, it is highly desirable to make clear the correlation between the thermodynamic behavior and the microscopic structure. For this purpose, we developed the simultaneous measurement of X-ray diffraction and differential scanning calorimetry, using synchrotron X-rays.
    No preview · Article · Apr 1995 · Thermochimica Acta
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    S Matuoka · S Kato · I Hatta
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    ABSTRACT: The ripple structure was studied as a function of temperature in fully hydrated dimyristoylphosphatidylcholine (DMPC)/cholesterol multibilayers using synchrotron x-ray small-angle diffraction and freeze-fracture electron microscopy. In the presence of cholesterol, the ripple structure appears below the pretransition temperature of pure DMPC multibilayers. In this temperature range the ripple periodicity is relatively large (25-30 nm) and rapidly decreases with increasing temperature. In this region, defined as region I, we observed coexistence of the P beta' phase and the L beta' phase. The large ripple periodicity is caused by the formation of the P beta' phase region in which cholesterol is concentrated and the L beta' phase region from which cholesterol is excluded. An increase in ripple periodicity also takes place in the narrow temperature range just below the main transition temperature. We define this temperature region as region III, where the ripple periodicity increases dramatically toward the main transition temperature. In region II, between regions I and III, the ripple periodicity decreases gradually with temperature. This behavior is quite similar to that of pure DMPC. Temperature-versus-ripple periodicity curves are parallel among pure DMPC and DMPCs with various cholesterol contents. We explain this behavior in terms of a model proposed by other workers.
    Preview · Article · Sep 1994 · Biophysical Journal
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    ABSTRACT: Model membranes of diacylphosphatidylcholines (CnPC), with saturated linear acyl chains of n > 12 carbons, show a single sharp phase transition (known as the main transition) between the gel phase P beta' and the liquid crystalline phase L alpha with differential scanning calorimetry. However, C12PC (dilauroylphosphatidylcholine) shows, as well as the sharp transition at -2 degrees C, a broad peak at 5 degrees C, originally observed by S. Mabrey and J.M. Sturtevant. The broad peak is not artificial: between the two peaks a new phase Lx was predicted for (C12PC) bilayers on the basis of calorimetry (Finegold, Shaw and Singer, Chem. Phys. Lipids 53 (1990), 177-184). The existence of Lx has now been confirmed by synchrotron X-ray diffraction on samples identical to those of the previous work, of similar preparation and at corresponding scan rates. With temperature, both small-angle (long lamellar) and wide-angle (hydrocarbon chain) spacings show abrupt discontinuities, and separate broader changes, at temperatures corresponding to the calorimetric sharp and broad peaks, respectively. All the X-ray diffraction profiles and spacing results are consistent with the following phase scheme with increasing temperature: gel ripple phase P beta'-->new, less ordered liquid crystalline phase Lx-->most disordered liquid crystalline phase L alpha. The phase Lx possibly exists in other CnPCs, and its examination may provide details of the main transition. Because Lx exists at a higher temperature than the main transition from P beta', it promises to be of biological relevance.
    No preview · Article · Feb 1994 · Chemistry and Physics of Lipids
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    S Matuoka · H Yao · S Kato · I Hatta
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    ABSTRACT: In the ripple phase of fully hydrated multilamellar vesicles of dipalmitoylphosphatidylcholine (DPPC), two kinds of small-angle x-ray diffraction profiles are observed on cooling through the main transition. One is a seemingly normal profile similar to that observed on heating and the other is the superposition of the diffraction profiles for the primary (normal) and the secondary ripple structures. We found that the profile obtained depended on the cooling rate. Increasing the cooling rate from 0.1 degrees C/min to 1 degrees C/min caused the peaks originating from the secondary ripple structure to diminish. After a cooling scan at 43 degrees C/min, the profile became similar to that of the normal ripple structure, although a trace of the secondary ripple structure remains. The results are interpreted in terms of the rise and fall of three-dimensional correlated domains composed of both primary and secondary ripple structures. At slow cooling rates, correlated domains of both kinds of ripple structures develop. As the cooling rate is increased, the domain of the primary ripple structure remains correlated, while that of the secondary ripple structure becomes less correlated. In addition, the multipeak profile appears even at rapid cooling rates, if the final low temperature lies just below the Tm for the main transition. This results suggests that formation of the correlated domains of the secondary ripple structure requires a certain time interval during which the DPPC vesicles experience the temperature just below the main transition. The secondary ripple structure takes place in phosphatidylcholines having more than 15 carbons in each hydrocarbon chain upon cooling through the main transition.
    Preview · Article · Jun 1993 · Biophysical Journal
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    ABSTRACT: The effects of poly(L-lysine) on the structural and thermotropic properties of dipalmitoylphosphatidylglycerol (DPPG) bilayers were studied with differential scanning calorimetry (DSC), X-ray diffraction and freeze-fracture electron microscopy. For thermal behavior, in the DPPG/poly(L-lysine) system the main transition temperature rises to 45.7 degrees C and the pretransition disappears in opposition to pure DPPG vesicles. An additional transition appears approximately at 36 degrees C for the DPPG/poly(L-lysine) system after incubation at 4 degrees C for two months. The incubated sample gives a X-ray diffraction pattern having several additional reflections in the range of 0.2-0.9 nm at 15 degrees C. These results suggest that even in the presence of poly(L-lysine) the DPPG bilayers form the subgel (Lc) phase after the long incubation at a low temperature. The X-ray diffraction measurements indicate that the structure of the Lc phase for DPPG/poly(L-lysine) system is different from that of pure DPPG bilayers. On the other hand, in the gel (L beta') phase, the wide-angle X-ray diffraction pattern suggests that the presence of poly(L-lysine) hardly affects the packing of hydrocarbon chains in the DPPG bilayers. The small-angle X-ray diffraction and freeze-fracture electron microscopy exhibit that the DPPG/poly(L-lysine) system forms a tightly packed multilamellar structure in which the poly(L-lysine) is intercalated between the subsequent DPPG bilayers.
    No preview · Article · Oct 1992 · Biochimica et Biophysica Acta
  • J. Hatta · M. Okada · S. Matuoka · H. Yao
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    ABSTRACT: Using an ac calorimetric method, detailed behaviour of the heat capacity in dipalmitoyl-phosphatidylcholine-cholesterol system was studied in the cholesterol concentration less than 5 mol%. It was revealed that the heat capacity near the main transition was composed of at least four anomalies, i.e., multipeak took place in the heat capacity. This fact indicates that a simple theory explaining coexistence of two phases in two component systems does not work in the multipeak region. Then, relation between the multipeak heat capacity and the change of the ripple structure with the cholesterol concentration should be taken into account, when we consider thermodynamical behaviour of the systems.
    No preview · Article · Aug 1992 · Journal of Thermal Analysis
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    ABSTRACT: Structure of dipalmitoylphosphatidic acid (DPPA) bilayers in the presence of poly(L-lysine) is proposed from the results of X-ray diffraction obtained by a storage phosphor detector with a high resolution called an imaging plate. The small-angle X-ray diffraction pattern exhibits that DPPA/poly(L-lysine) complex forms a highly ordered multilamellar structure. The electron density profile of the DPPA/poly(L-lysine) complex draws that only one poly(L-lysine) layer is intercalated between the neighboring DPPA bilayers. The wide-angle X-ray diffraction pattern suggests that the presence of poly(L-lysine) hardly affects the nature of hydrocarbon chain packing in the DPPA bilayers. The X-ray reflection from the DPPA/poly(L-lysine) complex indicates that the poly(L-lysine) molecules adopt a beta-sheet conformation on the surface of the DPPA bilayers. The both surface areas occupied by a headgroup of the DPPA and by a lysine residue in poly(L-lysine) are estimated from the observed spacings. The number ratio of lysine residues to DPPA headgroups per unit area is greater than unity. Therefore, one DPPA headgroup interacts with more than one lysine residue electrostatically, i.e., the electric charge distributions in both the surface of a DPPA bilayer and the poly(L-lysine) beta-sheet are incommensurate.
    No preview · Article · Dec 1991 · Biochimica et Biophysica Acta
  • Source
    Haruhiko Yao · Sinzi Matuoka · Boris Tenchov · Ichiro Hatta
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    ABSTRACT: Fully hydrated dipalmitoylphosphatidylcholine (DPPC) undergoes liquid crystalline to metastable P(beta), phase transition in cooling. A small angle x-ray scattering study has been performed for obtaining further evidence about the structure of this phase. From a high-resolution observation of x-ray diffraction profiles, a distinct multipeak pattern has become obvious. Among them the (01) reflection in the secondary ripple structure is identified clearly. There are peaks assigned straightforwardly to (10) and (20) reflections in the primary ripple structure and peaks assigned to (10) and (20) reflections in the secondary ripple structure. Therefore the multipeak pattern is due to superposition of the reflections cause by the primary and secondary ripple structures. The lattice parameters are estimated as follows: for the primary ripple structure a = 7.09 nm, b = 13.64 nm, and gamma = 95 degrees , and for the secondary ripple structure a = 8.2 nm, b = 26.6 nm, and gamma = 90 degrees . The lattice parameters thus obtained for the secondary ripple structure are not conclusive, however. The hydrocarbon chains in the primary ripple structure have been reported as being tilted against the bilayer plane and, on the other hand, the hydrocarbon chains in the secondary ripple structure are likely to be perpendicular to the bilayer plane. This fact seems to be related to a sequential mechanism of phase transitions. On heating from the L(beta), phase where the hydrocarbon chains are tilted the primary ripple structure having tilted hydrocarbon chains takes place and on cooling from the L(alpha) phase where the hydrocarbon chains are not tilted the secondary ripple structure with untilted chains tends to be stabilized. It appears that the truly metastable ripple phase is expressed by the second ripple structure although in the course of the actual cooling transition both the secondary and primary ripple structures form and coexist.
    Full-text · Article · Feb 1991 · Biophysical Journal
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    ABSTRACT: The ripple structure of 1,2-dimyristoyl-L-phosphatidylcholine (DMPC) multibilayer containing excess water (60 wt%) was studied by synchrotron X-ray small-angle diffraction. The (0,1) spacing which corresponds to the ripple repeat distance depends on temperature: At 13 degrees C the (0,1) spacing is 14.15 nm, the spacing decreases at higher temperatures and reaches 12.1 nm at 23.5 degrees C, just below the main transition temperature. The spacing is in good agreement between heating process and cooling process except for the supercooling region. The result suggests that the rearrangement of the ripple structure takes place during temperature change successively. The Landau-de Gennes free energy equation explains well the temperature dependence of the ripple repeat distance.
    No preview · Article · Nov 1990 · Biochimica et Biophysica Acta
  • Sinzi Matuoka · Ichiro Hatta

    No preview · Article · Jan 1990
  • Sinzi Matuoka · Ichiro Hatta
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    ABSTRACT: Synchrotron X-ray scattering experiments make it possible to investigate dynamic structural changes in biological materials. This extremely high intense X-ray source is applied to the study of hydrated phospholipid multilamellar vesicles which undergo phase transitions. Time-resolved X-ray scattering experiments after temperature jump make clear the kinetics of the phase transitions. Real time X-ray scattering experiments at low temperature scan rates are the powerful methods for observing transient structural changes during the phase transitions.
    No preview · Article · Jan 1990
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    ABSTRACT: The regularity of the bilayer structure was compared between dipalmitoylphosphatidic acid (DPPA) Langmuir-Blodgett (LB) films and 'oriented multilayers' of DPPA, using X-ray diffraction and electron spectroscopy for chemical analysis (ESCA). The angular variation of the (001) Bragg spot due to the irregularity of the lamellar repeat was remarkable in the system of oriented multilayers. In contrast, the spot of DPPA LB films exhibited only a slight angular variation, suggesting a regular structure of this film. The take-off angle dependence of the phosphorus: carbon ratio obtained by ESCA indicates that the regular layered structure in DPPA LB film is maintained after 49 layers are deposited.
    No preview · Article · Nov 1989 · Thin Solid Films
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    ABSTRACT: Primary photochemical behaviors of cattle rhodopsin analogues (Rh5 and Rh7) having cyclopenta- and cycloheptatrienylidene 11-cis-locked retinals (Ret5 and Ret7, respectively) were studied by excitation with a picosecond laser pulse (wavelength 532 nm; duration 21 ps). Picosecond absorption and fluorescence measurements of Rh5 showed formation of only a long-lived excited singlet state (tau l/e = 85 ps). The excited state of the retinal analogue having a five-membered ring was stabilized in protein (Rh5) more than in solvent (protonated Schiff base of Ret5; PSB5). Excitation of Rh7 produced two ground-state photoproducts, Rh7 (580) and Rh7 (630). According to the analysis of photon density dependency, Rh7 (580) was a single-photon product of Rh7, while Rh7 (630) was the photoproduct of Rh7 (580). Fluorescence emitted from a seven-membered ring system like Rh7 or a protonated Schiff base of Ret7 (PSB7) was weaker than that in a corresponding five-membered ring system, especially in protein (Rh7). The difference in photoreaction between Rh5 and Rh7 may originate from the difference in fixation of the 11-cis form. On the basis of the spectral and kinetic similarities between Rh7 (580) and photorhodopsin, a precursor of bathorhodopsin, it was proposed that both have twisted all-trans chromophores in the way of the isomerization. The protein moiety of rhodopsin which fixes the chromophore at both ends seems to accelerate the rotation of the C11-C12 double bond and to prevent it from going through relaxation processes other than the isomerization. This may be a plausible reason why rhodopsin has a large quantum yield (0.67).
    No preview · Article · Aug 1989 · Biochemistry
  • H Kandori · S Matuoka · Y Shichida · T Yoshizawa
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    ABSTRACT: The primary photochemical reactions of cattle rhodopsin suspended in H2O or D2O were compared between excitation with both a weak and an intense picosecond laser pulse (wavelength, 532 nm; duration, 25 ps) at room temperature. The time-dependent change of absorbance at about 575 nm demonstrated that photohodopsin, a precursor of bathorhodopsin, was produced immediately after the excitation with a weak picosecond laser pulse. It decayed to bathorhodopsin with a time constant of 45 ps which is close to the value reported previously [Shichida et al., (1984) Photobiochem. Photobiophys., 7, 221-228]. No deuterium effect was observed in this process. Excitation with an intense laser pulse induced instantaneous increase of the absorbance at about 575 nm and remained at almost constant level on the picosecond time scale, which was in good agreement with the pioneering work [Busch et al., (1972) Proc. Natl. Acad. Sci., USA, 69, 2802-2806]. No deuterium effect was observed in this photochemical process.
    No preview · Article · Mar 1989 · Photochemistry and Photobiology
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    ABSTRACT: Abstract The primary photochemical reactions of cattle rhodopsin suspended in H2O or D2O were compared between excitation with both a weak and an intense picosecond laser pulse (wavelength, 532 nm; duration, 25 ps) at room temperature. The time-dependent change of bsorbance at about 575 nm demonstrated that photorhodopsin, a precursor of bathorhodopsin, was produced immediately after the excitation with a weak picosecond laser pulse. It decayed to bathorhodopsin with a time constant of 45 ps which is close to the value reported previously [Shichida et al., (1984) Photobiochem. Photobiophys., 7, 221–228]. No deuterium effect was observed in this process. Excitation with an intense laser pulse induced instantaneous increase of the absorbance at about 575 nm and remained at almost constant level on the picosecond time scale, which was in good agreement with the pioneering work [Busch et al., (1972) Proc. Natl. Acad. Sci., USA, 69, 2802–2806], No deuterium effect was observed in this photochemical process.
    No preview · Article · Jan 1989 · Photochemistry and Photobiology
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    ABSTRACT: — The quantum yield of bleaching of isorhodopsin relative to that of rhodopsin was measured by irradiation of both pigments with a steady light source or a picosecond laser pulse. The each pigment was prepared by incubation of 11-cis or 9-cis retinal with opsin, respectively. The ratio of isorhodopsin to rhodopsin in the quantum yield was estimated to be 0.37 using irradiation with a steady light, while with a weak picosecond laser pulse (excitation photon density: below 20 μ.J/1.8 mmφ), it was estimated to be 0.39. Both values are in good agreement with each other. On the other hand, excitation with a strong picosecond laser pulse (above 20 μ.J/1.8 mmφ) produced a larger ratio than 0.39, indicating that saturation effects can be easily observed by irradiation with strong picosecond laser pulses.
    No preview · Article · Aug 1988 · Photochemistry and Photobiology
  • Toˆru Yoshizawa · Yoshinori Shichida · Sinzi Matuoka
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    ABSTRACT: The primary photochemical processes of rhodopsin studied by low temperature spectrophotometry and picosecond laser spectroscopy in our group was summarized. Low temperature spectroscopic experiments demonstrated that the retinylidene chromophores of hypso- and bathorhodopsins are in a twisted all-trans forms. Excitation of rhodopsin with 532 nm laser pulse (width: 25 psec) yielded a new bathochromic photoproduct "photorhodopsin"; its spectrum was located at longer wavelengths than that of bathorhodopsin. Photorhodopsin decays to bathorhodopsin with time constants of about 200 psec in squid and 40 psec in cattle. Squid and octopus hypsorhodopsins were produced within 25 psec by high energy pulse, but not by low energy pulse. Thus hypsorhodopsin is produced by two photon reactions (sequential two photochemical reactions) and decayed to bathorhodopsin with time constant of 125 psec.
    No preview · Article · Dec 1984 · Vision Research
  • Sinzi Matuoka · Yoshinori Shichida · Tôru Yoshizawa
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    ABSTRACT: Excitation of squid rhodopsin with a single laser pulse (532 nm, 25 ps) at 18 degrees C yielded photorhodopsin, a precursor of bathorhodopsin. In the linear region, no relation between amount of photorhodopsin and excitation-energy hypsorhodopsin was detected, while in a photon saturation region this was observed. The time constant of hypsorhodopsin to bathorhodopsin decay was about 125 ps. Dependencies of formation of photorhodopsin and hypsorhodopsin on the excitation energy suggest that hypsorhodopsins of squid and octopus are formed by a two-photon reaction. No cattle hypsorhodopsin was detected in our experimental conditions.
    No preview · Article · May 1984 · Biochimica et Biophysica Acta

Publication Stats

495 Citations
58.76 Total Impact Points

Institutions

  • 1992-2003
    • Sapporo Medical University
      • School of Medicine
      Sapporo, Hokkaidō, Japan
  • 1989-1994
    • Nagoya University
      • Graduate School of Engineering
      Nagoya, Aichi, Japan
  • 1993
    • Kwansei Gakuin University
      Nishinomiya, Hyōgo, Japan
  • 1983-1989
    • Kyoto University
      • Department of Biophysics
      Kioto, Kyōto, Japan