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1.
Skin Res Technol ; 28(3): 472-479, 2022 May.
Artículo en Inglés | MEDLINE | ID: mdl-35416349

RESUMEN

BACKGROUND: Facial massage is empirically known to be associated with morphological changes, such as improvements in facial sagging. However, quantified objective evaluations of massage-induced changes have not been performed to date. This preliminary pilot study aimed to verify the effectiveness of facial massages by using breakthrough computed tomographic technology. MATERIALS AND METHODS: Five healthy adult volunteers (three women and two men; age, 29-37 years) were enrolled, and computed tomography (CT) examinations using a 320 detectors-spiral CT system known as 320-multidetector-row CT (MDCT) were performed before and after facial massages. Each participant performed a self-massage twice daily for 2 weeks. Massage-induced changes in the cheeks and the superficial musculoaponeurotic system (SMAS) were analyzed by two radiologists on a workstation with a high-accuracy imaging analysis system. RESULTS: After facial massage, the malar top became thinner by -0.8% ± 0.45% and shifted cranially and horizontally over a distance of 3.9 ± 1.94 mm. The SMAS-height, defined as the highest vertical distance of the SMAS, increased by 2.6% ± 2.6%. The change rate in cheek thickness and SMAS-height showed a significant correlation (r = -0.63; P < 0.05). These changes were attributed to the lifting and tightening effects of facial massage. CONCLUSION: We conducted a detailed analysis of the effects of facial massages by using the breakthrough CT technology. Our results provide useful information for beauty treatments and could contribute to the collection of objective scientific evidence for facial massages.


Asunto(s)
Sistema Músculo-Aponeurótico Superficial , Adulto , Cara/diagnóstico por imagen , Femenino , Humanos , Masculino , Masaje , Proyectos Piloto , Tomografía Computarizada por Rayos X
2.
Plants (Basel) ; 10(12)2021 Dec 09.
Artículo en Inglés | MEDLINE | ID: mdl-34961180

RESUMEN

The spores of Lygodium japonicum, cultured in the dark, form a filamentous structure called protonema. Earlier studies have shown that gibberellin (GA) induces protonema elongation, along with antheridium formation, on the protonema. In this study, we have performed detailed morphological analyses to investigate the roles of multiple phytohormones in antheridium formation, protonema elongation, and prothallus formation in L. japonicum. GA4 methyl ester is a potent GA that stimulates both protonema elongation and antheridium formation. We found that these effects were inhibited by simultaneous application of abscisic acid (ABA). On the other hand, IAA (indole-3-acetic acid) promoted protonema elongation but reduced antheridium formation, while these effects were partially recovered by transferring to an IAA-free medium. An auxin biosynthesis inhibitor, PPBo (4-phenoxyphenylboronic acid), and a transport inhibitor, TIBA (2,3,5-triiodobenzoic acid), both inhibited protonema elongation and antheridium formation. L. japonicum prothalli are induced from germinating spores under continuous white light. Such development was negatively affected by PPBo, which induced smaller-sized prothalli, and TIBA, which induced aberrantly shaped prothalli. The evidence suggests that the crosstalk between these plant hormones might regulate protonema elongation and antheridium formation in L. japonicum. Furthermore, the possible involvement of auxin in the prothalli development of L. japonicum is suggested.

3.
Biophys J ; 96(3): 1210-7, 2009 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-19186155

RESUMEN

Tributyltin chloride (TBT-Cl) is an endocrine disruptor found in many animal species, and it is also known to be an inhibitor for the V-ATPases that are emerging as potential targets in the treatment of diseases such as osteoporosis and cancer. We demonstrated by using biochemical and single-molecular imaging techniques that TBT-Cl arrests an elementary step for rotary catalysis of the V(1) motor domain. In the presence of TBT-Cl, the consecutive rotation of V(1) paused for a long duration ( approximately 0.5 s), even at saturated ATP concentrations, and the pausing positions were localized at 120 degrees intervals. Analysis of both the pausing time and moving time revealed that TBT-Cl has little effect on the binding affinity for ATP, but, rather, it arrests the catalytic event(s). This is the first report to demonstrate that an inhibitor arrests an elementary step for rotary catalysis of a V-type ATP-driven rotary motor.


Asunto(s)
Disruptores Endocrinos/toxicidad , Thermus thermophilus/enzimología , Compuestos de Trialquiltina/toxicidad , ATPasas de Translocación de Protón Vacuolares/antagonistas & inhibidores , Adenosina Trifosfato/metabolismo , Biocatálisis/efectos de los fármacos , Cinética , Movimiento , Estructura Terciaria de Proteína , Rotación , ATPasas de Translocación de Protón Vacuolares/química , ATPasas de Translocación de Protón Vacuolares/metabolismo
4.
Proc Natl Acad Sci U S A ; 102(50): 17929-33, 2005 Dec 13.
Artículo en Inglés | MEDLINE | ID: mdl-16330761

RESUMEN

V(1), a water-soluble portion of vacuole-type ATPase (V-ATPase), is an ATP-driven rotary motor, similar to F(1)-ATPase. Hydrolysis of ATP is coupled to unidirectional rotation of the central rotor D and F subunits relative to the A(3)B(3) cylinder. In this study, we analyzed the rotation kinetics of V(1) in detail. At low ATP concentrations, the D subunit rotated stepwise, pausing every 120 degrees . The dwell time between steps revealed that V(1) consumes one ATP per 120 degrees step. V(1) generated torque of approximately 35 pN nm, slightly lower than the approximately 46 pN nm measured for F(1). Noticeably, the angles for both ATP cleavage and binding were apparently the same in V(1), in sharp contrast to F(1), which cleaves ATP at 80 degrees posterior to the binding of ATP. Thus, the mechanochemical cycle of V(1) has marked differences to that of F(1).


Asunto(s)
Adenosina Trifosfato/metabolismo , Proteínas Motoras Moleculares/fisiología , Rotación , Thermus thermophilus/enzimología , ATPasas de Translocación de Protón Vacuolares/fisiología , Escherichia coli , Cinética , Proteínas Motoras Moleculares/metabolismo , ATPasas de Translocación de Protón/metabolismo , ATPasas de Translocación de Protón Vacuolares/metabolismo
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