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1.
J Phys Ther Sci ; 35(12): 789-792, 2023 Dec.
Article in English | MEDLINE | ID: mdl-38075514

ABSTRACT

[Purpose] This study aimed to investigate the contribution of hip muscle torque to figure-of-eight walk (F8W) test in healthy young males. [Participants and Methods] Twenty healthy young males (40 limbs; mean age, 21.7 ± 0.6 years) participated. We measured the maximum F8W speed and steps. The hip muscle strengths (MS) of the flexor, extensor, abductor, and adductor muscles as well as the internal and external rotators (ER) were measured using a handheld belt-stabilized dynamometer. The hip muscle torque to weight-bearing index (WBI) is expressed as the measured MS divided by the lower thigh or shin length and body weight. [Results] F8W-time and F8W-rate were relevant to the ER-WBI (F8W time: ß=-0.330; F8W rate: ß=0.369). [Conclusion] This study's findings suggest that hip ER strength contributes to F8W in healthy young males.

2.
Biosci Biotechnol Biochem ; 86(5): 665-671, 2022 Apr 21.
Article in English | MEDLINE | ID: mdl-35234829

ABSTRACT

Mango (Mangifera indica L.) kernels are usually discarded as waste, but they contain many pharmacological properties and bioactivities. In this study, we isolated antiobesity agents from mango kernels that inhibit intracellular lipid formation in 3T3-L1 adipocytes. Two phenolic acids, ethyl gallate and ethyl digallate, and 2 tannin acids, 1,2,3,4,6-penta-O-galloyl-ß-d-glucose (PGG) and 3-O-digalloyl-1,2,4,6-tetra-O-ß-d-glucose (HGG), were identified from mango kernels and were found to be suppressed lipid accumulation as evidenced by Oil Red O staining. Furthermore, ethyl digallate, PGG, and HGG significantly downregulated the mRNA expression of adipogenic transcription factors such as C/EBPα and PPARγ. However, ethyl gallate did not affect the expression of these transcription factors. Our findings reveal the presence of antiobesity compounds in mango kernels, implying its therapeutic role against obesity.


Subject(s)
Mangifera , 3T3-L1 Cells , Adipogenesis , Animals , CCAAT-Enhancer-Binding Protein-alpha/metabolism , Lipid Metabolism , Lipids , Mice , PPAR gamma/metabolism , Plant Extracts/pharmacology , Tannins/metabolism , Tannins/pharmacology
3.
Inorg Chem ; 59(16): 11273-11286, 2020 Aug 17.
Article in English | MEDLINE | ID: mdl-32799483

ABSTRACT

Photosubstitution reactions of ruthenium complexes with pyrazole ligands, cis-[Ru(bpy)2(pzH)2]2+ (1a), cis-[Ru(bpy)2(pz)(pzH)]+ (1b), and cis-[Ru(bpy)2(pz)2]0 (1c) (pzH = pyrazole, bpy = 2,2'-bipyridine), were investigated. Dicationic complex 1a was deprotonated to 1b using moderate base (pKa = 15.2, MeCN), while the second deprotonation to give 1c required more severe conditions (pKa = 26.9). Monocationic complex 1b possessed an N-H···N-type intramolecular hydrogen bond between the pyrazole and pyrazolate ligands, as corroborated by the solid-state crystal structure. The photosubstitution quantum yield of 1a (Φ = 0.26) was comparable to that of cis-[Ru(bpy)2(pyridine)2]2+ (Φ = 0.24) in acetonitrile solution. In contrast, the photodissociation of a pzH ligand was strongly suppressed by the deprotonation of a pyrazole ligand N-H group. In the presence of 10 000 equiv of 4,4'-dimethylaminopyridine, the quantum yield dropped to ∼2 × 10-6 in acetonitrile. The photosubstitution quantum yield of 1b was even smaller than that of neutral complex 1c, although 1c had a smaller HOMO-LUMO energy gap than monocationic complex 1b. The small quantum yield of 1b was attributed to intramolecular hydrogen bonding between pyrazole and pyrazolate ligands. The apparent rate constants for the photosubstitution of 1b were highly solvent-dependent. The photosubstitution of 1b was suppressed in aprotic solvents, while the reaction was accelerated by 2 orders of magnitude in protic solvents with strong proton donor abilities.

4.
J Pharm Pharm Sci ; 22(1): 457-465, 2019.
Article in English | MEDLINE | ID: mdl-31539322

ABSTRACT

PURPOSE: Bile duct ligation (BDL) in experimental animals is widely used as an animal model of liver cholestasis and fibrosis. The transcriptional process and plasma membrane localization of transporters are regulated by nuclear receptors and scaffold proteins, respectively. However, the detailed changes of these factors in the livers of BDL rats remain unclear. To clarify the effects of BDL on the levels of transporters and metabolizing enzymes, nuclear receptors, and scaffold proteins, we investigated changes in mRNA and protein levels of livers from BDL rats. METHODS: Membrane proteins and microsomes were prepared from rats with BDL. The mRNA levels of transporters and nuclear receptors in livers of control and BDL rats were examined by real-time reverse transcription polymerase chain reaction. The protein levels of transporters, metabolizing enzymes and scaffold proteins in membrane proteins and microsomes were determined by liquid chromatography-tandem mass spectrometry-based targeted proteomics. RESULTS: Mdr1a mRNA was significantly decreased at 1 and 2 weeks of BDL. The mRNA levels of MRP2 were significantly decreased. The mRNA levels of nuclear receptors were significantly decreased in livers of 1-week BDL rats. The protein levels of P-gp were significantly increased by BDL. Regarding scaffold proteins, the protein levels of ezrin, moesin and EBP50 were significantly decreased at 2 weeks of BDL. The protein levels of radixin were significantly increased at 1 week of BDL. In 1-week BDL rats, the protein levels of metabolizing enzymes such as CYP and UGT were significantly decreased. CONCLUSIONS: This study reports the comprehensive changes of transporters, metabolizing enzymes, nuclear receptors, and ezrin/radixin/moesin proteins in the livers of BDL rats. The expression levels of nuclear receptors and radixin that regulate the transcription and localization of CYP and/or transporters were decreased by BDL.


Subject(s)
Bile Ducts/metabolism , Cytochrome P-450 Enzyme System/metabolism , Glycosyltransferases/metabolism , Liver/metabolism , Membrane Transport Proteins/metabolism , Receptors, Cytoplasmic and Nuclear/metabolism , Animals , Bile Ducts/enzymology , Liver/enzymology , Male , Membrane Transport Proteins/genetics , RNA, Messenger/genetics , RNA, Messenger/metabolism , Rats , Rats, Wistar , Receptors, Cytoplasmic and Nuclear/genetics
5.
Dig Endosc ; 26(1): 113-6, 2014 Jan.
Article in English | MEDLINE | ID: mdl-23363231

ABSTRACT

Plexiform schwannoma is a benign peripheral nerve sheath tumor composed exclusively of Schwann cells arranged in a plexiform pattern. Most plexiform schwannomas are skin tumors and visceral localization is very rare. To our knowledge, there are six cases localized in visceral organs. We describe herein the first known case of plexiform schwannoma of the rectum resected by endoscopic submucosal dissection (ESD). A 77-year-old woman presented with a short history of anal pain. Sigmoidoscopy demonstrated a submucosal tumor, 20 mm in diameter, of the rectum below the peritoneal reflection (Rb). We resected the tumorby ESD. The tumor consisted of multiple white nodules in the submucosal layer. Microscopic examination revealed that the tumor was composed mainly of Antoni A tissue, compatible with conventional schwannoma. Immunohistochemically, the tumor was positive for S-100, and negative for α-smooth muscle actin, c-kit and CD-34. No evidence of recurrence has been found in 2 years of follow up.


Subject(s)
Neurilemmoma/pathology , Rectal Neoplasms/pathology , Actins/metabolism , Aged , Dissection/methods , Endoscopy, Digestive System , Female , Humans , Immunohistochemistry , Neurilemmoma/metabolism , Neurilemmoma/surgery , Rectal Neoplasms/metabolism , Rectal Neoplasms/surgery , S100 Proteins/metabolism , Sigmoidoscopy
6.
Nihon Shokakibyo Gakkai Zasshi ; 108(4): 633-9, 2011 Apr.
Article in Japanese | MEDLINE | ID: mdl-21467771

ABSTRACT

We report a case of 72-year-old man found to have a primary malignant melanoma in the jejunum. The patient was noted to be anemic and had lower abdominal pain on his visit to the Department of Gastroenterology. However, an upper gastrointestinal series and colonofiberscopic examination revealed no abnormalities. After clinical examinations, the radiological workup, which included CT, X-ray of the small intestine and single-balloon enteroscopy, revealed an intraluminal polypoid tumor, with a patchy light gray and black pattern. Pre-operative biopsy specimens revealed a malignant melanoma. Segmental intestinal resection with regional lymph node dissection was performed. The tumor size was 7.0×9.5×5.8cm. Nodal metastasis was seen only in the mesenteric node draining from the tumor-bearing intestinal segment (stage IIIa). Adjuvant chemotherapy with dacarbazine, nimustine hydrochloride and vincristine sulfate was performed, and the patient was able to recover his level of activity of daily living for 6 months.


Subject(s)
Biopsy , Endoscopy, Gastrointestinal , Jejunal Neoplasms/pathology , Melanoma/pathology , Aged , Humans , Male , Preoperative Care
7.
RSC Adv ; 9(4): 2002-2010, 2019 Jan 14.
Article in English | MEDLINE | ID: mdl-35516112

ABSTRACT

A series of ruthenium complexes with chloro-substituted bidentate ligands, proximal-[Ru(tpy)(Cl-pyqu)L] n+ [n = 1 for L = Cl, and n = 2 for L = OH2, tpy = 2,2';6',2''-terpyridine, pyqu = 2-(2'-pyridyl)quinoline] were synthesized and their reversible photoisomerizations and thermal isomerizations were investigated experimentally. The crystal structures of the complexes indicated that introduction of a chloro substituent at the 4- or 4'-position of the pyqu ligand did not change the structure around the metal center from that of the non-substituted complex, proximal-[Ru(tpy)(pyqu)L] n+. In contrast, the 6'-substituted complexes had sterically hindered environments around the metal center. The ruthenium aqua complexes showed reversible photoisomerization between the proximal and distal isomers. The quantum yield for photoisomerization of the 6'-substituted ruthenium aqua complex was almost twice as large as those of the other derivatives. This is explained by weakening of the ligand field on the ruthenium center by introduction of a chloro substituent at the 6'-position. Thermal back isomerization from the distal isomer to the proximal one was observed for the 6'-substituted complex, but such reactions were not observed for the other derivatives. The steric hindrance in the 6'-substituted aqua complex enhanced both thermal isomerization and photoisomerization.

8.
Intern Med ; 42(9): 788-92, 2003 Sep.
Article in English | MEDLINE | ID: mdl-14518663

ABSTRACT

OBJECTIVE: The aim of this study was to investigate whether or not the purine degradation in the skeletal muscle during forearm exercise is augmented in patients with diabetes mellitus (DM). METHODS: We used the semi-ischemic forearm test to examine the release of lactate (deltaLAC), ammonia (deltaAmm) and hypoxanthine (deltaHX) before exercise, 0, 4, 10, and 60 minutes after exercise in eleven diabetic patients and seven normal controls. RESULTS: The sum of the increased HX (DM vs Controls: 26.1 +/- 21.2 vs 7.8 +/- 5.9 micromol/L, p < 0.05) was greater in diabetic patients. When patients were divided into the excessive response group (n = 7) and normal response group (n = 4), the maximum increments in deltaHX and deltaAmm in the excessive response group (16.8 +/- 3.2 micromol/l and 122 +/- 60 micromol/l) were greater (p < 0.05) than those in the control group (3.6 +/- 3.0 micromol/l and 32 +/- 34 micromol/l and the normal response group (2.9 +/- 2.9 micromol/l and 27.4 +/- 12.7 micromol/l). DeltaLAC both in the excessive response group (5.4 +/- 1.5 mmol/l) and the normal response group (3.6 +/- 1.0 mmol/l) were higher (p < 0.05) than that of the control group (1.7 +/- 0.5 mmol/l). The prevalence of diabetic retinopathy was higher in the excessive response group than in the normal response group (75% vs. 25%). CONCLUSION: These data suggest that patients with DM, especially with microangiopathy have augmented purine degradation during the semi-ischemic forearm test. Factors responsible for the augmented purine degradation in these patients remain to be determined.


Subject(s)
Diabetes Mellitus/metabolism , Diabetic Retinopathy/metabolism , Exercise Test/methods , Ischemia/metabolism , Muscle, Skeletal/metabolism , Purines/metabolism , Adolescent , Adult , Aged , Child , Diabetes Mellitus/physiopathology , Diabetic Retinopathy/physiopathology , Female , Forearm/blood supply , Humans , Male , Middle Aged , Muscle, Skeletal/blood supply
9.
J Hum Genet ; 52(2): 117-122, 2007.
Article in English | MEDLINE | ID: mdl-17111267

ABSTRACT

Organic cation transporters (OCTs) are responsible for the hepatic and renal transport of metformin. In this study we analyzed variants of OCT1 and OCT2 genes in 33 patients (24 responders and nine non-responders) based on the hypothesis that polymorphisms in both genes contribute to large inter-patient variability in the clinical efficacy of metformin. The sequences of the 5'-flanking and coding regions of the two genes of interest were screened by single-strand conformation polymorphism (SSCP) analysis. To compare the causative factors between responders and non-responders, we performed stepwise discriminant functional analysis. Age, body mass index (BMI) and treatment with lipid-lowering agents were demonstrated as positive predictors, and two mutations in the OCT1 gene, -43T > G in intron 1 and 408Met > Val (1222A > G) in exon 7, were negative and positive predictors, respectively, for the efficacy of metformin; the predictive accuracy was 55.5% (P < 0.05). Subsequent study indicated that OCT1 mRNA levels tended to be lower in human livers with the 408Met (1222A) variant, though the differences did not reach the level of significance. In this study it is suggested that OCT1 and OCT2 gene polymorphisms have little contribution to the clinical efficacy of metformin.


Subject(s)
Diabetes Mellitus, Type 2/drug therapy , Hypoglycemic Agents/therapeutic use , Metformin/therapeutic use , Organic Cation Transport Proteins/genetics , Organic Cation Transporter 1/genetics , Polymorphism, Genetic , Adult , Aged , Diabetes Mellitus, Type 2/genetics , Female , Humans , Male , Middle Aged , Organic Cation Transport Proteins/metabolism , Organic Cation Transporter 1/metabolism , Organic Cation Transporter 2 , Polymerase Chain Reaction , Polymorphism, Single-Stranded Conformational , RNA, Messenger/metabolism
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