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1.
Zhonghua Yu Fang Yi Xue Za Zhi ; 56(7): 990-993, 2022 Jul 06.
Article in Chinese | MEDLINE | ID: mdl-35899354

ABSTRACT

The aim of this study was to investigate the preventive effect of pancreatic duct stent on acute pancreatitis after endoscopic retrograde cholangiopancreatography. A retrospective analysis of the case data of patients who first underwent endoscopic retrograde cholangiopancreatography for choledocholithiasis in the Beijing Friendship Hospital from January 2015 to December 2019 for 5 years. According to whether the pancreatic duct stent was indwelled during the operation, they were divided into pancreatic duct stent group (147 cases) and non-indwelling pancreatic duct stent group (192 cases). The incidence of acute pancreatitis after endoscopic retrograde cholangiopancreatography was compared between the two groups according to COTTON criteria. Independent sample t test, Pearson Chi-square test (χ2) and Fisher's exact test were used to compare groups' differences. There were 2 cases of acute pancreatitis in the pancreatic duct stent group, all of which improved after 48 hours. There were 22 cases of acute pancreatitis in the non-indwelling pancreatic duct stent group, of which 20 cases improved within 48 hours, and the other 2 cases had severe pancreatitis, which improved and discharged after 30 days of treatment. There was significant difference in the incidence of acute pancreatitis between the pancreatic duct stenting group (1.4%) and the group without placement of pancreatic duct stents (11.5%) (χ²=12.905,P<0.001). In conclusion, Pancreatic duct stent may be an effective method to prevent PEP.


Subject(s)
Cholangiopancreatography, Endoscopic Retrograde , Pancreatitis , Acute Disease , Cholangiopancreatography, Endoscopic Retrograde/adverse effects , Cholangiopancreatography, Endoscopic Retrograde/methods , Humans , Pancreatic Ducts/surgery , Pancreatitis/epidemiology , Pancreatitis/etiology , Pancreatitis/prevention & control , Retrospective Studies , Stents/adverse effects
2.
Andrology ; 7(2): 220-227, 2019 03.
Article in English | MEDLINE | ID: mdl-30575326

ABSTRACT

BACKGROUND: Semenogelin 1 (SEMG1) is an important secretory protein in spermatozoa involved in the formation of a gel matrix encasing ejaculated spermatozoa. Previous studies show that the SEMG1 gene is highly expressed in spermatozoa from patients with asthenozoospermia (AZS); however, the underlying molecular mechanisms are not yet clear. OBJECTIVES: To study the molecular mechanism of high expression of SEMG1 gene and its potential roles in AZS. MATERIALS AND METHODS: Western blot and real-time PCR were used to detect the expression levels of SEMG1 protein and mRNA in the ejaculated spermatozoa from normozoospermic males and AZS patients. Bioinformatics analysis was used to predict miRNAs targeting for SEMG1 3'-untranslated region detection of the expression levels of all the candidate miRNAs in ejaculatory spermatozoa in AZS patients or normozoospermic volunteers. Luciferase reporter assays were performed to confirm it can directly bind to SEMG1. Correlation of miR-525-3p and SEMG1 mRNA expression with clinical sperm parameters were also analyzed. Finally, we conducted a follow-up study of reproductive history about all the subjects. RESULTS: SEMG1 mRNA and protein level were significantly higher in AZS patients compared to that in normozoospermic volunteers (p < 0.001). Subsequently, microRNA-525-3p (miR-525-3p) which was predicted as a candidate regulator of SEMG1 was found lower expressed in ejaculatory spermatozoa in AZS patients (p = 0.0074). Luciferase experiment revealed that microRNA-525-3p could directly target SEMG1 3'-untranslated region and suppress its expression. Importantly, our retrospective follow-up study showed that both low miR-525-3p expression and high SEMG1 expression level was significantly associated with low progressive sperm motility, abnormal sperm morphology, and infertility. DISCUSSION AND CONCLUSION: The elevated expression of SEMG1 and reduced expression of miR-525-3p are associated with AZS and male infertility. Our study provides a potential therapeutic target for the treatment of male infertility or for male contraception.


Subject(s)
Asthenozoospermia/genetics , Asthenozoospermia/metabolism , MicroRNAs/biosynthesis , Seminal Vesicle Secretory Proteins/biosynthesis , Spermatozoa/metabolism , Adult , Gene Expression Regulation/genetics , Humans , Male , MicroRNAs/genetics , Seminal Vesicle Secretory Proteins/genetics
3.
Andrology ; 5(5): 1007-1015, 2017 Sep.
Article in English | MEDLINE | ID: mdl-28914500

ABSTRACT

Exosomes are membranous nanovesicles of endocytic origin that carry and transfer regulatory bioactive molecules and mediate intercellular communication between cells and tissues. Although seminal exosomes have been identified in human seminal plasma, their exact composition and possible physiologic function remain unknown. The objective of this study was to perform a comprehensive proteomics analysis of exosomes derived from human seminal plasma. Seminal exosomes were isolated and purified from 12 healthy donors using a 30% sucrose cushion-based exosome-isolation protocol, followed by characterization by western blot, transmission electron microscopy, and nanoparticle tracking analysis before performing extensive liquid chromatography tandem mass spectrometry proteomics analysis. The identified proteins were analyzed by bioinformatics analysis, and seminal exosomes-associated proteins were selectively validated by western blot. A total of 1474 proteins were identified in all seminal exosomes samples, with Gene Ontology analysis demonstrating that these identified seminal exosomes-associated proteins were mostly linked to 'exosomes,' 'cytoplasm,' and 'cytosol.' Bioinformatics analysis indicated that these proteins were mainly involved in biologic processes, including metabolism, energy pathways, protein metabolism, cell growth and maintenance, and transport. Of these identified proteins, PHGDH, LGALS3BP, SEMG1, ACTB, GAPDH, and the exosomal-marker protein ALIX were validated by western blot. This study provided a more comprehensive description of the seminal exosomes proteome and could also be a resource for further screening of biomarkers and comparative proteomics studies, including those associated with male infertility and prostate cancer.


Subject(s)
Proteome , Semen/metabolism , Adult , Chromatography, High Pressure Liquid , Chromatography, Liquid , Databases, Protein , Exosomes/metabolism , Humans , Male , Semen Analysis , Tandem Mass Spectrometry
4.
J Mater Chem B ; 3(46): 9001-9010, 2015 Dec 14.
Article in English | MEDLINE | ID: mdl-32263031

ABSTRACT

Bacterial cellulose (BC) and hydroxyapatite (HA) possess unique structures and excellent biocompatibility. Considerable work has been performed to develop composites that promote bone repair. However, the use of BC/HA composites is limited because the lack of corresponding enzymes makes them non-degradable in vivo. In the present study, C6-carboxylated bacterial cellulose (TBC) was prepared in a bromide-free system. Several composite methods of TBC and HA are compared, including in situ formation, physical mixing and biomineralization. Composite sponges prepared by different methods were characterized by tensile testing, X-ray diffraction, Fourier transform infrared spectroscopy, scanning electron microscopy and in vivo degradation. The structural anisotropy of various sponges was analyzed to quantitatively evaluate their microstructure. The results suggest that the interaction between HA and TBC nanofibers has a large influence on microstructure and macroscopic properties. Moreover, the structural anisotropy and the speed of granulation ingrowth were strongly interdependent. This improved understanding of slowly degrading BC-based materials suggests that modified cellulose-based materials can be made degradable by altering their microstructure.

5.
Inorg Chem ; 39(12): 2488-92, 2000 Jun 12.
Article in English | MEDLINE | ID: mdl-11196999

ABSTRACT

The new heteronuclear iminodiacetic acid (H2L) complexes [LnCu6(mu 3-OH)3(HL)2(L)4](ClO4)(2).25H2O with Ln = La (1) and Tb (2) have been prepared in aqueous solution and characterized by single-crystal X-ray diffraction to be isomorphous (crystallographic data for 1 and 2: hexagonal, P63/m; a = b = 12.6425(14) A, c = 24.541(5) A, Z = 2 (1); a = b = 12.5802(9) A, c = 24.285(4) A, Z = 2 (2)). Ln3+ was found to be located in the center of the trigonal prismatic cage formed by six Cu2+ ions, with a tricapped trigonal prismatic coordination environment of nine O atoms. The magnetic properties of complexes 1 and 2 have been studied. The results indicate the presence of ferromagnetic couplings between Tb3+ and Cu2+ in compound 2.

6.
Talanta ; 40(5): 637-40, 1993 May.
Article in English | MEDLINE | ID: mdl-18965677

ABSTRACT

A new spectrophotometric determination method of hexavalent chromium in waste water and plating baths is described based on the oxidation of beryllon III by chromium(VI) in 0.02M sulphuric acid medium. The decrease in the absorbance of beryllon III was measured at 482 nm with an apparent molar absorptivity of 5.15 x 10(4)1.mole(-1).cm(-1). Beer's law was obeyed for chromium(VI) over the range 0-25 mug/25 ml. After the oxidation of Cr(III) to Cr(VI) by ammonium persulphate, total chromium can be determined. Therefore, chromium(III) can be calculated by subtracting chromium(VI) from total chromium. The detection limit is 0.015 and 0.020 mug/25 ml for chromium(VI) and total chromium, respectively. A sensitive spectrophotometric method for trace Cr(III) and Cr(VI) in waste water and plating baths was developed with good precision and accuracy. The reaction is also discussed.

7.
Biochemistry ; 27(19): 7361-5, 1988 Sep 20.
Article in English | MEDLINE | ID: mdl-3207682

ABSTRACT

Several representative branched-chain analogues of distearin (DS) were synthesized and tested for their abilities to activate protein kinase C (PKC) and to compete for the binding of [3H]phorbol 12,13-dibutyrate (PDBu) to the enzyme. Substitutions of stearoyl moieties at sn-1 and sn-2 with 8-methylstearate decreased activities on these parameters, relative to those of the parental diacylglycerol DS, a weak PKC activator. Substitutions with 8-butyl, 4-butyl, or 8-phenyl derivatives, on the other hand, increased activities of the resulting analogues to levels comparable to those seen for diolein (DO), a diacylglycerol prototype shown to be a potent PKC activator. Kinetic analysis indicated that 8-methyldistearin (8-MeDS) acted by decreasing, whereas 8-butyldistearin (8-BuDS) and 8-phenyldistearin (8-PhDS) acted by increasing, the affinities of PKC for phosphatidylserine (PS, a phospholipid cofactor) and Ca2+ compared to the values seen in the absence or presence of DS. The stimulatory effect of 8-BuDS and 8-PhDS on PKC, as DO, was additive to that of 1,2-(8-butyl)distearoylphosphatidylcholine [1,2(8-Bu)DSPC] and, moreover, they abolished the marked inhibition of the enzyme activity caused by high concentrations of 1,2(8-Bu)DSPC. The present findings demonstrated a structure-activity relationship of the branched-chain DS analogues in the regulation of PKC, perhaps related to their abilities to specifically modify interactions of PKC with PS and/or Ca2+ critically involved in enzyme activation/inactivation.


Subject(s)
Diglycerides/pharmacology , Glycerides/pharmacology , Protein Kinase C/metabolism , Binding, Competitive , Calcium/pharmacology , Diglycerides/metabolism , Enzyme Activation/drug effects , Kinetics , Micelles , Molecular Structure , Octoxynol , Phorbol 12,13-Dibutyrate/metabolism , Phosphatidylserines/pharmacology , Polyethylene Glycols , Structure-Activity Relationship
8.
Biochemistry ; 27(13): 4607-12, 1988 Jun 28.
Article in English | MEDLINE | ID: mdl-3167002

ABSTRACT

A series of distearoylphosphatidylcholine (DSPC) analogues having various branched alkyl chains were synthesized and tested for their abilities to regulate protein kinase C (PKC). The greatest improvement (about 3-fold) in the PKC inhibitory activity over that seen for the parental lipid (i.e., DSPC) was accomplished by substitution of 8-methylstearate at sn-2 and 16-methylstearate at both sn-1 and sn-2 positions of glycerol; substitutions at both sn-1 and sn-2 with 8-methylstearate, on the other hand, caused a decrease (about 4-fold) in its inhibitory activity. Introduction of butyl, phenyl, or keto functions to various positions in the fatty alkyl chain substituted at both sn-1- and sn-2 positions imparted upon the DSPC analogues an ability to potently stimulate PKC to an extent comparable to those attainable by diacylglycerol or phorbol ester; the analogues having substitution only at the sn-2 position, in comparison, had no or reduced stimulatory activity. The butyl, phenyl, and keto analogues of DSPC, as with DSPC itself and its methyl analogues, inhibited PKC at high concentrations. Kinetic analysis indicated that the methyl DSPC analogues inhibited the enzyme competitively with respect to phosphatidylserine (PS; a phospholipid cofactor) and Ca2+. The butyl analogues activated the enzyme without affecting its affinity for PS or Ca2+, indicating a mechanism different from that seen for diacylglycerol or phorbol ester. The inhibitory activity of the methyl DSPC analogues and the stimulatory activity of the butyl DSPC analogues were reduced when PKC was activated by phorbol ester. Both classes of the analogues were unable to compete for the binding of [3H]phorbol dibutyrate to PKC.(ABSTRACT TRUNCATED AT 250 WORDS)


Subject(s)
Phosphatidylcholines/pharmacology , Protein Kinase C/metabolism , Calcium Chloride/pharmacology , Enzyme Activation , Kinetics , Phorbol 12,13-Dibutyrate/metabolism , Protein Binding , Protein Kinase C/antagonists & inhibitors , Structure-Activity Relationship
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