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1.
Biology (Basel) ; 10(12)2021 Dec 10.
Article in English | MEDLINE | ID: mdl-34943226

ABSTRACT

Intermuscular bones (IBs) are small spicule-like bones located in the myosepta of basal teleosts, which negatively affect the edibleness and economic value of fish. Blunt snout bream (Megalobrama amblycephala, with epineural and epipleural IBs) and tilapia (Oreochromis niloticus, without epineural and epipleural IBs) are two major aquaculture species and ideal models for studying the formation mechanisms of fish IBs. Here, we compared myosepta development between M. amblycephala and O. niloticus, based on histological analysis, transcriptome profiling, and expression analysis of bone-related genes. The histological results showed that dye condensation began to appear in the myosepta 20 days post hatching (dph) in M. amblycephala, and IBs could be clearly observed 50 dph in the myosepta, based on different staining methods. However, in O. niloticus, dye condensation was not observed in the myosepta from 10 to 60 dph. Differentially expressed genes (DEGs) at different developmental stages were screened by comparing the transcriptomes of M. amblycephala and O. niloticus, and KEGG analysis demonstrated that these DEGs were enriched in many bone-related pathways, such as focal adhesion, calcium, and Wnt signaling pathways. Quantitative PCR was performed to further compare the expression levels of some bone-related genes (scxa, scxb, runx2a, runx2b, bgp, sp7, col1a2, entpd5a, entpd5b, phex, alpl, and fgf23). All the tested genes (except for alpl) exhibited higher expression levels in M. amblycephala than in O. niloticus. A comparison of the dorsal and abdominal muscle tissues between the two species also revealed significant expression differences for most of the tested genes. The results suggest that scxa, scxb, runx2a, runx2b, entpd5a, col1a2, and bgp may play important roles in IB development. Our findings provide some insights into the molecular mechanisms of IB formation, as well as clues for further functional analysis of the identified genes to better understand the development of IBs.

2.
Biomacromolecules ; 22(11): 4501-4509, 2021 11 08.
Article in English | MEDLINE | ID: mdl-34601873

ABSTRACT

Biografting is a promising and ecofriendly approach to meet various application requirements of products. Herein, a popular green enzyme, laccase, was adopted to graft a hydrophobic phenolic compound (lauryl gallate, LG) onto chitosan (CTS). The resultant chitosan derivate (Lac/LG-CTS) was systematically analyzed by Fourier transform infrared (FTIR), grafting efficiency, scanning probe microscopy (SPM), and X-ray diffraction (XRD). This grafting technique produced a multifunctional chitosan copolymer with remarkably enhanced antioxidant property, hydrophobicity, and moisture barrier property. Furthermore, the swelling capacity and acid solubility of the copolymer film decreased significantly, although the tensile strength and elongation were slightly weakened as compared to those of native chitosan. These results suggest that the Lac/LG-CTS holds great potential as a food-packaging material, preservative agent, or edible coating material.


Subject(s)
Chitosan , Antioxidants , Catalysis , Gallic Acid/analogs & derivatives , Hydrophobic and Hydrophilic Interactions , Laccase
3.
Medicine (Baltimore) ; 95(32): e4499, 2016 Aug.
Article in English | MEDLINE | ID: mdl-27512867

ABSTRACT

OBJECTIVE: To investigate the changes of retinal nerve fiber layer (RNFL) thickness in obstructive sleep apnea syndrome (OSAS) patients. METHODS: Relevant studies were selected from 3 major literature databases (PubMed, Cochrane Library, and EMBASE) without language restriction. Main inclusion criteria is that a case-control study in which RNFL thickness was measured by a commercial available optical coherence tomography (OCT) in OSAS patients. Meta-analysis was performed using STATA 12.0 software. Efficacy estimates were evaluated by weighted mean difference with corresponding 95% confidence intervals (CIs). Primary outcome evaluations were: the average changes of RNFL thickness in total OSAS patients, subgroup analysis of RNFL thickness changes in patients of different OSAS stages, and subgroup analysis of 4-quadrant RNFL thickness changes in total OSAS patients. RESULTS: Of the initial 327 literatures, 8 case-control studies with 763 eyes of OSA patients and 474 eyes of healthy controls were included (NOS scores ≥6). For the people of total OSAS, there had an average 2.92 µm decreased RNFL thickness compared with controls (95% CI: -4.61 to -1.24, P = 0.001). For subgroup analysis of OSAS in different stages, the average changes of RNFL thickness in mild, moderate, severe, and moderate to severe OSAS were 2.05 (95% CI: -4.40 to 0.30, P = 0.088), 2.32 (95% CI: -5.04 to 0.40, P = 0.094), 4.21 (95% CI: -8.36 to -0.06, P = 0.047), and 4.02 (95% CI: -7.65 to -0.40, P = 0.03), respectively. For subgroup analysis of 4-quadrant, the average changes of RNFL thickness in Superior, Nasal, Inferior, and Temporal quadrant were 2.43 (95% CI: -4.28 to -0.57, P = 0.01), 1.41 (95% CI: -3.33 to 0.51, P = 0.151), 3.75 (95% CI: -6.92 to -0.59, P = 0.02), and 0.98 (95% CI: -2.49 to 0.53, P = 0.203), respectively. CONCLUSION: Our study suggests that RNFL thickness in OSAS patients is much thinner than healthy population, especially in superior and inferior quadrant. The impact of OSAS disease on RNFL and visual function should be taken seriously in the further study.


Subject(s)
Retinal Neurons/pathology , Sleep Apnea, Obstructive/pathology , Case-Control Studies , Humans , Middle Aged , Tomography, Optical Coherence
4.
Biochem Biophys Res Commun ; 457(2): 187-93, 2015 Feb 06.
Article in English | MEDLINE | ID: mdl-25545058

ABSTRACT

Oridonin is an orally available drug isolated from Traditional Chinese Medicine. Previous studies with oridonin have demonstrated broad-spectrum anticancer activity in a variety of cancer types. However, the effect of oridonin in uveal melanoma has not been addressed. In this study, we aimed to investigate whether oridonin elicited anticancer activity and its underlying mechanism in human uveal melanoma cells. We demonstrated that oridonin potently reduced cell viability, induced apoptosis and inhibited clonogenic survival and growth with single digit micromolar concentrations in uveal melanoma OCM-1 and MUM2B cell lines. We found that oridonin markedly increased the expression of proapoptotic Bcl-2 family protein Bim in uveal melanoma cells, and knockdown Bim by small interfering RNA significantly attenuated oridonin-induced cell death, indicating an essential role of Bim in oridonin-mediated anticancer activity. Additionally, we observed that oridonin suppressed Fatty Acid Synthase (FAS) expression in uveal melanoma cells, and enforced FAS expression by insulin partially rescued the cells from oridonin-induced apoptosis, showing that inhibition of FAS also contributed to oridonin-mediated apoptosis. Taken together, we reported that oridonin displays potent anticancer effect against uveal melanoma cells through upregulation of Bim and inhibition of FAS. Since oridonin is a popular anticancer agent, our study therefore may have translational implication on the management of patients with uveal melanoma.


Subject(s)
Apoptosis/drug effects , Diterpenes, Kaurane/pharmacology , Down-Regulation/drug effects , Fatty Acid Synthases/metabolism , Melanoma/enzymology , Melanoma/pathology , Up-Regulation/drug effects , Uveal Neoplasms/enzymology , Uveal Neoplasms/pathology , Antineoplastic Agents/pharmacology , Apoptosis Regulatory Proteins , Bcl-2-Like Protein 11 , Caspases/metabolism , Cell Line, Tumor , Cell Survival/drug effects , Humans , Membrane Proteins , Proto-Oncogene Proteins , Tumor Stem Cell Assay
5.
Zhonghua Nan Ke Xue ; 15(1): 20-5, 2009 Jan.
Article in Chinese | MEDLINE | ID: mdl-19288743

ABSTRACT

OBJECTIVE: To identify the specific protein in the epididymal luminal fluid that may play a role in sperm epididymal maturation or modification on the surface of spermatozoa. METHODS: We compared the differential protein components in the lumen fluids from the caput and cauda segments of the epididymis of normal rats as well as from the cauda segment of experimental left varicocele (ELV) rats by SDS-PAGE or 2D-electrophoresis. The protein spots of interest were selected for MS identification, and the target proteins further characterized by immuno-blot assay. RESULTS: MS analysis showed that one of the most prominent proteins, M(r) 22 000, was identical to the phosphatidylethanolamine-binding protein (PBP), and it was further identified as PBP by immuno-blot assay. CONCLUSION: PBPs were present in a variety of molecular forms in the epididymal luminal fluid, including the glycosylated form, and ELV markedly elevated the PBP level in the cauda luminal fluid of the rats. Thus, the association of this molecule with sperm surface modification remains an interest for future investigation.


Subject(s)
Epididymal Secretory Proteins/isolation & purification , Epididymis/metabolism , Varicocele/metabolism , Animals , Disease Models, Animal , Male , Rats
6.
Anal Biochem ; 350(2): 165-70, 2006 Mar 15.
Article in English | MEDLINE | ID: mdl-16480680

ABSTRACT

Water channel proteins, known as aquaporins, are transmembrane proteins that mediate osmotic water permeability. In a previous study, we found that acetazolamide could inhibit osmotic water transportation across Xenopus oocytes by blocking the function of aquaporin-1 (AQP1). The purpose of the current study was to confirm the effect of acetazolamide on water osmotic permeability using the human embryonic kidney 293 (HEK293) cells transfected with pEGFP/AQP1 and to investigate the interaction between acetazolamide and AQP1. The fluorescence intensity of HEK293 cells transfected with pEGFP/AQP1, which corresponds to the cell volume when the cells swell in a hyposmotic solution, was recorded under confocal laser fluorescence microscopy. The osmotic water permeability was assessed by the change in the ratio of cell fluorescence to certain cell area. Acetazolamide, at concentrations of 1 and 10muM, inhibited the osmotic water permeability in HEK293 cells transfected with pEGFP/AQP1. The direct binding between acetazolamide and AQP1 was detected by surface plasmon resonance. AQP1 was prepared from rat red blood cells and immobilized on a CM5 chip. The binding assay showed that acetazolamide could directly interact with AQP1. This study demonstrated that acetazolamide inhibited osmotic water permeability through interaction with AQP1.


Subject(s)
Acetazolamide/pharmacology , Aquaporin 1/metabolism , Cell Membrane Permeability/drug effects , Osmosis/drug effects , Water/metabolism , Animals , Cell Line , Humans , Male , Rats , Surface Plasmon Resonance , Transfection
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