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Biomedical subjects

Ming Jiang

Publications and source records attributed to Ming Jiang.

At least 19 recordsLinked to original sources
PubMed2026

Integrated Multi-Omics Analysis Reveals the Genetic Basis of Phenotypic Variation in Tibetan Sheep.

Body size is a key economic trait influencing the profitability of farmed animals. This study used genome-wide association studies (GWAS) to identify five single nucleotide polymorphisms (SNPs) significantly associated with body size in the Tibetan sheep population, advancing molecular breeding and providing a basis for genomic selection. These SNPs are located within five candidate genes. SNaPshot validated GWAS results, demonstrating significant correlations between candidate SNPs and body size traits in Tibetan sheep. Concurrently, hematoxylin and eosin staining, alongside muscle fiber analysis, confirmed pronounced morphological differences in muscle tissue between sheep of varying conformation. Therefore, transcriptome and proteomics were performed on the longest dorsi muscle from large and small Tibetan sheep of both sexes. The transcriptome, together with weighted gene co-expression network analysis (WGCNA), identified VEPH1 and PRKG1 as core genes regulating body characteristics in Tibetan sheep through their involvement in the PI3K-Akt signaling pathway and pathways related to fat deposition. The integrative analyses demonstrated significantly different expression of CARNS1 and CRYAB at both transcriptional and protein levels between the muscles of large- and small-sized Tibetan sheep of both sexes, suggesting their importance in body size traits by influencing muscle morphology. This study provides valuable genomic resources that advance sheep genetics research.

GWAS↗
PubMed2024

MYO5B gene mutations may promote the occurrence of very early onset inflammatory bowel disease: a case report.

BACKGROUND: With recent advances in gene sequencing technology, more than 60 genetic mutations associated with very early onset inflammatory bowel disease (VEO-IBD) have been reported. Most of the genes are associated with immune deficiencies. The Myosin 5B (MYO5B) gene is primarily involved in cell motility and material transport which is associated with congenital intractable diarrhea and cholestasis. No studies have examined the relationship between the MYO5B gene and VEO-IBD. We report a case of a child with a mutation in the MYO5B gene who was diagnosed with VEO-IBD, then we investigated the association between the MYO5B gene and VEO-IBD. CASE PRESENTATION: A 7-month-old baby girl with a chief complaint of "blood in the stool for more than 4 months and vaginal pus and blood discharge for 3 weeks" was diagnosed with VEO-IBD, and her symptoms improved after treatment with mesalazine. The whole-exome sequencing was performed with peripheral blood. Immunohistochemistry was performed on the terminal ileal tissue. Western blotting, quantitative polymerase chain reaction (Q-PCR) and immunofluorescence were performed with cultured organoid tissue from the terminal ileum. Whole-exome sequencing identified heterozygous missense of MYO5B variant of unknown significance (p. [I769N]; [T1546M]). Immunohistochemistry revealed a significant decrease in the expression of MYO5B protein in the terminal ileum of the child with MYO5B mutation; Q-PCR revealed a decrease in the mRNA levels of occludin and ZO-1 and both the mRNA levels and protein levels of MYO5B was downregulated in the patient. Immunofluorescence images showed that MYO5B gene mutation disrupted the apical delivery of transporters SGLT1, NHE3 and AQP7. CONCLUSIONS: MYO5B gene mutation leading to the downregulation of MYO5B protein may promote the occurrence of VEO-IBD by decreasing mRNA and protein levels of intestinal tight junction genes and dislocating the apical transporters.

Humans↗
PubMed2007

Hydrogen-bonded dendronized polymers and their self-assembly in solution.

Frechet-type benzyl ether dendrons of second and third generations with a carboxyl group (G2, G3) at the apex site could attach to poly(4-vinylpyridine) (PVP), forming hydrogen-bonded dendronized polymers (HB denpols) in their common solvent, chloroform. The HB denpols show unique self-assembly behavior, forming vesicles in the common solvent under ultrasonic treatment. The structure and morphology of the vesicles were characterized by dynamic light scattering (DLS), static light scattering (SLS), SEM, TEM, and AFM. The size of the vesicles decreases and the thickness of the vascular membrane increases as the molar ratio of Gx/PVP increases. The hydrogen bonding, pi-pi aromatic stacking of the dendrons, and the considerable difference in architecture between the dendron Gx and PVP are the main factors facilitating the assembly of the HB denpols in the common solvent.

Journal Article↗
PubMed2006

Protein 4.2 Komatsu (D175Y) associated with the lack of interaction with ankyrin in human red blood cells.

Membrane skeletal proteins play an important role in regulating the shape and function of the human red blood cell. Protein 4.2 interacts with cytoplasmic domain of band 3 (CDB3) and ankyrin for association between the skeleton network and the membrane. The deficiency of protein 4.2 may result in hereditary spherocytosis. In order to explore the molecular mechanism of the linkage of protein 4.2 Komatsu (D175Y) and protein 4.2 Nippon (A142T) with hereditary spherocytosis, a series of protein 4.2-derived mutants were designed and expressed in Escherichia coli. Their interactions with ankyrin and CDB3 were investigated by Far Western blot and pull-down assay in vitro. The results showed that the mutant D175Y of protein 4.2 cannot interact with ankyrin while mutant A142T, just like normal protein 4.2, can bind to ankyrin directly and can associate with CDB3 in the presence of ankyrin. Based on comparing the binding abilities of the protein 4.2 mutants D175F, D175A, D175K and D175Y with ankyrin and CDB3, we suggested that defective binding of protein 4.2 Komatsu to ankyrin is resulted from the charge effect of amino acid residue 175 substitution (D-->Y), which leads to significant structural change in protein 4.2 function domain.

Anion Exchange Protein 1, Erythrocyte↗
PubMed2006

Selective solid-phase extraction of tebuconazole in biological and environmental samples using molecularly imprinted polymers.

Molecularly imprinted polymers (MIPs) were prepared by precipitation polymerization using tebuconazole (TBZ) as a template. Frontal chromatography and selectivity experiments were used to determine the binding capabilities and binding specificities of different MIPs. The polymer that had the highest binding selectivity and capability was used as the solid-phase extraction (SPE) sorbent for the direct extraction of TBZ from different biological and environmental samples (cabbage, pannage, shrimp, orange juice and tap water). The extraction protocol was optimized and the optimum conditions were: conditioning with 5 mL methanol:acetic acid (9:1), 5 mL methanol and 5 mL water respectively, loading with 5 mL aqueous samples, washing with 1.2 mL acetonitrile (ACN):phosphate buffer (5:5, pH3), and eluting with 3 mL methanol. The MIPs were able to selectively recognize, effectively trap and preconcentrate TBZ over a concentration range of 0.5-15 micromol/L. The intraday and interday RSDs were less than 9.7% and 8.6%, respectively. The limit of quantification was 0.1 micromol/L. Under optimum conditions, the MISPE recoveries of spiked cabbage, pannage, shrimp, orange juice and tap water were 62.3%, 75.8%, 71.6%, 89% and 93.9%, respectively. MISPE gave better HPLC separation efficiencies and higher recoveries than C18 SPE and strong cation exchange (SCX) SPE.

Acetic Acid↗
PubMed2006

Arginase-flotillin interaction brings arginase to red blood cell membrane.

Flotillin-1 and arginase are both up-regulated in red blood cell membrane of type 2 diabetic patients. For studying why the soluble arginase can bind to the membrane and whether such binding would modify arginase activity, the arginase1 and related proteins were cloned and expressed. The results showed that flotillin-1 can interact with arginase1, and hence arginase activity was up-regulated by 26.8%. It was estimated that about 61% of arginase1 is bound to the membrane mediated by flotillin-1. The arginase activity in diabetic patients was significantly higher than that of the controls (752.4+/-38.5 U/mg protein vs 486.7+/-28.7 U/mg protein).

Adult↗
PubMed2006

Nanogels prepared by self-assembly of oppositely charged globular proteins.

Ovalbumin and lysozyme are two main proteins in hen egg white with the isoelectric points of 4.8 and 11, respectively. Herein we report the manufacture of stable, narrowly distributed nanogels (hydrodynamic radius about 100 nm) using a novel and convenient method: ovalbumin and lysozyme solutions were mixed at pH 5.3, the mixture solution was adjusted to pH 10.3, then subsequently stirred and heated. The nanogels were characterized using a combination of techniques. The nanogels have spherical shape and core-shell structure. The core is mainly composed of lysozyme and the shell is mainly composed of ovalbumin. The proteins in the nanogels are in denatured states and they are bound by intermolecular hydrophobic interactions, hydrogen bonds, and disulfide bonds. The charges of the nanogels can be modulated by the pH of the medium. The electrostatic repulsion of ovalbumin molecules on the nanogel surface stabilizes the nanogels in aqueous solution. The formation mechanism of the nanogels is discussed.

Hot Temperature↗
PubMed2006

Selective solid-phase extraction of cholesterol using molecularly imprinted polymers and its application in different biological samples.

Non-covalent molecularly imprinted polymers (MIPs) of cholesterol were prepared by UV initiated polymerization. A polymer that had the highest binding selectivity and capability was used as solid-phase extraction (SPE) sorbents for direct extraction of cholesterol from different biological samples (human serum, cow milk, yolk, shrimp, pork and beef). The extraction conditions of molecularly imprinted SPE (MISPE) were optimized and the optimum protocol was: conditioning MISPE cartridges with n-hexane, loading with n-hexane, washing with n-hexane and n-hexane:toluene=9:1, respectively, then eluting with chloroform:ethanol:acetic acid=3:1:1. Cholesterol MISPE selectively recognized, effectively trapped and pre-concentrated cholesterol over a concentration range of 10-80 microg/mL. Recoveries ranged from 80.6% to 92.7%, with R.S.D. lower than 9.8%. Under the optimal condition, MISPE recoveries of spiked human serum, yolk, cow milk, shrimp, pork and beef were 91.1%, 80.4%, 86.6%, 78.2%, 81.4% and 80.1%, respectively. Compared with C18 SPE, almost all of the matrix interferences were removed after MISPE, and better baselines and higher selectivity were achieved.

Animals↗
PubMed2006

Associations of protein 4.2 with band 3 and ankyrin.

Protein-protein and protein-lipid interactions are thought to play the vital role in maintenance and deformation of red blood cell (RBC) membrane. Protein 4.2, a 76-KDa peripheral protein, binds to the cytoplasmic domain of band 3 (CDB3) and also interacts with ankyrin in RBCs. In order to explore the characteristics of protein 4.2-CDB3-ankyrin interactions, three protein 4.2-derived recombinant proteins encompassing amino acid residues 31-200, 1-300, and 187-260 respectively were expressed in Escherichia coli. Their interactions with CDB3 and ankyrin were investigated by using Far-Western blot and pull-down assay. The results showed that the CDB3-binding site of protein 4.2 is located in the region of residues 200-211 and the ankyrin-binding site is located in the region of residues 187-200 of protein 4.2. Our findings also suggested that the ankyrin D34 domain can interact directly with protein 4.2. The proper tertiary structures of these protein 4.2 fragments are essential for protein 4.2-ankyrin interaction. Meanwhile, ankyrin can enhance the interaction between protein 4.2 and CDB3.

Anion Exchange Protein 1, Erythrocyte↗
PubMed2006

Selective solid-phase extraction of bisphenol A using molecularly imprinted polymers and its application to biological and environmental samples.

Molecularly imprinted polymers (MIPs) were prepared using bisphenol A (BPA) as a template by precipitation polymerization. The polymer that had the highest binding selectivity and ability was used as solid-phase extraction (SPE) sorbents for direct extraction of BPA from different biological and environmental samples (human serum, pig urine, tap water and shrimp). The extraction protocol was optimized and the optimum conditions were as follows: conditioning with 5 mL methanol-acetic acid (3:1), 5 mL methanol, 5 mL acetonitrile and 5 mL water, respectively, loading with 5 mL aqueous samples, washing with 1 mL acetonitrile, and eluting with 3 mL methanol. MIPs can selectively recognize, effectively trap and preconcentrate BPA over a concentration range of 2-20 microM. Recoveries ranged from 94.03 to 105.3%, with a relative standard deviation lower than 7.9%. Under the optimal condition, molecularly imprinted SPE recoveries of spiked human serum, pig urine, tap water and shrimp were 65.80, 82.32, 76.00 and 75.97%, respectively, when aqueous samples were applied directly. Compared with C18 SPE, a better baseline, better high-performance liquid chromatography separation efficiency and higher recoveries were achieved after molecularly imprinted SPE.

Animals↗
PubMed2006

Acidic solution properties of beta-casein-graft-dextran copolymer prepared through Maillard reaction.

The copolymer of beta-casein-graft-dextran was prepared using the Maillard reaction and the acidic solution properties of the copolymer were studied with dynamic light scattering. At pH range 4-5 where is close to the isoelectric point of beta-casein, the copolymer forms micelles which are spherical verified by atomic force microscopy imaging. The size and existent time of the micelles depend on the graft degree and the length of dextran side chains of the copolymers. During storage at pH 4.6, the micelles formed by the copolymers with short side chains and low graft degree tend to precipitate, while the micelles formed by the copolymers with long side chains and high graft degree tend to dissociate. The micellization of the copolymers can be suppressed by adding NaCl. Optical microscopy and turbidity studies show that the copolymers dissolved in molecular state and with higher hydrophilicity have better emulsifying ability.

Biocompatible Materials↗
PubMed2006

Polymeric self-assembly into micelles and hollow spheres with multiscale cavities driven by inclusion complexation.

The inclusion complexation between beta-CD (beta-cyclodextrin) and adamantyl group (ADA) is used as a driving force in constructing polymeric micelles. The micelles composed of a hydrophobic core of PtBA-ADA and a hydrophilic shell of PGMA-CD show unique properties due to the presence of beta-CDs on the micellar surface. The micelles can be converted to hollow spheres of PGMA-CD networks. The hollow spheres possess a central hole in the size of submicrometers and many cavities of beta-CDs of 0.7 nm on the surface.

Journal Article↗
PubMed2006

Stable and pH-sensitive nanogels prepared by self-assembly of chitosan and ovalbumin.

Two natural macromolecules, chitosan and ovalbumin, were used to produce nanogels by a new, green, and convenient method. Chitosan and ovalbumin solutions were mixed; the pH of the resulting solution was adjusted; and the solution was successively stirred and heated. After that, ovalbumin gelled forming nanospheres. The chitosan chains are supposed to be partly trapped in the nanogel core upon heating because of the electrostatic attractions between chitosan and ovalbumin, while the rest of the chitosan chains should form the shell of the nanogels. The nanogels did not change the size distribution after long-time storage and did not dissociate in the pH range of 2-10.5. The dispersibility, size, and hydrophobicity/hydrophilicity of the nanogels are pH-dependent. The nanogels are good candidates for cosmetic and pharmaceutical applications.

Chitosan↗
PubMed2006

Induction of transforming growth factor-beta 1 on dentine pulp cells in different culture patterns.

Recent studies have documented that TGF-beta1 takes part in dental pulp tissue repair. Moreover, dental pulp cells have the potential to differentiate into odontoblast-like cells and produce reparative dentine in this process. However, the molecular mechanisms and potential interactions between TGF-beta1 and dental pulp cells are not clear due to the complexity of the pulp/dentine microenvironment. In this study, we investigated the induction of TGF-beta1 on the dental pulp cells in cell culture, tissue culture and three-dimensional culture patterns. These results demonstrated that TGF-beta1 significantly increased the proliferation of cells and activity of ALPase. Dental pulp cells cultured in the presence of TGF-beta1 formed mineralization nodules. In the organ culture, dental pulp cells treated with TGF-beta1 differentiated into odontoblast-like cells and formed a pulp-dentinal complex; and TGF-beta1 significantly induced synthesis of dentine relative proteins DSPP, DMP-1. The dental pulp cells share some characteristics of the odontoblast, such as a parallel arrangement with columnar form and a unilateral cell process. Together, these data indicate that TGF-beta1 can make dental pulp cells differentiated into odontoblast-like cells and form the pulp-dentinal complex. Moreover, these results suggest that TGF-beta1 is an important regulatory factor in odontoblast differentiation during tooth development and pulp repair.

Bone Matrix↗
PubMed2006

Direct enrichment and high performance liquid chromatography analysis of ultra-trace Bisphenol A in water samples with narrowly dispersible Bisphenol A imprinted polymeric microspheres column.

Direct injection, enrichment and high performance liquid chromatography (HPLC) analysis of ultra-trace Bisphenol A (BPA) in water samples using one narrowly dispersible BPA imprinted polymeric microspheres (MIPM) column in one analysis process was developed. One BPA imprinted MIPM that had the best globular morphology and imprinted efficiency was used as HPLC stationary phase and applied to direct analysis of ultra-trace BPA in water. The optimum direct analysis conditions were: conditioning the MIPM column with water for 10min, injecting 40mL water sample directly, eluting with 70% methanol for 13min and then 100% methanol for 7min. Under the optimum conditions, the MIPM column can simultaneously extract, enrich, separate and determine ultra-trace BPA in one analysis process with UV detector by injection of large volume water samples (40mL). The calibration graph was linear with R(2)>0.998 in the ranges from 0.1-100nmol/L BPA standard solution. The intra- and inter-day RSD are less than 9.5 and 9.6%, respectively. The limit of quantification was 0.1nmol/L. RSD for spiked tap and lake water was less than 8.9% and the recoveries were 96-101.8%. The enrichment factor for BPA was 10,000 as 40mL water sample was directly injected and analyzed.

Benzhydryl Compounds↗