Time filter

Source Type

Shi X.,Zhejiang Sci-Tech University | Fang Q.,Zhejiang Sci-Tech University | Ding M.,Zhejiang Sci-Tech University | Wu J.,Zhejiang Sci-Tech University | And 6 more authors.
Journal of Biomaterials Applications | Year: 2016

To develop biocompatible composite microspheres for novel hemostatic use, we designed and prepared a novel biomaterial, composite microspheres consisting of carboxymethyl chitosan, sodium alginate, and collagen (CSCM). The ultra-structure of CSCM was investigated by scanning electron microscopy assay. In hemostatic function experiment, it was found that CSCM could facilitate platelet adherence, platelet aggregation, and platelet activation in vitro. Besides, the maximum swelling of CSCM submerged in PBS for 50 min was over 300% of that exhibited by commercial hemostatic compound microporous polysaccharide haemostatic powder (CMPHP). In addition, CSCM exhibited good biodegradability and non-cytotoxicity. These results demonstrated that CSCM may be useful in platelet plug formation, and this study would provide important information for further research on hemostasis experiment in vivo. © 2015 The Author(s).

Zhang J.,Zhejiang Sci-Tech University | Zhang J.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | Liu Y.,Zhejiang Sci-Tech University | Liu Y.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | And 23 more authors.
Gene | Year: 2013

MicroRNAs are indispensable players in the regulation of a broad range of biological processes. Here, we report the first deep sequencing of the whitespotted bamboo shark (Chiloscyllium plagiosum) liver. We mapped 91 miRNAs in the Callorhinchus milii genome that have previously been described in the Danio rerio, Fugu rubripes, Oryzias latipes, Xenopus laevis, Xenopus tropicalis, Homo sapiens, and Mus musculus. In addition, 156 new putative candidate (PC) C. plagiosum miRNAs were identified. From these 247 miRNAs, 39 miRNA clusters were identified, and the expression of these clustered miRNAs was observed to vary significantly. A total of 7 candidate miRNAs were selected for expression confirmation by stem-loop RT-PCR. This study resulted in the addition of a significant number of novel miRNA sequences to GenBank and laid the foundation for further understanding of the function of miRNAs in the regulation of C. plagiosum liver development. © 2013 Elsevier B.V.

Lv Z.,Zhejiang Sci-Tech University | Lv Z.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | Wang T.,Zhejiang Sci-Tech University | Wang T.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | And 20 more authors.
International Journal of Genomics | Year: 2013

The Ras oncogene of silkworm pupae (Bras2) may belong to the Ras superfamily. It shares 77% of its amino acid identity with teratocarcinoma oncogene 21 (TC21) related ras viral oncogene homolog-2 (R-Ras2) and possesses an identical core effector region. The mRNA of Bombyx mori Bras2 has 1412 bp. The open reading frame contains 603 bp, which encodes 200 amino acid residues. This recombinant BmBras2 protein was subsequently used as an antigen to raise a rabbit polyclonal antibody. Western blotting and real-time PCR analyses showed that BmBras2 was expressed during four developmental stages. The BmBras2 expression level was the highest in the pupae and was low in other life cycle stages. BmBras2 was expressed in all eight tested tissues, and it was highly expressed in the head, intestine, and epidermis. Subcellular localization studies indicated that BmBras2 was predominantly localized in the nuclei of Bm5 cells, although cytoplasmic staining was also observed to a lesser extent. A cell proliferation assay showed that rBmBras2 could stimulate the proliferation of hepatoma cells. The higher BmBras2 expression levels in the pupal stage, tissue expression patterns, and a cell proliferation assay indicated that BmBras2 promotes cell division and proliferation, most likely by influencing cell signal transduction. © 2013 Zhengbing Lv et al.

Yu W.,Zhejiang Sci-Tech University | Yu W.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | Wang M.,Zhejiang Sci-Tech University | Wang M.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | And 6 more authors.
International Journal of Genomics | Year: 2013

Storage protein 2 (SP2) not only is an important source of energy for the growth and development of silkworm but also has inhibitory effects on cell apoptosis. Endothelial cell (EC) apoptosis is an important contributing factor in the development of atherosclerosis; therefore, study of the antiapoptotic activity of SP2 on ECs provides information related to the treatment of atherosclerosis and other cardiovascular diseases. In this study, the sp2 gene was cloned and expressed in Escherichia coli to produce a 6xHis-tagged fusion protein, which was then used to generate a polyclonal antibody. Western blot results revealed that SP2 levels were higher in the pupal stage and hemolymph of fifth-instar larvae but low in the egg and adult stages. Subcellular localization results showed that SP2 is located mainly on the cell membrane. In addition, a Bac-to-Bac system was used to construct a recombinant baculovirus for SP2 expression. The purified SP2 was then added to a culture medium for human umbilical vein ECs (HUVECs), which were exposed to staurosporine. A cell viability assay demonstrated that SP2 could significantly enhance the viability of HUVEC. Furthermore, both ELISA and flow cytometry results indicated that SP2 has anti-apoptotic effects on staurosporine-induced HUVEC apoptosis. © 2013 Wei Yu et al.

Lv Z.,Zhejiang Sci-Tech University | Lv Z.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | Zhang X.,Zhejiang Sci-Tech University | Zhang X.,Zhejiang Provincial Key Laboratory of Silkworm Bioreactor and Biomedicine | And 22 more authors.
Gene | Year: 2012

Background: Prohibitin (PHB) is an evolutionarily conserved multifunctional protein with ubiquitous expression. However, its molecular roles are largely unknown. Methods: To better understand the function of prohibitin protein in silkworm (BmPHB), its coding sequence was isolated from a cDNA library of silkworm pupae. An His-tagged BmPHB fusion protein was expressed in . Escherichia coli Rosetta (DE3) and purified with affinity and reversed-phase chromatography. Purified rBmPHB was used to generate anti-BmPHB polyclonal antibody. The subcellular localization of BmPHB was analysed by immunohistochemistry. Results: BmPHB gene has an ORF of 825. bp, encoding a predicted peptide with 274 amino acid residues. Immunostaining indicate that prohibitin is expressed in nucleus and predominately in cytoplasm. Western blot analyses indicated that, in the fifth instar larva, BmPHB was expressed descendingly in gonad, malpighian tubule, trachea, fatty body, intestine, and head. However, no expression was detected in larva's silk gland and epidermis. In addition, BmPHB was expressed in the nascent egg, larva and pupa, but not in the moth. Conclusions: The expression of . BmPHB gene presents differential characteristic in different stage and tissues. It may play important roles in the development of silkworm. General significance: Studies on . prohibitin have been still restricted to a few specific insects and insect cell lines such as . Drosophila, . Acyrthosiphon pisum and mosquito cell lines, not yet in silkworm. This is a first characterization of prohibitin in silkworm, . B. mori. © 2012 Elsevier B.V.

Discover hidden collaborations