scholarly journals A novel polypeptide from Cervus nippon Temminck proliferation of epidermal cells and NIH3T3 cell line.

2006 ◽  
Vol 53 (2) ◽  
pp. 395-397 ◽  
Author(s):  
Shu-Wen Guan ◽  
Leng-Xin Duan ◽  
Yuan-Yuan Li ◽  
Ben-Xiang Wang ◽  
Qiu-Li Zhou

A novel polypeptide, velvet antler polypeptide (VAPPs), having a stimulary effect on proliferation of some cell was isolated from the velvet antler of sika deer (Cervus nippon Temminck). This polypeptide consists of a single chain of 32 amino-acid residues VLSAT DKTNV LAAWG KVGGN APAFG AEALE RM. VAPPs showed marked stimulary effect on rat epidermal cells and NIH3T3 cell line (dose range from 10-40 mg x L(-1) and 5-80 mg x L(-1), respectively).

Cell Research ◽  
2002 ◽  
Vol 12 (3-4) ◽  
pp. 229-233 ◽  
Author(s):  
Xi CHEN ◽  
Wei ZHANG ◽  
Yun Fei GAO ◽  
Xiao Qin SU ◽  
Zhong He ZHAI

2020 ◽  
Vol 02 (01) ◽  
pp. e23-e27
Author(s):  
Xinyi Xiao ◽  
Hui Chen ◽  
Pameila Paerhati ◽  
Meiqi Zhou ◽  
Zhuoyi Yang ◽  
...  

Abstract Aim NIH3T3 cell line with expression of human receptor for advanced glycation end-products (hRAGE) transduced with lentivirus vectors was used to analyze affinity, biological activity, and/or molecular mechanisms of molecules targeting the hRAGE pathway. Method The DNA fragment coding for hRAGE gene was integrated into the genome of NIH3T3 cells using lentivirus transduction. Cells expressing hRAGE were selected with puromycin, and the level of hRAGE expression was analyzed by Western blot. To establish a stable cell line, colonies of hRAGE-expressing cells were generated, and the level of RAGE expression in each engineered cell line was analyzed within 20 generations. Flow cytometry assay was used to verify affinity of anti-hRAGE antibody binding to hRAGE on the surface of engineered cells. The engineered NIH3T3 cell line was applied to assess effects of anti-hRAGE blocking antibody on amyloid β-induced cells apoptosis by CCK-8 assay. Results The engineered NIH3T3 cell line (hRAGE-NIH3T3) could stably express human RAGE. Commercial anti-RAGE polyclonal antibody could recognize and bind to human RAGE on the surface of hRAGE-NIH3T3 but not original NIH3T3 cells. In addition, hRAGE-NIH3T3 was more sensitive to RAGE pathway-dependent stimulation. Our data show that the hRAGE-NIH3T3 cell line established is an excellent tool in the study of RAGE-targeting molecules based on the cellular level, biological function, and RAGE-mediated molecular mechanisms.


2013 ◽  
Vol 380-384 ◽  
pp. 4295-4298
Author(s):  
Wen He Zhu ◽  
Jun Jie Xu ◽  
Wei Zhang ◽  
Yan Li ◽  
Xiao Jing Lu ◽  
...  

A highly osteogenic hybrid bioabsorbable scaffold was developed for bone reconstruction. Though the use of a bioabsorbable collagen and chitosan scaffold for loading velvet antler polypeptide to repair bone defect and drug treatment. Velvet antler polypeptide and collagen were extracted for developing the compounded material. The SEM results show that the collagen and chitosan scaffold maintain the natural three dimensional network structures. The cell proliferation experiment result show that the can promote the osteoblast proliferation for a long time . These results indicated that this compound scaffold can sustainable to release drug and is a good material in bone defect and drug treatment.


2003 ◽  
Vol 17 (7) ◽  
pp. 1192-1202 ◽  
Author(s):  
Gregory B. Fralish ◽  
Brian Dattilo ◽  
David Puett

Abstract Binding of the heterodimeric glycoprotein hormone, chorionic gonadotropin (CG), occurs to the heptahelical LH receptor N-terminal ectodomain (ECD), a large portion of which has been modeled as a leucine-rich repeat protein. In this study, we expressed and purified three single chain N-CG-ECD-C complexes, one comprising the full-length ECD, 1–341 (encoded by exons 1–10 and a portion of 11), and two C-terminal ECD deletion fragments, 1–294 (encoded by exons 1–10) and 1–180 (encoded by exons 1–7). The fusion proteins, including yoked CG (N-β-α-C), were characterized by Western blot analysis and circular dichroism (CD). Analysis of the CD spectra obtained on the CG-ECD fusion proteins, and of the difference spectrum of each after subtracting the CG contribution, yielded secondary structures consistent with a repeating β-strand/α-helix fold as predicted in the homology model. A marked decrease in helicity was observed when the C-terminal 47 amino acid residues were removed from the ECD. Removal of an additional 114 residues, i.e. the region encoded by exons 8–10, results in the loss of fewer helical residues. These results suggest that the hinge region of the ECD, predicted to contain only limited secondary structure, interacts with and stabilizes the ligand-occupied N-terminal portion. Furthermore, the results support a repeating fold, consistent with the proposed model for the LHR ECD.


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