Effect of Crystal Size of Calcium Oxalate Dihydrate on Cytotoxicity of African Green Monkey Kidney Epithelial Cells

2016 ◽  
Vol 31 (3) ◽  
pp. 317
Author(s):  
GAN Qiong-Zhi ◽  
ZHANG Chong-Yu ◽  
OUYANG Jian-Ming
Keyword(s):  
Epithelial Cells ◽  
Calcium Oxalate ◽  
Crystal Size ◽  
African Green Monkey ◽  
Monkey Kidney ◽  
Calcium Oxalate Dihydrate ◽  
African Green Monkey Kidney ◽  
Oxalate Dihydrate ◽  
Green Monkey ◽  
Kidney Epithelial Cells

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells

1985 ◽  
Vol 5 (9) ◽  
pp. 2181-2189
Author(s):  
L V Jones ◽  
R W Compans ◽  
A R Davis ◽  
T J Bos ◽  
D P Nayak
Keyword(s):  
Influenza Virus ◽  
Influenza A ◽  
Surface Expression ◽  
African Green Monkey ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
African Green Monkey Kidney ◽  
Amino Terminal ◽  
Green Monkey ◽  
Na Gene

We have investigated the site of surface expression of the neuraminidase (NA) glycoprotein of influenza A virus, which, in contrast to the hemagglutinin, is bound to membranes by hydrophobic residues near the NH2-terminus. Madin-Darby canine kidney or primary African green monkey kidney cells infected with influenza A/WSN/33 virus and subsequently labeled with monoclonal antibody to the NA and then with a colloidal gold- or ferritin-conjugated second antibody exhibited specific labeling of apical surfaces. Using simian virus 40 late expression vectors, we also studied the surface expression of the complete NA gene (SNC) and a truncated NA gene (SN10) in either primary or a polarized continuous line (MA104) of African green monkey kidney cells. The polypeptides encoded by the cloned NA cDNAs were expressed on the surface of both cell types. Analysis of [3H]mannose-labeled polypeptides from recombinant virus-infected MA104 cells showed that the products of cloned NA cDNA comigrated with glycosylated NA from influenza virus-infected cells. Both the complete and the truncated glycoproteins were found to be preferentially expressed on apical plasma membranes, as detected by immunogold labeling. These results indicate that the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.

Assessment of potential miRNA biomarkers of VERO-cell tumorigenicity in a new line (AGMK1-9T7) of African green monkey kidney cells

Vaccine ◽  
2017 ◽  
Vol 35 (41) ◽  
pp. 5503-5509 ◽  
Author(s):  
Belete Teferedegne ◽  
Daniel M. Rotroff ◽  
Juliete Macauley ◽  
Gideon Foseh ◽  
Gladys Lewis ◽  
...  
Keyword(s):  
Vero Cell ◽  
African Green Monkey ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
African Green Monkey Kidney ◽  
Green Monkey

scholarly journals Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells.

1985 ◽  
Vol 5 (9) ◽  
pp. 2181-2189 ◽  
Author(s):  
L V Jones ◽  
R W Compans ◽  
A R Davis ◽  
T J Bos ◽  
D P Nayak
Keyword(s):  
Influenza Virus ◽  
Influenza A ◽  
Surface Expression ◽  
African Green Monkey ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
African Green Monkey Kidney ◽  
Amino Terminal ◽  
Green Monkey ◽  
Na Gene

We have investigated the site of surface expression of the neuraminidase (NA) glycoprotein of influenza A virus, which, in contrast to the hemagglutinin, is bound to membranes by hydrophobic residues near the NH2-terminus. Madin-Darby canine kidney or primary African green monkey kidney cells infected with influenza A/WSN/33 virus and subsequently labeled with monoclonal antibody to the NA and then with a colloidal gold- or ferritin-conjugated second antibody exhibited specific labeling of apical surfaces. Using simian virus 40 late expression vectors, we also studied the surface expression of the complete NA gene (SNC) and a truncated NA gene (SN10) in either primary or a polarized continuous line (MA104) of African green monkey kidney cells. The polypeptides encoded by the cloned NA cDNAs were expressed on the surface of both cell types. Analysis of [3H]mannose-labeled polypeptides from recombinant virus-infected MA104 cells showed that the products of cloned NA cDNA comigrated with glycosylated NA from influenza virus-infected cells. Both the complete and the truncated glycoproteins were found to be preferentially expressed on apical plasma membranes, as detected by immunogold labeling. These results indicate that the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.

Size-dependent toxicity and interactions of calcium oxalate dihydrate crystals on Vero renal epithelial cells

2015 ◽  
Vol 3 (9) ◽  
pp. 1864-1878 ◽  
Author(s):  
Xin-Yuan Sun ◽  
Jian-Ming Ouyang ◽  
Wen-Yu Zhu ◽  
Yu-Bao Li ◽  
Qiong-Zhi Gan
Keyword(s):  
Epithelial Cells ◽  
Calcium Oxalate ◽  
Calcium Oxalate Dihydrate ◽  
Renal Epithelial Cells ◽  
Size Dependent ◽  
Oxalate Dihydrate

Size-dependent toxicity and interactions of calcium oxalate dihydrate crystals on Vero renal epithelial cells were demonstrated.

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