Influenza Virus: Association of Mouse-Lung Virulence with Plaque Formation in Mouse Kidney Cells

Intervirology ◽  
1976 ◽  
Vol 7 (4-5) ◽  
pp. 201-210 ◽  
Author(s):  
Bertram Flehmig ◽  
Angelika Vallbracht ◽  
Hans-Joachim Gerth
Keyword(s):  
Influenza Virus ◽  
Plaque Formation ◽  
Mouse Kidney ◽  
Mouse Lung ◽  
Kidney 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.

scholarly journals A NIMA-related Kinase, Fa2p, Localizes to a Novel Site in the Proximal Cilia of Chlamydomonas and Mouse Kidney Cells

2004 ◽  
Vol 15 (11) ◽  
pp. 5172-5186 ◽  
Author(s):  
Moe R. Mahjoub ◽  
M. Qasim Rasi ◽  
Lynne M. Quarmby
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Cell Types ◽  
Mouse Kidney ◽  
Kidney Cells ◽  
Polycystic Kidney ◽  
Cycle Progression ◽  
Cystic Kidneys ◽  
Ciliary Function ◽  
The Relationship

Polycystic kidney disease and related syndromes involve dysregulation of cell proliferation in conjunction with ciliary defects. The relationship between cilia and cell cycle is enigmatic, but it may involve regulation by the NIMA-family of kinases (Neks). We previously showed that the Nek Fa2p is important for ciliary function and cell cycle in Chlamydomonas. We now show that Fa2p localizes to an important regulatory site at the proximal end of cilia in both Chlamydomonas and a mouse kidney cell line. Fa2p also is associated with the proximal end of centrioles. Its localization is dynamic during the cell cycle, following a similar pattern in both cell types. The cell cycle function of Fa2p is kinase independent, whereas its ciliary function is kinase dependent. Mice with mutations in Nek1 or Nek8 have cystic kidneys; therefore, our discovery that a member of this phylogenetic group of Nek proteins is localized to the same sites in Chlamydomonas and kidney epithelial cells suggests that Neks play conserved roles in the coordination of cilia and cell cycle progression.

1,25-Dihydroxyvitamin D3Is a Novel Transcriptional Regulator of the Anti-Aging Gene Klotho in Human and Mouse Kidney Cells.

2010 ◽  
pp. P2-27-P2-27
Author(s):  
RE Forster ◽  
CL Lowmiller ◽  
GK Whitfield ◽  
CA Haussler ◽  
PW Jurutka ◽  
...  
Keyword(s):  
Transcriptional Regulator ◽  
Mouse Kidney ◽  
Kidney Cells ◽  
Human And Mouse

Repression of a G0-associated 65-kilodalton protein in actively proliferating and SV40-transformed mouse kidney cells

1992 ◽  
Vol 70 (2) ◽  
pp. 149-155 ◽  
Author(s):  
Timothy M. Rose ◽  
Sandra Tremblay ◽  
Edward W. Khandjian
Keyword(s):  
Primary Cultures ◽  
Growth Arrest ◽  
Mouse Kidney ◽  
Specific Gene ◽  
Nuclear Fraction ◽  
Quiescent State ◽  
Kidney Cells ◽  
Experimental Conditions ◽  
Two Dimensional Gel Electrophoresis ◽  
Mouse Cells

The pattern of [35S]methionine-labeled proteins from primary cultures of mouse kidney epithelial cells arrested in G0 phase was analyzed by two-dimensional gel electrophoresis and compared with that observed from cultures of actively proliferating and SV40-transformed mouse kidney cells. A major polypeptide (p65) migrating with a molecular mass of 65 000 daltons and a pI of 5.8 was detected in quiescent cultures of cells which had exhausted their finite division potential. Under the experimental conditions used, these cells had lost sensitivity to growth factors and were irreversibly blocked in G0 phase of the cell cycle. In cultures of actively proliferating mouse kidney cells, the expression of p65 was not observed until just prior to arrest. Moreover, proliferating cultures of immortalized mouse kidney cells that had been reactivated from their quiescent state by infection with SV40 did not express p65. Subcellular localization studies suggest that p65 is associated with the crude nuclear fraction. In addition, p65 is glycosylated and binds the lectin concanavalin A. Pulse–chase experiments demonstrated that p65 was short lived with an estimated half life of 10 min. Thus, p65 appears to be a growth-arrest specific gene product whose expression is repressed during the proliferative state of mitotically active mouse kidney cells.Key words: G0 phase, senescence, proliferation, quiescence, SV40-transformed mouse cells.

Expression of oncomodulin does not lead to the transformation or immortalization of mammalian cells in vitro

1989 ◽  
Vol 94 (3) ◽  
pp. 517-525
Author(s):  
A.M. Mes-Masson ◽  
S. Masson ◽  
D. Banville ◽  
L. Chalifour
Keyword(s):  
Mammalian Cells ◽  
Mouse Kidney ◽  
Kidney Cells ◽  
T Antigens ◽  
Primary Mouse ◽  
Specific Antisera ◽  
Growth Properties ◽  
Metallothionein Promoter ◽  
Specific Mrna

A recombinant plasmid (pMTONCO) containing the coding sequences for rat oncomodulin under the direction of the metallothionein promoter was constructed. pMTONCO was co-transfected with the pSV2-NEO plasmid into primary mouse kidney cells or Rat-1 cells using the calcium phosphate technique and stable transformants were isolated after selection with G418. Transcription from the metallothionein promoter was inducible with heavy metals and produced an oncomodulin-specific mRNA. The presence of oncomodulin protein in stable cell lines was verified by immunoprecipitation with specific antisera. While a plasmid encoding the polyomavirus T-antigens was able to prolong the life-span of primary mouse kidney cells in culture, no equivalent activity was noted when the pMTONCO plasmid was used to transfect primary cells. When expressed in Rat-1 cells, oncomodulin did not affect the growth properties of these cells, nor did it predispose cells to higher frequencies of oncogenic transformation to a viral oncogene. We conclude that oncomodulin is neither an immortalizing nor transforming agent in vitro.

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