Initiation and characterization of primary mouse kidney epithelial cultures

1988 ◽  
Vol 24 (7) ◽  
pp. 683-695 ◽  
Author(s):  
C. L. Bell ◽  
H. S. Tenenhouse ◽  
C. R. Scriver
Keyword(s):  
Mouse Kidney ◽  
Primary Mouse ◽  
Epithelial Cultures

scholarly journals Purification and characterization of type IV collagen from mouse kidney.

1986 ◽  
Vol 34 (2) ◽  
pp. 789-797 ◽  
Author(s):  
TSUTOMU OIKAWA ◽  
TAKAO IWAGUCHI ◽  
MIKIO KIMURA ◽  
AKIO MATSUZAWA
Keyword(s):  
Type Iv Collagen ◽  
Mouse Kidney ◽  
Purification And Characterization ◽  
Type Iv

scholarly journals Characterization of primary rat nasal epithelial cultures in CFTR knockout rats as a model for CF sinus disease

2017 ◽  
Vol 127 (11) ◽  
pp. E384-E391 ◽  
Author(s):  
Kiranya E. Tipirneni ◽  
Do-Yeon Cho ◽  
Daniel F. Skinner ◽  
Shaoyan Zhang ◽  
Calvin Mackey ◽  
...  
Keyword(s):  
Sinus Disease ◽  
Epithelial Cultures

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.

P53-transformation-related protein: Kinetics of synthesis and accumulation in sv40-infected primary mouse kidney cell cultures

Virology ◽  
1985 ◽  
Vol 147 (2) ◽  
pp. 275-286 ◽  
Author(s):  
Arlette Duthu ◽  
Jean-Claude Ehrhart ◽  
Sam Benchimol ◽  
Krish Chandrasekaran ◽  
Pierre May
Keyword(s):  
Cell Cultures ◽  
Kidney Cell ◽  
Mouse Kidney ◽  
Related Protein ◽  
Protein Kinetics ◽  
Primary Mouse ◽  
Kinetics Of

A 105 000 dalton antigen of transformed mouse cells is a stress protein

1985 ◽  
Vol 63 (12) ◽  
pp. 1258-1264 ◽  
Author(s):  
T. M. Rose ◽  
E. W. Khandjian
Keyword(s):  
Primary Cultures ◽  
Stress Protein ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Mouse Kidney ◽  
Immunofluorescent Staining ◽  
Protein Antigens ◽  
Primary Mouse ◽  
Mouse Cells ◽  
Cytoplasmic Structures

Antisera prepared in mice against syngeneic spontaneously transformed AL/N cells (anti-TAL/N serum) identified a number of protein antigens synthesized by simian virus 40 (SV40) transformed cells, among which was a protein with a molecular mass of 105 000 daltons (p105). Of these transformed cell antigens which were immunogenic in a syngeneic system, only p105 was detected in primary mouse kidney cell cultures, p105 isolated from normal and transformed mouse cells was demonstrated to be identical by two-dimensional gel analysis. Relatively small amounts of p105 were synthesized in quiescent primary cultures, while the protein was actively synthesized in SV40-infected as well as in proliferating mouse kidney cells, and its synthesis in quiescent cells could be induced by subjecting the cultures to glucose starvation or heat-shock treatment. Immunofluorescent staining and cellular fractionation showed that p105 is normally localized to cytoplasmic structures. The results suggest that the expression of p105 is intimately associated with the metabolic state of the cell.

Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B)

2001 ◽  
Vol 354 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Penio T. TODOROV ◽  
Rachel E. HARDISTY ◽  
Steve D. M. BROWN
Keyword(s):  
Binding Sites ◽  
Strong Association ◽  
Mouse Kidney ◽  
Scatchard Analysis ◽  
Tail Region ◽  
Immunoblotting Analysis ◽  
Kd Values ◽  
Myosin Viia

Myosin VIIA is a motor molecule with a conserved head domain and tail region unique to myosin VIIA, which probably defines its unique function in vivo. In an attempt to further characterize myosin VIIA function we set out to identify molecule(s) that specifically associate with it. We demonstrate that 17 and 55kDa proteins from mouse kidney and cochlea co-purify with myosin VIIA on affinity columns carrying immobilized anti-myosin VIIA antibody. N-terminal sequencing and immunoblotting analysis identified the 17kDa protein as calmodulin, whereas MS and immunoblotting analysis identified the 55kDa protein as microtubule-associated protein-2B (MAP-2B). Myosin VIIA can also be co-immunoprecipitated from kidney homogenate using anti-calmodulin or anti-MAP2 (recognizing isoforms 2A and 2B) antibodies, confirming the strong association between calmodulin and myosin VIIA and between MAP-2B and myosin VIIA. Myosin VIIA binds to calmodulin with an apparent Kd of 10-9 M. Scatchard analysis of the binding of myosin VIIA to MAP-2B provided evidence for two binding sites, with Kd values of 10-10 and 10-9 M, which have been mapped to medial and C-terminal tail domains of myosin VIIA. The characterization of the interaction of calmodulin and MAP-2B with myosin VIIA provides new insights into the function of myosin VIIA.

scholarly journals Enzymatic histochemistry of mouse kidney in plastic.

1987 ◽  
Vol 35 (4) ◽  
pp. 483-487 ◽  
Author(s):  
T P Pretlow ◽  
A S Lapinsky ◽  
L C Flowers ◽  
R W Grane ◽  
T G Pretlow
Keyword(s):  
Alkaline Phosphatase ◽  
Proximal Tubule ◽  
Leucine Aminopeptidase ◽  
Kidney Diseases ◽  
Mouse Kidney ◽  
Frozen Sections ◽  
Gamma Glutamyl Transpeptidase ◽  
Glutamyl Transpeptidase ◽  
Bowman's Capsule

Two-micrometer sections of methacrylate-embedded kidney were used to investigate the enzymatic activities of mouse kidney where the proximal tubule and Bowman's capsule from the same corpuscle were viewed in the same section. Alkaline phosphatase, acid phosphatase, 5'-nucleotidase, gamma-glutamyl transpeptidase, N-acetyl-beta-glucosaminidase, leucine aminopeptidase, alpha-naphthyl butyrate esterase, and adenosine triphosphatase activities were observed in the proximal tubule, but only 5'-nucleotidase, alpha-naphthyl butyrate esterase, and alkaline phosphatase were observed in the squamous portion of the parietal epithelium of Bowman's capsule. The use of methacrylate-embedded tissue allowed more precise localization of enzymatic activity than is possible with most frozen sections. This may provide interesting applications not only for characterization of kidney diseases but also for characterization of other normal and abnormal tissues.

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