ALKALINE PHOSPHATASE LEVELS IN TWO CLOSELY RELATED CELL LINES IN TISSUE CULTURE

1966 ◽  
Vol 8 (4) ◽  
pp. 613-615 ◽  
Author(s):  
Edward O. Dodson
Keyword(s):  
Tissue Culture ◽  
Alkaline Phosphatase ◽  
Cell Lines ◽  
Related Cell

scholarly journals Cancer stem cells and cisplatin‐resistant cells isolated from non‐small‐lung cancer cell lines constitute related cell populations

2014 ◽  
Vol 3 (5) ◽  
pp. 1099-1111 ◽  
Author(s):  
Blanca D. Lopez‐Ayllon ◽  
Veronica Moncho‐Amor ◽  
Ander Abarrategi ◽  
Inmaculada Ibañez Cáceres ◽  
Javier Castro‐Carpeño ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Stem Cells ◽  
Cancer Stem Cells ◽  
Cell Lines ◽  
Cancer Cell ◽  
Cancer Cell Lines ◽  
Cell Populations ◽  
Lung Cancer Cell ◽  
Related Cell ◽  
Resistant Cells

Establishment of Alkaline Phosphatase deficient odontogenous cell lines to analyze dental aspects of hypophosphatasia

2021 ◽  
Author(s):  
S Paulus ◽  
S Graser ◽  
T Kreuzahler ◽  
M Rudert ◽  
D Docheva ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Lines

scholarly journals Human common acute lymphoblastic leukemia-derived cell lines are competent to recombine their T-cell receptor delta/alpha regions along a hierarchically ordered pathway

Blood ◽  
1992 ◽  
Vol 80 (9) ◽  
pp. 2353-2362
Author(s):  
TE Hansen-Hagge ◽  
S Yokota ◽  
HJ Reuter ◽  
K Schwarz ◽  
CR Bartram
Keyword(s):  
Tissue Culture ◽  
T Cell ◽  
T Cell Receptor ◽  
Cell Lines ◽  
Signal Sequence ◽  
Lymphoblastic Leukemia ◽  
Cell Receptor ◽  
Culture Conditions ◽  
Initial Culture ◽  
Human B Cell

Rearrangements of the T-cell receptor (TCR) delta locus are observed in the majority of human B-cell precursor acute lymphoblastic leukemias (ALL) with a striking predominance of V delta 2(D)D delta 3 recombinations in common ALL (cALL) patients. Recently, we and others showed that almost 20% of cALL cases are characterized by further recombination of V delta 2(D)D delta 3 segments to J alpha elements, thereby deleting the TCR delta locus in analogy to the delta Rec/psi J alpha pathway in differentiating alpha/beta-positive T cells. We report here that two human cALL-derived cell lines, REH and Nalm-6, are competent to recombine the TCR delta/alpha locus under standard tissue culture conditions. Analysis of different REH subclones obtained by limiting dilution of the initial culture showed a biased recombination of V delta 2D delta 3 to distinct J alpha elements. During prolonged tissue culture, a subclone acquired growth advantage and displaced parental cells as well as other subclones. Frequently, the DJ junctions of REH subclones contained extended stretches of palindromic sequences derived from modified D delta 3 coding elements. The other cell line, Nalm-6, started the TCR delta/alpha recombination with an unusual signal joint of a cryptic recombinase signal sequence (RSS) upstream of D delta 3 to the 3′ RSS of D delta 3. The RSS dimer was subsequently rearranged in all investigated subclones to an identical J alpha element. Both cell lines might become valuable tools to unravel the complex regulation of TCR delta/alpha recombination pathways in malignant and normal lymphopoiesis.

scholarly journals Use of Tissue Culture Cell Lines to Evaluate HIV Antiviral Resistance

2008 ◽  
Vol 24 (7) ◽  
pp. 957-967 ◽  
Author(s):  
Halina Krowicka ◽  
James E. Robinson ◽  
Rebecca Clark ◽  
Shannon Hager ◽  
Stephanie Broyles ◽  
...  
Keyword(s):  
Tissue Culture ◽  
Cell Lines ◽  
Culture Cell ◽  
Antiviral Resistance ◽  
Tissue Culture Cell

Studies on the Mechanism of Substrate Induction and L-Cyst(e)ine Repression of Alkaline Phosphatase in Mammalian Cell Cultures

1967 ◽  
Vol 2 (4) ◽  
pp. 545-555
Author(s):  
M. J. GRIFFIN ◽  
R. P. COX
Keyword(s):  
Tissue Culture ◽  
Alkaline Phosphatase ◽  
Cell Cultures ◽  
Phosphate Esters ◽  
Kidney Cell Line ◽  
Monkey Kidney Cell ◽  
African Green Monkey Kidney ◽  
Mammalian Cell Cultures ◽  
Green Monkey ◽  
Substrate Induction

The mechanisms of substrate induction and L-cyst(e)ine repression of alkaline phosphatase were studied in tissue culture using an established African green monkey kidney cell line (BS-C-I). L-Cyst(e)ine repression and substrate induction are mutually antagonistic. Evidence is presented which suggests that the increase in alkaline phosphatase levels induced by mono-phosphate esters may in part be due to protection of the enzyme from cellular degradation, while L-cyst(e)ine is believed to act either by repressing the synthesis of the enzyme or by selectively increasing its catabolism.

Alkaline phosphatase activity from human osteosarcoma cell line SaOS-2: an isoenzyme standard for quantifying skeletal alkaline phosphatase activity in serum.

1989 ◽  
Vol 35 (2) ◽  
pp. 223-229 ◽  
Author(s):  
J R Farley ◽  
E Kyeyune-Nyombi ◽  
N M Tarbaux ◽  
S L Hall ◽  
D D Strong
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Cell Lines ◽  
Alkaline Phosphatase Activity ◽  
Osteosarcoma Cell ◽  
Kinetic Assay ◽  
Human Osteosarcoma ◽  
Alp Activity ◽  
Human Osteosarcoma Cell ◽  
Skeletal Alkaline Phosphatase

Abstract Earlier we described a kinetic assay for quantifying skeletal alkaline phosphatase (ALP) isoenzyme activity in serum. The precision of the assay depends on including ALP standards for the skeletal, hepatic, intestinal, and placental isoenzymes. We wondered whether human osteosarcoma cells could provide an efficient alternative to human bone or Pagetic serum as a source of the skeletal ALP standard. ALP activities prepared from five human osteosarcoma cell lines were compared with a bone-derived ALP standard with respect to heat stability and sensitivity to chemical effectors. Two of the cell lines (SaOS-2 and TE-85) contained ALP activities that resembled the bone-derived standard. We selected SaOS-2 cells for additional evaluation (as a potential source of isoenzyme standard), because they contained 40-50 times more ALP activity than did the TE-85 cells. To include the SaOS-2 cell-derived ALP activity in the quantitative isoenzyme assay, we diluted the enzyme in a solution containing heat-inactivated (i.e., ALP-negative) human serum. Surprisingly, this dilution caused a 60-125% increase in maximum enzyme activity. In the quantitative assay of ALP isoenzyme in serum, the SaOS-2 derived ALP was indistinguishable from the serum skeletal ALP standard, with respect to the above criteria and assay variations. Evidently ALP from SaOS-2 cells is suited as a standard for measuring skeletal ALP activity in this assay.

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