HUMAN OSTEOSARCOMA CELLS, TUMORIGENIC IN NUDE-MICE, EXPRESS BETA(1)-INTEGRINS AND LOW-LEVELS OF ALKALINE-PHOSPHATASE ACTIVITY

1993 ◽  
Author(s):  
K SCOTLANDI ◽  
M SERRA ◽  
MC MANARA ◽  
P NANNI ◽  
G NICOLETTI ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Nude Mice ◽  
Alkaline Phosphatase Activity ◽  
Osteosarcoma Cells ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells ◽  
Low Levels

scholarly journals Presence and activity of alkaline phosphatase in two human osteosarcoma cell lines.

1989 ◽  
Vol 37 (7) ◽  
pp. 1069-1074 ◽  
Author(s):  
J C Randall ◽  
D C Morris ◽  
S Zeiger ◽  
K Masuhara ◽  
T Tsuda ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Membrane ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Osteogenic Sarcoma ◽  
Ultrastructural Level ◽  
Osteosarcoma Cell ◽  
Osteosarcoma Cells ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cells

The presence and activity of alkaline phosphatase in SAOS-2 and TE-85 human osteosarcoma cells grown in culture were examined at the ultrastructural level. A monoclonal antibody raised against purified human bone osteosarcoma alkaline phosphatase was used to localize the enzyme in cultures of the osteosarcoma cells. Similar cultures were analyzed for alkaline phosphatase activity using an enzyme cytochemical method with cerium as the capture agent. Alkaline phosphatase was immunolocalized at the light microscopic level in an osteogenic sarcoma and ultrastructurally on the SAOS-2 cell membrane and the enclosing membrane of extracellular vesicular structures close to the cells. In contrast, the TE-85 cells were characterized by the absence of all but a few traces of immunolabeling at the cell surface. Enzyme cytochemical studies revealed strong alkaline phosphatase activity on the outer surface of the SAOS-2 cell membrane. Much lower enzyme activity was observed in the TE-85 cells. The results support biochemical data from previous studies and confirm that SAOS-2 cells have a significantly greater concentration of alkaline phosphatase at the plasma membrane.

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.

Individual and combined effects of intact PTH, amino-terminal, and a series of truncated carboxyl-terminal PTH fragments on alkaline phosphatase activity in dexamethasone-treated rat osteoblastic osteosarcoma cells, ROS 17/2.8

1993 ◽  
Vol 128 (4) ◽  
pp. 367-372 ◽  
Author(s):  
Chizu Nakamoto ◽  
Hisamitsu Baba ◽  
Masaaki Fukase ◽  
Kiichiro Nakajima ◽  
Terutoshi Kimura ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Combined Effects ◽  
Osteosarcoma Cells ◽  
Intact Pth ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Carboxyl Terminal ◽  
Osteoblastic Osteosarcoma

The individual and combined effects of intact PTH, amino-terminal, and a series of truncated carboxyl-terminal PTH fragments on alkaline phosphatase activity were examined in dexamethasone-treated rat osteoblastic osteosarcoma cells ROS 17/2.8. Dexamethasone-induced alkaline phosphatase activity was inhibited not only by hPTH(1–84) and amino-terminal PTH fragment hPTH(1–34), but also by carboxyl-terminal PTH fragment hPTH(69–84) in a dose-related fashion. At 10−7 mol/1, hPTH(1–84) completely abolished dexamethasone-induced alkaline phosphatase activity, while hPTH(1–34) and hPTH(69–84) reduced alkaline phosphatase activity to 0.16±0.02 and 0.80±0.03 fold, respectively, of the control value obtained in the absence of PTH peptides. The combination of hPTH(1–34) and hPTH(69—84) resulted in reduction of alkaline phosphatase activity to the level obtained by hPTH(1-84). The shorter carboxyl-terminal PTH fragment hPTH(71–84) did not affect alkaline phosphatase activity or modulate the action of hPTH(1–34). The longer carboxyl-terminal PTH fragment hPTH(53-84) stimulated alkaline phosphatase activity up to 1.23±0.03 fold and partially blunted the inhibitory effect of hPTH(1–34) on alkaline phosphatase activity. These findings suggest that carboxyl-terminal PTH fragments could exert diverse effects on the target cells, depending on the length of deletion of amino-terminal amino acids of PTH molecule, and interact with amino-terminal PTH fragment. The two amino-terminal amino acids of hPTH(69–84) and the 53–68 portion of hPTH(53–84) might be responsible for the respective inhibitory and stimulatory effects of the peptides on alkaline phosphatase activity.

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