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At least 343 records · Page 19Linked to original sources
PubMed1996

ALP induction by beta-glycerophosphate during the non-mineralization phase in vitro.

beta-GP influences on rat osteoblast development at the early period of culture i.e., the non-mineralization phase, and changes with the different cell passages were investigated. Alkaline phosphatase (ALP) was chosen as a main object. Northern blot analysis revealed up to two-fold increase in the steady state level of ALP mRNA after stimulation of rat osteoblast with 10 mM beta-GP. Likewise, 10 mM beta-GP induced a 10-30% increase in ALP activity (P < 0.01) of early passages (1 to 4), but not of later passages (5 to 6). The beta-GP induced increase in ALP activity was totally inhibited by the protein synthesis inhibitor, cycloheximide (50 microM). beta-GP stimulation was found to be without effect on cell proliferation measured as 3H-thymidine incorporation. It is concluded that beta-GP has no effect on proliferation but induces an increase in both mRNA level and activity of ALP in the non-mineralization phase of cultures of fetal rat calvarial cells, which lasts for several passages but will disappear in older cultures.

Alkaline Phosphatase↗
PubMed1997

Stable transfection of nonosteogenic cell lines with tissue nonspecific alkaline phosphatase enhances mineral deposition both in the presence and absence of beta-glycerophosphate: possible role for alkaline phosphatase in pathological mineralization.

It is documented that alkaline phosphatase (AP) plays an important role in bone mineralization. Considering that TN-AP is expressed in periodontal ligament fibroblasts, renal epithelial cells, and vascular endothelial cells, and that TN-AP is both a calcium-/phosphate-binding protein and a phosphohydrolytic enzyme, we hypothesize that membrane-bound AP also plays an important role in the initiation of physiological and pathological mineralizations in tissues other than bone and cartilage. To test this hypothesis, nonosteoblast cell lines, including a fibroblast line, a renal epithelial line, and a capillary endothelial line, were stably transfected to express high levels of rat bone AP on their cell surfaces. These rat bone AP-expressing cells were then cultured on filter membranes in the presence or absence of beta-glycerol phosphate. von Kossa staining for calcium phosphate and transmission electron microscopy with electron diffraction analysis for minerals were employed to investigate the effect of membrane AP on extracellular calcium phosphate mineralization. Our results indicated that AP expression on these nonosteoblast-like cell surfaces have induced extracellular hydroxyapatite (HAP) mineralization. Our findings support the concept that membrane-bound AP contributes to extracellular apatitic mineralization by mechanisms that do not necessarily involve its hydrolase activity. They also suggest that AP might be important for the initiation of pathological mineralization in nonosteogenic tissues.

Alkaline Phosphatase↗