casein-kinase-ii and Hypophosphatemia--Familial

casein-kinase-ii has been researched along with Hypophosphatemia--Familial* in 1 studies

Other Studies

1 other study(ies) available for casein-kinase-ii and Hypophosphatemia--Familial

Article	Year
Skeletal casein kinase activity defect in the HYP mouse. Calcified tissue international, 1997, Volume: 61, Issue:3 The Hyp mouse, a model for human X-linked hypophosphatemia (XLH), is characterized by phosphate wasting and defective mineralization. Since osteopontin (OPN) is considered pivotal for biological mineralization, we examined the biosynthesis of OPN in osteoblasts of +/Y and Hyp/Y mice. Immunoprecipitation analyses using a specific antibody to OPN revealed that Hyp/Y and +/Y osteoblasts secrete similar levels of OPN as determined by [35S]-methionine biosynthetic labeling, but a reduced phosphorylation was noted after 32P-PO4 biosynthetic labeling. Northern blot hybridization analysis of +/Y and Hyp/Y mice osteoblast mRNAs, using a cDNA probe for mouse OPN, revealed no difference in the steady state levels of osteopontin mRNA. Analysis of casein kinase II activity in +/Y and Hyp/Y mice osteoblast, kidney, heart and liver membrane fractions revealed that casein kinase II activity in the Hyp/Y mice osteoblasts and kidney is only 35%-50%, respectively, of that of the +/Y mice tissues. The accumulated data are consistent with a post-translation defect in the Hyp/Y mouse osteoblast which results in the under-phosphorylation of osteopontin and subsequent under-mineralization of bone matrix. Topics: Animals; Casein Kinase II; Cells, Cultured; Disease Models, Animal; Hypophosphatemia, Familial; Kidney; Liver; Mice; Mice, Mutant Strains; Myocardium; Osteoblasts; Osteopontin; Phosphoproteins; Protein Serine-Threonine Kinases; Sialoglycoproteins	1997

Article

Year

Skeletal casein kinase activity defect in the HYP mouse.

Calcified tissue international, 1997, Volume: 61, Issue:3

The Hyp mouse, a model for human X-linked hypophosphatemia (XLH), is characterized by phosphate wasting and defective mineralization. Since osteopontin (OPN) is considered pivotal for biological mineralization, we examined the biosynthesis of OPN in osteoblasts of +/Y and Hyp/Y mice. Immunoprecipitation analyses using a specific antibody to OPN revealed that Hyp/Y and +/Y osteoblasts secrete similar levels of OPN as determined by [35S]-methionine biosynthetic labeling, but a reduced phosphorylation was noted after 32P-PO4 biosynthetic labeling. Northern blot hybridization analysis of +/Y and Hyp/Y mice osteoblast mRNAs, using a cDNA probe for mouse OPN, revealed no difference in the steady state levels of osteopontin mRNA. Analysis of casein kinase II activity in +/Y and Hyp/Y mice osteoblast, kidney, heart and liver membrane fractions revealed that casein kinase II activity in the Hyp/Y mice osteoblasts and kidney is only 35%-50%, respectively, of that of the +/Y mice tissues. The accumulated data are consistent with a post-translation defect in the Hyp/Y mouse osteoblast which results in the under-phosphorylation of osteopontin and subsequent under-mineralization of bone matrix.

Topics: Animals; Casein Kinase II; Cells, Cultured; Disease Models, Animal; Hypophosphatemia, Familial; Kidney; Liver; Mice; Mice, Mutant Strains; Myocardium; Osteoblasts; Osteopontin; Phosphoproteins; Protein Serine-Threonine Kinases; Sialoglycoproteins

1997