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Articles by K Miyazono
Total Records ( 2 ) for K Miyazono
  K Miyazono , Y Kamiya and M. Morikawa
 

Bone morphogenetic proteins (BMPs) exhibit broad spectra of biological activities in various tissues, including bone, cartilage, blood vessels, heart, kidney, neurons, liver and lung. BMPs are members of the transforming growth factor-β (TGF-β) family that bind to type II and type I serine-threonine kinase receptors, and transduce signals through Smad and non-Smad signalling pathways. Recent findings have revealed that BMP signalling is finely tuned by various mechanisms in both positive and negative fashions. Perturbations of BMP signalling pathways are linked to a wide variety of clinical disorders, including vascular diseases, skeletal diseases and cancer. Administration of recombinant BMP ligands and increasing endogenous expression of BMPs provide therapeutic effects on some diseases. The recent development of BMP receptor inhibitors may also prove useful for some clinical diseases induced by hyperactivation of the BMP signalling pathways.

  M Nagata , S Nagata , K Yuki , K Isogaya , M Saitoh , K Miyazono and K. Miyazawa
 

c-Ski has been known to be phosphorylated at serine residue(s), which results in slower migration of c-Ski in SDS–polyacrylamide gel electrophoresis. The position(s) of phosphorylation, however, has not been determined. In the present study, we identified a phosphorylation site of c-Ski which affects its electrophoretic motility as serine 515 using MALDI–TOF mass spectrometry. A phosphorylation-resistant mutant, c-Ski S515A, did not exhibit a phosphatase-sensitive band shift. In addition, we confirmed that endogenous c-Ski is phosphorylated at serine 515, using a specific antibody. The phosphorylation status of c-Ski, however, does not appear to affect its stability or effects on TGF-β signalling. Identification of the phosphorylation site of c-Ski would allow us further examination of physiological significance of c-Ski phosphorylation.

 
 
 
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