| pubmed-article:1737754 | pubmed:abstractText | The Ch21 protein is one of the marker proteins whose synthesis and secretion by differentiating tibia chondrocytes is progressively increased during chicken embryogenesis (Descalzi-Cancedda, F., Manduca, P., Tacchetti, C., Fossa, P., Quarto, R. and Cancedda, R. (1988) J. Cell Biol. 107, 2455-2463). We report the corresponding full-length cDNA sequence and the complete primary structure of the protein, which contains a 20-residue signal peptide. The synthesis of the protein is directed by a 1450-base mRNA characterized by an unusually long 5'-untranslated leader sequence and is regulated only at the transcriptional level as shown by run-off transcription assays. During differentiation, maximal expression of the protein characterizes stage II hypertrophic chondrocytes. In situ hybridization on embryo sections reveals that the protein is expressed by several structures derived from the chondrogenic lineage and that, in addition, it is a major translational product in granulocytes. High cell density largely influences the expression of the Ch21 protein in chondrocyte cultures. When embryonic avian cells of different origin are grown to confluency, the expression of the Ch21 protein is observed in only some of the cell lines. Thus quiescence per se is not the primary factor determining the expression of the protein. | lld:pubmed |
