RESUMEN
A custom CGH microarray that covers the SOX9 regulatory region. Log2 ratio scatterplot showing individual data points. Blue box highlights copy number gain with 3' breakpoint region magnified.
Asunto(s)
Duplicación de Gen , Cariotipo , Secuencias Reguladoras de Ácidos Nucleicos , Factor de Transcripción SOX9/genética , Desarrollo Sexual/genética , Enfermedades Testiculares/diagnóstico , Enfermedades Testiculares/genética , Adolescente , Biomarcadores , Estudios de Asociación Genética , Humanos , Masculino , Especificidad de Órganos/genética , FenotipoRESUMEN
Matrix Gla protein plays an essential role in preventing the calcification of blood vessel walls, cartilage and other tissues. We report here the primary structure of chicken matrix Gla protein as deduced from the cDNA sequence. The avian protein exhibited the characteristic motifs previously identified in the mammalian proteins, but its amino acid sequence shared only 51-56% identity with the latter proteins. Moreover, a region proposed to function as binding site for gamma-carboxylase in the mammalian proteins was poorly conserved in the chicken protein. Our sequence data should be helpful in the design of mutational analyses which are intended to characterize functional interactions of matrix Gla proteins with other proteins.
Asunto(s)
Proteínas de Unión al Calcio/genética , ADN Complementario/genética , Proteínas de la Matriz Extracelular , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Sitios de Unión , Proteínas de Unión al Calcio/química , Embrión de Pollo , Clonación Molecular , Regulación del Desarrollo de la Expresión Génica , Datos de Secuencia Molecular , Especificidad de Órganos , ARN Mensajero/análisis , Homología de Secuencia de Aminoácido , Proteína Gla de la MatrizRESUMEN
By subtractive cDNA cloning we have identified a novel constituent of chicken cartilage termed matrilin-3. This constituent is encoded by a mRNA of 2.2 kbp whose expression is restricted to cartilaginous tissues. The predicted protein is composed of 452 amino acids with a molecular mass of 49 kDa. It contains a single von Willebrand factor A-like domain, four epidermal growth factor-like repeats and an alpha-helical region which may induce the formation of oligomers via a coiled-coil. The primary structure is similar to that of matrilin-1 which is also expressed in a cartilage-specific manner. This similarity suggests that the genes for the two proteins may have evolved from a common ancestor by gene duplication.
Asunto(s)
Cartílago/química , Proteínas de la Matriz Extracelular/química , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Northern Blotting , Cartílago/citología , Embrión de Pollo , Clonación Molecular , Proteínas de la Matriz Extracelular/análisis , Proteínas de la Matriz Extracelular/genética , Humanos , Hibridación in Situ , Proteínas Matrilinas , Datos de Secuencia Molecular , ARN Mensajero/análisis , Alineación de Secuencia , Análisis de Secuencia de ADNRESUMEN
We have isolated a cDNA clone for human matrilin-3 from a cartilage-specific cDNA library. The polypeptide predicted from the nucleotide sequence of this clone shared 83% identity with matrilin-3 from mouse and 61% with that from chicken. It was composed of 486 amino acid residues that were arranged in seven domains: a signal peptide, a von Willebrand factor A domain, four EGF repeats, and an alpha-helical region. The gene for human matrilin-3 (MATN3) was assigned to chromosome region 2p24-p23. The corresponding mRNA of 2.8 kb was expressed in every type of cartilage investigated thus far. It was also produced in vitro by primary chondrocytes isolated from articular cartilage. However, dedifferentiated chondrocytes of the third passage did not express it at all. Matrilin-3 might therefore serve as a marker for the differentiation state of chondrocytes.