Molecular cloning, tissue distribution and quantitative analysis of two proopiomelanocortin mRNAs in Japanese flounder (Paralichthys olivaceus)

Annotation and analysis of expressed sequence tags (ESTs) from Chinese sturgeon (Acipenser sinensis) pituitary cDNA library

“…Acipenseriform POMC A and POMC B formed two distinct subclades with 100% bootstrap support. Some amphibians and fish species are thought to have undergone chromosome duplication resulting in two POMC genes (Kim et al, 2009). A similar pattern was also observed for the GtH-α gene.…”

“…GH was identified as two contigs of 56 individuals and 8 ESTs. The results revealed that pomc should be greatly expressed in the pituitary of Chinese sturgeon (Table 3), coincident with a wide range of physiological functions of POMC-derived peptides, such as stress and immune responses, skin pigmentation, sexual behavior, cardiovascular regulation, and energy homeostasis (Kim et al, 2009). Five hormone-related genes (all identified as singletons) were gonadotropin-releasing hormone receptor I (GnRHR), carboxypeptidase H (cpH), peptidylprolyl isomerase B (ppiB), stathmin-like 3 (stmn3), and neuroendocrine protein 7B2 precursor.…”

Subfunctionalization of POMC paralogues in Senegalese sole (Solea senegalensis)

“…The pomc gene is well-conserved among vertebrates, and the presence of two paralogues has been reported for carp, zebrafish and flounder [2,15,20,31]. Duplications are not uncommon in the evolution of the pomc gene family.…”

Molecular characterization and functional analysis of a protease-related protein in Chang-liver cells

“…To study the ADAMs or their related proteins involved in Chang-liver cells under abnormal conditions, such as being treated by ATP in modified Hanks buffer, it is necessary to clone the full-length cDNAs of them, for example, to screen the target gene from cDNA library (11,12). We constructed the cDNA expression library of Chang-liver cells treated by the modified Hanks buffer containing ATP (13), then screened the cDNA library with common ADAMs antibody raised against a conserved region from the metalloprotease domain of several known ADAMs molecules and predicted to recognize most ADAMs and ADAM related proteins.…”