TY - JOUR
T1 - Expression and processing of the activin-A/erythroid differentiation factor precursor
T2 - A member of the transforming growth factor-β superfamily
AU - Huylebroeck, Danny
AU - Van Nimmen, Kristien
AU - Waheed, Abdul
AU - Von Figura, Kurt
AU - Marmenout, Anne
AU - Fransen, Lucie
AU - De Waele, Peter
AU - Jaspar, Jean Marie
AU - Franchimont, Paul
AU - Stunnenberg, Henk
AU - Van Heuverswijn, Hugo
PY - 1990/8
Y1 - 1990/8
N2 - The biosynthesis and intracellular processing of the polypeptide precursor of the βA-chain of the fertility hormone inhibin were assessed by infecting a wide spectrum of cell types with a recombinant vaccinia virus. Most cell lines, including follicular granulosa cells, secrete both prohormone and mature hormone as homodimers (activin) composed of disulfidelinked subunits of 54 kDa (proactivin-A) and 14 KDa (activin-A), respectively, and a small amount of prohormone-mature hormone heterodimers. Mature activin is secreted from mouse pituitary cells (AtT-20), while pig kidney cells [PK(15)] secrete mostly proactivin. More prohormone is secreted in the presence of NH4Cl, suggesting that prohormone processing is facilitated by low pH. Proactivin-A is not a ligand for the mannose-6-phosphate/insulin growth factor-II receptor. The recombinant activin stimulates FSH release from pituitary cells and differentiates erythroleukemia cell lines in vitro.
AB - The biosynthesis and intracellular processing of the polypeptide precursor of the βA-chain of the fertility hormone inhibin were assessed by infecting a wide spectrum of cell types with a recombinant vaccinia virus. Most cell lines, including follicular granulosa cells, secrete both prohormone and mature hormone as homodimers (activin) composed of disulfidelinked subunits of 54 kDa (proactivin-A) and 14 KDa (activin-A), respectively, and a small amount of prohormone-mature hormone heterodimers. Mature activin is secreted from mouse pituitary cells (AtT-20), while pig kidney cells [PK(15)] secrete mostly proactivin. More prohormone is secreted in the presence of NH4Cl, suggesting that prohormone processing is facilitated by low pH. Proactivin-A is not a ligand for the mannose-6-phosphate/insulin growth factor-II receptor. The recombinant activin stimulates FSH release from pituitary cells and differentiates erythroleukemia cell lines in vitro.
UR - https://www.scopus.com/pages/publications/0025084588
M3 - Article
C2 - 1963471
AN - SCOPUS:0025084588
SN - 0888-8809
VL - 4
SP - 1153
EP - 1165
JO - Molecular Endocrinology
JF - Molecular Endocrinology
IS - 8
ER -