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Title: Expression and processing of the activin-A/erythroid differentiation factor precursor: a member of the transforming growth factor-beta superfamily
Authors: Huylebroeck, Danny
Van Nimmen, K
Waheed, A
von Figura, K
Marmenout, A
Fransen, L
De Waele, Peter
Jaspar, J M
Franchimont, P
Stunnenberg, H #
Issue Date: Apr-1991
Series Title: Molecular endocrinology (Baltimore, Md.) vol:4 issue:8 pages:1153-65
Abstract: The biosynthesis and intracellular processing of the polypeptide precursor of the beta A-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 disulfide-linked 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.
ISSN: 0888-8809
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
# (joint) last author

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