Expression and processing of the activin-A/erythroid differentiation factor precursor: A memberof the transforming growthfactor-β superfamily

Danny Huylebroeck, Kristien Van Nimmen, Abdul Waheed, Kurt Von Figura, Anne Marmenout, Lucie Fransen, Peter De Waele, Jean Marie Jaspar, Paul Franchimont, Henk Stunnenberg, Hugo Van Heuverswijn

Onderzoeksoutput: Bijdrage aan tijdschriftArtikelpeer review

32 Citaten (Scopus)

Samenvatting

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 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)j secrete mostly proac-tivin. More prohormone is secreted in the presence of NH4CI, suggesting that prohormone processing is facilitated by low pH. Proactivin-A is not a ligand for the mannose-6-phosphate/insulin growth factor-ll receptor. The recombinant activin stimulates FSH release from pituitary cells and differentiates eryth-roleukemia cell lines in vitro.

Originele taal-2Engels
Pagina's (van-tot)1153-1165
Aantal pagina's13
TijdschriftMolecular Endocrinology
Volume4
Nummer van het tijdschrift8
DOI's
StatusGepubliceerd - aug. 1990
Extern gepubliceerdJa

Vingerafdruk

Duik in de onderzoeksthema's van 'Expression and processing of the activin-A/erythroid differentiation factor precursor: A memberof the transforming growthfactor-β superfamily'. Samen vormen ze een unieke vingerafdruk.

Citeer dit