Prolactin (PRL) is a zinc-binding protein. I. Zinc interactions with monomeric PRL and divalent cation protection of intragranular PRL cysteine thiols

Endocrinology
M Y LorensonA M Walker

Abstract

PRL in secretory granules is osmotically inert. Previous studies by us and others have suggested that this is due in part to hormone oligomerization. Data suggest intermolecular disulfide bridges and/or intermolecular ionic interactions, as thiols, urea, and chelators increase monomerization of the majority of granule PRL. Because of the inhibitory effect of zinc on PRL release from isolated granules and the effects of zinc on the specific packing of PRL within granules, we examined the possibility that zinc contributed to the stability and/or oligomerization of intragranular PRL. To do this, we first analyzed zinc binding to purified monomeric rat PRL in solution. Zinc binding was demonstrated using the chromogenic chelator 5,5'-nitrilodibarbituric acid (murexide) and was confirmed by matrix-assisted, time of flight mass analysis. Because these spectrophotometric methods were not applicable for intragranular PRL studies, we tested the influence of zinc on granule PRL indirectly. As hormone free thiols were potentially formed during PRL oligomerization and storage, these were possible sites for hormone-divalent cation interactions. By derivatization of thiols with 4-vinyl pyridine and isolation of the carboxyterminal region of ...Continue Reading

Citations

Apr 23, 2011·FEBS Letters·Jeffrey L VoorheesCharles L Brooks
Jun 25, 2015·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·L A L MauésJ L M do Nascimento
May 5, 2007·Journal of Human Lactation : Official Journal of International Lactation Consultant Association·Caitlin E O'BrienFang Dong
Apr 1, 1997·FEBS Letters·E A PermyakovC L Brooks
Jun 3, 2004·The Journal of Nutrition·Winyoo ChowanadisaiBo Lönnerdal
Jul 5, 2001·Protein Expression and Purification·L StrokovskayaJ Michalik

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