ArticleEndocrine2001
Prostaglandin F2alpha-activated protein kinase Calpha phosphorylates myristoylated alanine-rich C kinase substrate protein in bovine luteal cells.
Article in Endocrine, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Prostaglandin F2alpha represses IGF-I-stimulated IRS1/phosphatidylinositol-3-kinase/AKT signaling in the corpus luteum: role of ERK and P70 ribosomal S6 kinase.Molecular endocrinology (Baltimore, Md.) · 2010Article
- MARCKS regulation of mucin secretion by airway epithelium in vitro: interaction with chaperones.American journal of respiratory cell and molecular biology · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prostaglandin F2alpha (PGF2alpha)-induced secretion of oxytocin by the bovine corpus luteum involves the phosphorylation of a unique protein kinase C (PKC) substrate, myristoylated alanine-rich C kinase substrate (MARCKS) protein. This study was conducted to determine the specific PKC isoform engaged in phosphorylation of MARCKS protein in bovine luteal cells. In experiment 1, dispersed luteal cells recovered from the corpus luteum on d 8 of the estrous cycle were preincubated with [32P] orthophosphate and then exposed to PGF2alpha alone or in combination with PKC inhibitors. Autoradiography and densitometry of Western blots revealed that MARCKS protein was phosphorylated by a conventional PKC (cPKC) isoform. Experiment 2 was conducted to identify the specific cPKC isoform that phosphorylates MARCKS protein in luteal cells. Corpora lutea were removed from control and PGF2alpha-treated heifers on d 8 of the cycle, and PKC isoforms associated with membrane and cytosolic fractions were determined. Treatment with PGF2alpha increased membrane concentrations of PKCalpha within 5 min after treatment (p < 0.005). Collectively, these data suggest that phosphorylation of MARCKS protein coinciding with oxytocin secretion is mediated by PKCalpha.
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Registered trials
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