ArticleDiabetologia1986
Polyamine-enhanced casein kinase II in mouse pancreatic islets.
Article in Diabetologia, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 13 citations in OpenAlex.
- A critical role for CK2 in cytokine-induced activation of NFκB in pancreatic β cell death.Endocrine · 2014Article
- A novel regulatory mechanism for trimeric GTP-binding proteins in the membrane and secretory granule fractions of human and rodent beta cells.The Biochemical journal · 1996Article
- Polyamines and insulin production in isolated mouse pancreatic islets.The Biochemical journal · 1988Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The occurrence of polyamine-stimulated protein kinase (casein kinase II) in cytosol of mouse pancreatic islets was investigated. Islet protein phosphorylation was enhanced by spermidine, spermine, lysine-rich histone and polylysine; the major endogenous substrates in the cytosol were three proteins of Mr 50,000, 55,000 and 100,000. Cadaverine and putrescine were without effects. A Mr 100,000 protein is a major substrate for Ca2+-calmodulin-dependent protein kinase, and Mr 50,000 and 55,000 proteins are substrates for cyclic adenosine 3',5'-cyclic monophosphate (AMP) dependent protein kinase in mouse islets. However, neither cyclic-AMP-dependent protein kinase inhibitor nor trifluoperazine inhibited polyamine-enhanced protein phosphorylation. Both basal and polyamine-enhanced protein phosphorylation patterns were identical when either [gamma-32P] adenosine 5'-triphosphate (ATP) or [gamma-32P] guanosine 5'-triphosphate (GTP) was used as phosphate donors, indicative of the presence of a polyamine-stimulated casein kinase II in pancreatic islets. It is suggested that polyamines and polyamine-enhanced casein kinase II activity may have an important role in regulation of protein phosphorylation in pancreatic islets.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.