Evidence map›Paper›PMID 15906148›Full record

ArticleJournal of bioenergetics and biomembranes2005

Retinoylation reaction of proteins in Leydig (TM-3) cells.

Erika Cione, Paola Tucci, Adele Chimento, Vincenzo Pezzi, Giuseppe Genchi

Abstract read
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In one paragraph

Article in Journal of bioenergetics and biomembranes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 8 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Erika CioneDipartimento Farmaco-Biologico, Edificio Polifunzionale, Università della Calabria, 87036 Rende (Cosenza), Italy.
Paola Tucci
Adele Chimento
Vincenzo Pezzi
Giuseppe Genchi
University of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The covalent incorporation of [(3)H]all-trans-retinoic acid into proteins has been studied in Leydig (TM-3) cells. The maximum retinoylation activity of Leydig cells proteins was 570+/- 27 fmoles/8 x 10(4) cells at 37( composite function)C. About 95% of [(3)H]retinoic acid was trichloroacetic acid-soluble after proteinase-K digestion or after hydrolysis with hydroxylamine. Thus, retinoic acid is most probably linked to proteins as a thiol ester. The retinoylation process was inhibited by 13-cis-retinoic acid and 9-cis-retinoic acid with IC(50) values of 0.6 and 1.2 microM respectively. Dibutyryl-cAMP and forskolin increased the retinoylation activity by 75 and 81% at 500 and 25 microM respectively. Also hCG increased the retinoylation binding activity of 110% at 250 ng/mL. After cycloheximide treatment of the Leydig cells the binding activity of [(3)H]RA was about the same that in the control, suggesting that the bond occurs on proteins in pre-existing cells. Retinoylation was not inhibited by high concentrations of palmitic or myristic acids (500 microM); on the contrary, there was an increase of the binding activity of about 60 and 50% respectively.

Indexed as

AnimalsCell LineKineticsLeydig CellsMaleMiceMice, Inbred BALB CProtein BindingProteinsRadioisotope Dilution TechniqueTretinoinTritiumProteinsTretinoinTritium

Identifiers

PMID15906148
OpenAlexW2084651826

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.