Evidence map›Paper›PMID 18474603›Full record

ArticleThe Journal of biological chemistry2008

Prothyrotropin-releasing hormone targets its processing products to different vesicles of the secretory pathway.

Mario Perello, Ronald Stuart, Eduardo A Nillni

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.6field-weighted citation impact, top 42% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

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  17. Mechanisms by which the orexigen NPY regulates anorexigenic α-MSH and TRH.American journal of physiology. Endocrinology and metabolism · 2013
    Article
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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

3 authors at 2 institutions in 1 country.

Mario PerelloDivision of Endocrinology, Department of Medicine, The Warren Alpert Medical School of Brown University/Rhode Island Hospital, Providence, RI 02903, USA.
Ronald Stuart
Eduardo A Nillni
Brown University · USRhode Island Hospital · US

Funding

PROTRH GENE TRANSCRIPTION AND BIOSYNTHESIS BY LEPTINR01DK058148 · NIDDK · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI NILLNI, EDUARDO A. · 2000 to 2008
$2.4M
ProTRH sorting to the regulated secretory pathwayR01NS045231 · NINDS · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI NILLNI, EDUARDO A · 2003 to 2006
$1.0M
NIDDK NIH HHS R01 DK 58148NINDS NIH HHS R01 NS 045231
6 · The paper itself

Abstract

Prothyrotropin-releasing hormone (pro-TRH) is initially cleaved by the prohormone convertase-1/3 (PC1/3) in the trans-Golgi network generating N- and C-terminal intermediate forms that are then packed into secretory vesicles. However, it is not known whether these peptides are differentially sorted within the secretory pathway. This is of key importance because the processing products of several prohormones fulfill different biological functions. Using AtT20 cells stably transfected with prepro-TRH cDNA, we found that two specific N- and C-terminal peptides were located in different vesicles. Furthermore, the C-terminal pro-TRH-derived peptides were more efficiently released in response to KCl and norepinephrine, a natural secretagogue of TRH. Similar sorting and secretion of N- and C-terminal peptides occurs in vivo. When we blocked the initial proteolytic processing by a mutagenic approach, the differential sorting and secretion of these peptides were prevented. In summary, our data show that pro-TRH-derived peptides are differentially sorted within the secretory pathway and that the initial cleavage in the trans-Golgi network is key to this process. This could be a common mechanism used by neuroendocrine cells to regulate independently the secretion of different bioactive peptides derived from the same gene product.

Indexed as

AnimalsCell LineHypothalamusMaleMicroscopy, ImmunoelectronPeptide FragmentsProtein PrecursorsPyrrolidonecarboxylic AcidRatsRats, Sprague-DawleyThyrotropin-Releasing HormonePeptide FragmentsProtein Precursorspro-thyrotropin releasing hormonePyrrolidonecarboxylic AcidThyrotropin-Releasing Hormone

Identifiers

PMID18474603
PMCPMC2459294
OpenAlexW2015509791

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.