Evidence map›Paper›PMID 9971741›Full record

ArticleThe Journal of cell biology1999

Induction of integral membrane PAM expression in AtT-20 cells alters the storage and trafficking of POMC and PC1.

G D Ciccotosto, M R Schiller, B A Eipper, R E Mains

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Germline loss-of-functionmedRxiv : the preprint server for health sciences · 2023
    Article
  2. Germline loss-of-functionFrontiers in endocrinology · 2023
    Article
  3. Peptidylglycine α-amidating monooxygenase is required for atrial secretory granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Article
  5. Review
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  9. Article
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  12. POMC Neurons: From Birth to Death.Annual review of physiology · 2017
    Review
  13. Article
  14. Article
  15. Article
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  20. Review
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

4 authors at 2 institutions in 1 country.

G D CiccotostoDepartments of Neuroscience and Physiology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
M R Schiller
B A Eipper
R E Mains
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR01DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, MAINS, RICHARD E · 1986 to 2019
$7.3M
Cell Biology of Bioactive Peptide SecretionR56DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAINS, RICHARD E · 2008 to 2008
$303k
REGULATED ENDOCRINE ER PROTEIN AFFECTS POMC PROCESSINGR03DA010478 · NIDA · JOHNS HOPKINS UNIVERSITY · PI SCHILLER, MARTIN R · 1996 to 1997
–
CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR37DK032948 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MAINS, RICHARD E · 1990 to 1998
–
NIDA NIH HHS DA10478NIDDK NIH HHS DK32948NIDDK NIH HHS R01 DK032948NIDDK NIH HHS R56 DK032948
6 · The paper itself

Abstract

Peptidylglycine alpha-amidating monooxygenase (PAM) is an essential enzyme that catalyzes the COOH-terminal amidation of many neuroendocrine peptides. The bifunctional PAM protein contains an NH2-terminal monooxygenase (PHM) domain followed by a lyase (PAL) domain and a transmembrane domain. The cytosolic tail of PAM interacts with proteins that can affect cytoskeletal organization. A reverse tetracycline-regulated inducible expression system was used to construct an AtT-20 corticotrope cell line capable of inducible PAM-1 expression. Upon induction, cells displayed a time- and dose-dependent increase in enzyme activity, PAM mRNA, and protein. Induction of increased PAM-1 expression produced graded changes in PAM-1 metabolism. Increased expression of PAM-1 also caused decreased immunofluorescent staining for ACTH, a product of proopiomelanocortin (POMC), and prohormone convertase 1 (PC1) in granules at the tips of processes. Expression of PAM-1 resulted in decreased ACTH and PHM secretion in response to secretagogue stimulation, and decreased cleavage of PC1, POMC, and PAM. Increased expression of a soluble form of PAM did not alter POMC and PC1 localization and metabolism. Using the inducible cell line model, we show that expression of integral membrane PAM alters the organization of the actin cytoskeleton. Altered cytoskeletal organization may then influence the trafficking and cleavage of lumenal proteins and eliminate the ability of AtT-20 cells to secrete ACTH in response to a secretagogue.

Indexed as

Multienzyme ComplexesProprotein Convertase 1ActinsAdrenocorticotropic HormoneAnimalsAspartic Acid EndopeptidasesBiological Transport, ActiveCell LineCytoskeletonDose-Response Relationship, DrugDoxycyclineEnzyme InductionGene ExpressionMiceMixed Function OxygenasesModels, BiologicalActinsAdrenocorticotropic HormoneAspartic Acid EndopeptidasesDoxycyclineMixed Function OxygenasesMultienzyme ComplexesPcsk1 protein, mousepeptidylglycine monooxygenasePro-OpiomelanocortinProprotein Convertase 1Proprotein ConvertasesRNA, Messenger

Identifiers

PMID9971741
PMCPMC2132922
OpenAlexW2143358122

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.