Evidence map›Paper›PMID 8458870›Full record

ArticleThe Journal of cell biology1993

COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells.

S L Milgram, R E Mains, B A Eipper

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.7field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 80 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

3 authors at 2 institutions in 1 country.

S L MilgramNeuroscience Department, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
R E Mains
B A Eipper
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
CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR37DK032948 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MAINS, RICHARD E · 1990 to 1998
–
NIDA NIH HHS DA-00097NIDA NIH HHS DA-00098NIDDK NIH HHS DK-32948
6 · The paper itself

Abstract

Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the COOH-terminal amidation of bioactive peptides through a two step reaction catalyzed by separate enzymes contained within the PAM precursor. To characterize the trafficking of integral membrane PAM proteins in neuroendocrine cells, we have generated stable AtT-20 cell lines expressing full length and COOH-terminally truncated integral membrane PAM proteins. Full length integral membrane PAM was present on the cell surface in low but detectable amounts and PAM proteins which reached the cell surface were rapidly internalized but not immediately degraded in lysosomes. Internalized PAM complexed with PAM antibody was found in a subcellular compartment which overlapped with internalized transferrin and with structures binding WGA. Thus the punctate juxtanuclear staining of full length PAM represents PAM in endosomes. Endoproteolytic processing of full length PAM-1 and PAM-2 resulted in the secretion of soluble PAM proteins; the secretion of these soluble PAM proteins was stimulus dependent. Although some of the truncated PAM protein was also processed and stored in AtT-20 cells, much of the expressed protein was redistributed to the plasma membrane. Soluble proteins not observed in large amounts in cells expressing full length PAM were released from the surface of cells expressing truncated PAM and little internalization of truncated integral membrane PAM was observed. Thus, the COOH-terminal domain of PAM contains information important for its trafficking within the regulated secretory pathway as well as information necessary for its retrieval from the cell surface.

Indexed as

Multienzyme ComplexesProtein Processing, Post-TranslationalAnimalsBase SequenceBiological TransportCell LineDNAFluorescent Antibody TechniqueKineticsMixed Function OxygenasesMolecular Sequence DataPituitary Gland, AnteriorPrecipitin TestsProtein PrecursorsProtein Sorting SignalsTransfectionDNAMixed Function OxygenasesMultienzyme Complexespeptidylglycine monooxygenaseProtein PrecursorsProtein Sorting Signals

Identifiers

PMID8458870
PMCPMC2119776
OpenAlexW2161767563

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.