Evidence map›Paper›PMID 28036279›Full record

ArticleOncotarget2017

Proteins that interact with calgranulin B in the human colon cancer cell line HCT-116.

Jae Kyung Myung, Seung-Gu Yeo, Kyung Hee Kim, Kwang-Soo Baek, Daye Shin, Jong Heon Kim, Jae Youl Cho, Byong Chul Yoo

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 9 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

8 authors at 3 institutions in 1 country.

Jae Kyung MyungDepartment of System Cancer Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang, Korea.
Seung-Gu YeoDepartment of Radiation Oncology, Soonchunhyang University College of Medicine, Cheonan, Korea.
Kyung Hee KimColorectal Cancer Branch, Research Institute, National Cancer Center, Goyang, Korea.
Kwang-Soo BaekColorectal Cancer Branch, Research Institute, National Cancer Center, Goyang, Korea.
Daye ShinDepartment of System Cancer Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang, Korea.
Jong Heon KimDepartment of System Cancer Science, Graduate School of Cancer Science and Policy, National Cancer Center, Goyang, Korea.
Jae Youl ChoDepartment of Genetic Engineering, Sungkyunkwan University, Suwon, Korea.
Byong Chul YooColorectal Cancer Branch, Research Institute, National Cancer Center, Goyang, Korea.
National Cancer Center · KRSoonchunhyang University · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calgranulin B is released from immune cells and can be internalized into colon cancer cells to prevent proliferation. The present study aimed to identify proteins that interact with calgranulin B to suppress the proliferation of colon cancer cells, and to obtain information on the underlying anti-tumor mechanism(s) of calgranulin B. Calgranulin B expression was induced in colon cancer cell line HCT-116 by infection with calgranulin B-FLAG expressing lentivirus, and it led to a significant suppression of cell proliferation. Proteins that interacted with calgranulin B were obtained by immunoprecipitation using whole homogenate of lentivirus-infected HCT-116 cells which expressing calgranulin B-FLAG, and identified using liquid chromatography-mass spectrometry/mass spectrometry analysis. A total of 454 proteins were identified that potentially interact with calgranulin B, and most identified proteins were associated with RNA processing, post-transcriptional modifications and the EIF2 signaling pathway. Direct interaction of calgranulin B with flotillin-1, dynein intermediate chain 1, and CD59 glycoprotein has been confirmed, and the molecules N-myc proto-oncogene protein, rapamycin-insensitive companion of mTOR, and myc proto-oncogene protein were shown to regulate calgranulin B-interacting proteins. Our results provide new insight and useful information to explain the possible mechanism(s) underlying the role of calgranulin B as an anti-tumor effector in colon cancer cells.

Indexed as

Protein Interaction MapsCalgranulin BCD59 AntigensCell ProliferationChromatography, High Pressure LiquidColonic NeoplasmsCytoplasmic DyneinsHCT116 CellsHumansMembrane ProteinsN-Myc Proto-Oncogene ProteinProteomicsProto-Oncogene MasProto-Oncogene Proteins c-mycSignal TransductionTandem Mass SpectrometryCalgranulin BCD59 AntigensCD59 protein, humanCytoplasmic DyneinsflotillinsMAS1 protein, humanMembrane ProteinsMTOR protein, humanMYCN protein, humanMYC protein, humanN-Myc Proto-Oncogene ProteinProto-Oncogene MasProto-Oncogene Proteins c-mycTOR Serine-Threonine Kinasesanti-tumor effectcalgranulin Bcolon cancerHCT-116S100A9

Identifiers

PMID28036279
PMCPMC5351672
OpenAlexW2564757276

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.