Evidence map›Paper›PMID 33542717›Full record

ArticleFrontiers in immunology2020

Membrane Interactome of a Recombinant Fragment of Human Surfactant Protein D Reveals GRP78 as a Novel Binding Partner in PC3, a Metastatic Prostate Cancer Cell Line.

Gargi Thakur, Gajanan Sathe, Indra Kundu, Barnali Biswas, Poonam Gautam, Saad Alkahtani, Susan Idicula-Thomas, Ravi Sirdeshmukh, Uday Kishore, Taruna Madan

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 16 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

10 authors at 6 institutions in 3 countries.

Gargi ThakurDepartment of Innate Immunity, Indian Council of Medical Research (ICMR)-National Institute for Research in Reproductive Health, Mumbai, India.
Gajanan SatheInstitute of Bioinformatics, Bengaluru, India.
Indra KunduBiomedical Informatics Centre, ICMR-National Institute for Research in Reproductive Health, Mumbai, India.
Barnali BiswasDepartment of Innate Immunity, Indian Council of Medical Research (ICMR)-National Institute for Research in Reproductive Health, Mumbai, India.
Poonam GautamLaboratory of Molecular Oncology, ICMR-National Institute of Pathology, New Delhi, India.
Saad AlkahtaniDepartment of Zoology, College of Science, King Saud University, Riyadh, Saudi Arabia.
Susan Idicula-ThomasBiomedical Informatics Centre, ICMR-National Institute for Research in Reproductive Health, Mumbai, India.
Ravi SirdeshmukhInstitute of Bioinformatics, Bengaluru, India.
Uday KishoreBiosciences, College of Health, Medicine and Life Sciences, Brunel University London, Uxbridge, United Kingdom.
Taruna MadanDepartment of Innate Immunity, Indian Council of Medical Research (ICMR)-National Institute for Research in Reproductive Health, Mumbai, India.
National Institute for Research in Reproductive Health · INManipal Academy of Higher Education · INBrunel University of London · GBIndian Council of Medical Research · INKing Saud University · SANational Institute of Pathology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Surfactant protein-D (SP-D), a member of the collectin family has been shown to induce apoptosis in cancer cells. SP-D is composed of an N-terminal collagen-like domain and a calcium-dependent carbohydrate recognition domain (CRD). Recently, we reported that a recombinant fragment of human SP-D (rfhSP-D), composed of homotrimeric CRD region, induced intrinsic apoptotic pathway in prostate cancer cells. Here, we analyzed the membrane interactome of rfhSP-D in an androgen-independent prostate cancer cell line, PC3, by high resolution mass spectrometry and identified 347 proteins. Computational analysis of PPI network of this interactome in the context of prostate cancer metastasis and apoptosis revealed Glucose Regulated Protein of 78 kDa (GRP78) as an important binding partner of rfhSP-D. Docking studies suggested that rfhSP-D (CRD) bound to the substrate-binding domain of glycosylated GRP78. This was further supported by the observations that human recombinant GRP78 interfered with the binding of rfhSP-D to anti-SP-D polyclonal antibodies; GRP78 also significantly inhibited the binding of recombinant full-length human SP-D with a monoclonal antibody specific to the CRD in a dose-dependent manner. We conclude that the interaction with rfhSP-D is likely to interfere with the pro-survival signaling of GRP78.

Indexed as

Cell MembraneEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHumansMaleNeoplasm MetastasisNeoplasm ProteinsPC-3 CellsProstatic NeoplasmsPulmonary Surfactant-Associated Protein DRecombinant ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, humanNeoplasm ProteinsPulmonary Surfactant-Associated Protein DRecombinant ProteinsapoptosisGRP78innate immunityinteractome analysisprostate cancersignalingsurfactant protein D

Identifiers

PMID33542717
PMCPMC7850985
OpenAlexW3124794618

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.