Evidence map›Paper›PMID 27038811›Full record

ArticleCell stress & chaperones2016

Endoplasmic reticulum stress-induced apoptosis accompanies enhanced expression of multiple inositol polyphosphate phosphatase 1 (Minpp1): a possible role for Minpp1 in cellular stress response.

Surya P Kilaparty, Rakhee Agarwal, Pooja Singh, Krishnaswamy Kannan, Nawab Ali

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. Review
  5. Biallelic Loss-of-Function Variant inInternational journal of molecular sciences · 2025
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  10. Stable Isotopomers ofACS central science · 2022
    Article
  11. Insights to the Structural Basis for the Stereospecificity of theInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Inositol Signaling in the Basidiomycete FungusJournal of fungi (Basel, Switzerland) · 2021
    Article
  17. Article
  18. Pontocerebellar hypoplasia due to bi-allelic variants in MINPP1.European journal of human genetics : EJHG · 2021
    Article
  19. Article
  20. Article
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

5 authors at 2 institutions in 1 country.

Surya P KilapartyDepartment of Biology, University of Arkansas at Little Rock, 2801 S University Avenue, Little Rock, AR, 72204, USA.
Rakhee AgarwalDepartment of Biology, University of Arkansas at Little Rock, 2801 S University Avenue, Little Rock, AR, 72204, USA.
Pooja SinghDepartment of Biology, University of Arkansas at Little Rock, 2801 S University Avenue, Little Rock, AR, 72204, USA.
Krishnaswamy KannanDepartment of Internal Medicine, University of Arkansas for Medical Sciences, Little Rock, AR, 72205, USA.
Nawab AliDepartment of Biology, University of Arkansas at Little Rock, 2801 S University Avenue, Little Rock, AR, 72204, USA. nali@ualr.edu.
University of Arkansas at Little Rock · USUniversity of Arkansas for Medical Sciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol polyphosphates represent a group of differentially phosphorylated inositol metabolites, many of which are implicated to regulate diverse cellular processes such as calcium mobilization, vesicular trafficking, differentiation, apoptosis, etc. The metabolic network of these compounds is complex and tightly regulated by various kinases and phosphatases present predominantly in the cytosol. Multiple inositol polyphosphate phosphatase 1 (Minpp1) is the only known endoplasmic reticulum (ER) luminal enzyme that hydrolyzes various inositol polyphosphates in vitro as well as in vivo conditions. However, access of the Minpp1 to cytosolic substrates has not yet been demonstrated clearly and hence its physiological function. In this study, we examined a potential role for Minpp1 in ER stress-induced apoptosis. We generated a custom antibody and characterized its specificity to study the expression of Minpp1 protein in multiple mammalian cells under experimentally induced cellular stress conditions. Our results demonstrate a significant increase in the expression of Minpp1 in response to a variety of cellular stress conditions. The protein expression was corroborated with the expression of its mRNA and enzymatic activity. Further, in an attempt to link the role of Minpp1 to apoptotic stress, we studied the effect of Minpp1 expression on apoptosis following silencing of the Minpp1 gene by its specific siRNA. Our results suggest an attenuation of apoptotic parameters following knockdown of Minpp1. Thus, in addition to its known role in inositol polyphosphate metabolism, we have identified a novel role for Minpp1 as a stress-responsive protein. In summary, our results provide, for the first time, a probable link between ER stress-induced apoptosis and Minpp1 expression.

Indexed as

3T3 CellsAnimalsAntibodiesApoptosisCell Line, TumorEndoplasmic ReticulumEndoplasmic Reticulum StressHumansMicePhosphoric Monoester HydrolasesRatsRats, Sprague-DawleyReactive Oxygen SpeciesRNA InterferenceRNA, Small InterferingStress, PhysiologicalAntibodiesmultiple inositol-polyphosphate phosphatasePhosphoric Monoester HydrolasesReactive Oxygen SpeciesRNA, Small InterferingApoptosisEndoplasmic reticulumER stressInositol phosphatesMinpp1Multiple inositol polyphosphate phosphatase

Identifiers

PMID27038811
PMCPMC4907990
OpenAlexW2330551892

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.