Evidence map›Paper›PMID 30284223›Full record

ArticleJournal of endocrinological investigation2019

Quantitative proteomics analysis of sporadic parathyroid adenoma tissue samples.

A K Arya, S K Bhadada, P Singh, D Dahiya, G Kaur, S Sharma, U N Saikia, A Behera, S D Rao, M Bhasin

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Article in Journal of endocrinological investigation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

7 citing papers in PubMed, 10 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 3 institutions in 2 countries.

A K AryaDepartment of Endocrinology, Postgraduate Institute of Medical Education and Research (PGIMER), Room No. 2, 4th Floor Block-F, Nehru Hospital, PGIMER, Chandigarh, 160012, India.
S K BhadadaDepartment of Endocrinology, Postgraduate Institute of Medical Education and Research (PGIMER), Room No. 2, 4th Floor Block-F, Nehru Hospital, PGIMER, Chandigarh, 160012, India. bhadadask@rediffmail.com.
P SinghDepartment of Endocrinology, Postgraduate Institute of Medical Education and Research (PGIMER), Room No. 2, 4th Floor Block-F, Nehru Hospital, PGIMER, Chandigarh, 160012, India.
D DahiyaDepartment of General Surgery, PGIMER, Chandigarh, India.
G KaurDepartment of Endocrinology, Postgraduate Institute of Medical Education and Research (PGIMER), Room No. 2, 4th Floor Block-F, Nehru Hospital, PGIMER, Chandigarh, 160012, India.
S SharmaDepartment of Biochemistry, PGIMER, Chandigarh, India.
U N SaikiaDepartment of Histopathology, PGIMER, Chandigarh, India.
A BeheraDepartment of General Surgery, PGIMER, Chandigarh, India.
S D RaoBone and Mineral Research Laboratory, Henry Ford Hospital, Detroit, USA.
M BhasinDepartment of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Post Graduate Institute of Medical Education and Research · INBeth Israel Deaconess Medical Center · USHenry Ford Hospital · US

Funding

Indian Council of Medical Research 2011-15750
6 · The paper itself

Abstract

objectiveMolecular pathogenesis of parathyroid tumors is incompletely understood. Identification of novel molecules and understanding their role in parathyroid tumorigenesis by proteomics approach would be informative with potential clinical implications.

methodAdenomatous (n = 5) and normal (n = 2) parathyroid tissue lysates were analyzed for protein profile by LC-MS/MS method and the proteins were classified using bioinformatics tools such as PANTHER and toppfun functional enrichment tool. Identified proteins were further validated by western blotting and qRT-PCR (n = 20).

resultComparative proteomics analysis revealed that a total of 206 proteins (74 upregulated and 132 downregulated) were differentially expressed (≥ twofold change) in adenomas. Bioinformatics analysis revealed that 48 proteins were associated with plasma membrane, 49 with macromolecular complex, 39 were cytoplasm, 38 were organelle related, 21 were cell junction and 10 were extracellular proteins. These proteins belonged to a diverse protein family such as enzymes, transcription factors, cell signalling, cell adhesion, cytoskeleton proteins, receptors, and calcium-binding proteins. The major biological processes predicted for the proteins were a cellular, metabolic and developmental process, cellular localization, and biological regulation. The differentially expressed proteins were found to be associated with MAPK, phospholipase C (PLC) and phosphatidylinositol (PI) signalling pathways, and with chromatin organization. Western blot and qRT-PCR analysis of three proteins (DNAJC2, ACO2, and PRDX2) validated the LC-MS/MS findings.

conclusionThis exploratory study demonstrates the feasibility of proteomics approach in finding the dysregulated proteins in benign parathyroid adenomas, and our preliminary results suggest that MAPK, PLC and PI signalling pathways and chromatin organization are involved in parathyroid tumorigenesis.

Indexed as

AdenomaAdultBiomarkers, TumorCase-Control StudiesFemaleFollow-Up StudiesHumansMaleMiddle AgedParathyroid GlandsParathyroid NeoplasmsProteomeProteomicsYoung AdultBiomarkers, TumorProteomeHypercalcemiaMAPK pathwayPANTHERParathyroid adenomaProteomics

Identifiers

PMID30284223
OpenAlexW2895185943

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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.