Evidence map›Paper›PMID 32331836›Full record

ArticleBiochemical and biophysical research communications2020

Markers of malignant prostate cancer cells: Golgi localization of α-mannosidase 1A at GM130-GRASP65 site and appearance of high mannose N-glycans on cell surface.

Pi-Wan Cheng, Samuel Davidson, Ganapati Bhat

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 18 citations in OpenAlex.

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  14. The Role of GM130 in Nervous System Diseases.Frontiers in neurology · 2021
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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 1 institution in 1 country.

Pi-Wan ChengDepartment of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE, USA; College of Medicine, and, University of Nebraska Medical Center, Omaha, NE, USA; Eppley Institute of Research on Cancer and Allied Diseases, Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA. Electronic address: pcheng@unmc.edu.
Samuel DavidsonCollege of Medicine, and, University of Nebraska Medical Center, Omaha, NE, USA. Electronic address: Samuel.davidson@unmc.edu.
Ganapati BhatDepartment of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE, USA. Electronic address: Ganapati.bd@gmail.com.
University of Nebraska Medical Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
Tracking and Evaluation CoreU54GM115458 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI RIZZO, MATTHEW · 2016 to 2025
$42.8M
NCI NIH HHS P30 CA036727NIGMS NIH HHS U54 GM115458
6 · The paper itself

Abstract

The ability to distinguish malignant from indolent prostate cancer cells is critically important for identification of clinically significant prostate cancer to minimize unnecessary overtreatment and sufferings endured by patients who have indolent cancer. Recently, we discovered that loss of giantin function as the primary Golgi targeting site for endoplasmic reticulum-derived transport vesicles in aggressive prostate cancer cells caused a shift of the Golgi localization site of α-mannosidase 1A to 130 KDa Golgi matrix protein (GM130)-65 KDa Golgi reassembly-stacking protein (GRASP65) site resulting in emergence of high mannose N-glycans on trans-Golgi enzymes and cell surface glycoproteins. To extend this observation, we isolated two cell clones (Clone 1 and Clone 2) from high passage LNCaP cells, which exhibited androgen refractory property missing in low passage LNCaP cells, and characterized their malignant property. We have found that comparing to Clone 2, which does not have cell surface high mannose N-glycans and exhibits localization of α-mannosidase 1A at giantin site, Clone 1 displays cell surface high mannose N-glycans, exhibits localization of α-mannosidase 1A at GM130-GRASP65 site, and shows a faster rate of closing the wound in a wound healing assay. The results indicate that Golgi localization of α-mannosidase 1A at GM130-GRASP65 site and appearance of cell surface high mannose N-glycans may serve as markers of malignant prostate cancer cells.

Indexed as

AutoantigensBiomarkers, TumorCell Line, TumorCell MembraneGolgi ApparatusGolgi Matrix ProteinsHumansMaleMannoseMembrane ProteinsPolysaccharidesProstatic NeoplasmsAutoantigensBiomarkers, TumorGolgi Matrix ProteinsGolgin subfamily A member 2GORASP1 protein, humanMannoseMembrane ProteinsPolysaccharidesAdvanced prostate cancer markersGalanthus nivalis lectinGM130-GRASP65Golgi α-mannosidase 1AHigh mannose N-glycans

Identifiers

PMID32331836
PMCPMC7745625
OpenAlexW3017752365

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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.