Clinicopathologic Features and Prognostic Implications of Golgi Phosphoprotein 3 in Non-small Cell Lung Cancer: A Meta-analysis

There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

Abstract

Background: A number of studies have investigated the role of Golgi phosphoprotein-3 (GOLPH3) in the pathogenesis and progression of non-small cell lung cancer (NSCLC). However, the results of previous studies are heterogeneous and controversial. The aim of this meta-analysis was to clarify its association with the clinicopathological characteristics of patients and evaluate the prognostic significance of GOLPH3 in NSCLC.

Methods: A systematic search was conducted through PMC, PubMed, Medline, Web of Science, Chinese National Knowledge Infrastructure and Wanfang database. The odds ratio (OR) and hazard ratio (HR) with 95 % CI were calculated by STATA 12.0.

Results: 8 qualified studies with a total of 1001 patients with NSCLC were included. Pooled results showed that GOLPH3 was highly expressed in tumor tissues compared with adjacent lung tissues (OR, 7.55), and overexpression of GOLPH3 was significantly correlated with advanced clinical stage (OR, 3.42), poor differentiation of tumor (OR, 1.97) and positive lymph node metastasis (OR, 2.58), but no association with histological type, gender, age or tumor size was found in NSCLC patients. In addition, the pooled HR for overall survival was 1.79 by univariate analysis and 1.91 by multivariate analysis. The pooled HR for progression-free survival was 2.50.

Conclusions: GOLPH3 could be a risk factor for progression of NSCLC and might act as a potential prognostic biomarker for NSCLC patients.

Related collections

Most cited references 23

Record: found
Abstract: found
Article: not found

Extracting summary statistics to perform meta-analyses of the published literature for survival endpoints.

M Parmar, V. Torri, L. Stewart (1998)

Meta-analyses aim to provide a full and comprehensive summary of related studies which have addressed a similar question. When the studies involve time to event (survival-type) data the most appropriate statistics to use are the log hazard ratio and its variance. However, these are not always explicitly presented for each study. In this paper a number of methods of extracting estimates of these statistics in a variety of situations are presented. Use of these methods should improve the efficiency and reliability of meta-analyses of the published literature with survival-type endpoints.

0 comments Cited 835 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding.

Holly Dippold, Michelle Ng, Suzette Farber-Katz … (2009)

Golgi membranes, from yeast to humans, are uniquely enriched in phosphatidylinositol-4-phosphate (PtdIns(4)P), although the role of this lipid remains poorly understood. Using a proteomic lipid-binding screen, we identify the Golgi protein GOLPH3 (also called GPP34, GMx33, MIDAS, or yeast Vps74p) as a PtdIns(4)P-binding protein that depends on PtdIns(4)P for its Golgi localization. We further show that GOLPH3 binds the unconventional myosin MYO18A, thus connecting the Golgi to F-actin. We demonstrate that this linkage is necessary for normal Golgi trafficking and morphology. The evidence suggests that GOLPH3 binds to PtdIns(4)P-rich trans-Golgi membranes and MYO18A conveying a tensile force required for efficient tubule and vesicle formation. Consequently, this tensile force stretches the Golgi into the extended ribbon observed by fluorescence microscopy and the familiar flattened form observed by electron microscopy.

0 comments Cited 147 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

GMx33: a novel family of trans-Golgi proteins identified by proteomics.

Kristin Howell, M Ladinsky, Terran D R Lane … (2000)

The known functions of the Golgi complex include the sorting, packaging, post-translational modification, and transport of secretory proteins, membrane proteins, and lipids. Other functions still remain elusive to cell biologists. With the goal of identifying novel Golgi proteins, a proteomics project was undertaken to map the major proteins of the organelle using two-dimensional gels, to identify the unknowns using tandem mass spectrometry, and to screen for Golgi residents using GFP-fusion constructs. Multiple unknowns were identified, and the initial characterization of one of these proteins is reported here. GMx33 alpha is a member of a conserved family of cytosolic Golgi-associated proteins with no known homology to any known functional domain or protein. Biochemical analyses show that GMx33 alpha differentially partitions into all phases of multiple detergent extractions, and two-dimensional immunoblots reveal that there are multiple differentially modified forms of GMx33 alpha associated with the Golgi, several of which are phosphorylated. Evidence suggests that these post-translational modifications regulate its association with the Golgi. GMx33 alpha was not found on Golgi budded vesicles, and immuno-electron microscopy co-localizes GMx33 alpha to the trans-face on the same three cisternae as TGN38 in normal rat kidney cells. This work represents the preliminary characterization of a novel family of trans-Golgi-associated proteins.

0 comments Cited 40 times – based on 0 reviews      Review now

Bookmark

All references

Author and article information

Journal

Journal ID (nlm-ta): J Cancer

Journal ID (iso-abbrev): J Cancer

Journal ID (publisher-id): jca

Title: Journal of Cancer

Publisher: Ivyspring International Publisher (Sydney )

ISSN (Electronic): 1837-9664

Publication date Collection: 2019

Publication date (Electronic): 4 October 2019

Volume: 10

Issue: 23

Pages: 5754-5763

Affiliations

Department of Respiratory and Critical Care Medicine, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, Shaanxi 710061, China

Author notes

✉ Corresponding author: Dr. Manxiang Li; Department of Respiratory and Critical Care Medicine, the First Affiliated Hospital of Xi'an Jiaotong University; No. 277, West Yanta Road, Xi'an, Shaanxi 710061, China; Telephone: +86-029-85324053; Fax: +86-029-85324053; E-mail address: manxiangli@ 123456hotmail.com .

Competing Interests: The authors have declared that no competing interest exists.

Article

Publisher ID: jcav10p5754

DOI: 10.7150/jca.30067

PMC ID: 6843888

SO-VID: 02be042e-4a1a-4e25-8d1b-2fe7f7dcad43

License:

This is an open access article distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/4.0/). See http://ivyspring.com/terms for full terms and conditions.

Clinicopathologic Features and Prognostic Implications of Golgi Phosphoprotein 3 in Non-small Cell Lung Cancer: A Meta-analysis

Read this article at

Abstract

Related collections

Karger: Oncology

Most cited references 23

Extracting summary statistics to perform meta-analyses of the published literature for survival endpoints.

GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding.

GMx33: a novel family of trans-Golgi proteins identified by proteomics.

Author and article information

Journal

Affiliations

Author notes

Article

History

Categories

Comments

Comment on this article

Similar content 289

Cited by 3

Most referenced authors 1,077