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Last update 08 May 2025

GPLD1

Last update 08 May 2025

Basic Info

Synonyms

Glycoprotein phospholipase D, Glycosyl-phosphatidylinositol-specific phospholipase D, glycosylphosphatidylinositol specific phospholipase D1

+ [6]

Introduction

This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane.

Drugs associated with GPLD1

Sch-420789

Target

GPLD1

Mechanism

GPLD1 inhibitors

Active Org.-

Originator Org.

Schering-Plough Corp.

Active Indication-

Inactive Indication

Bacterial Infections [+2]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with GPLD1

100 Translational Medicine associated with GPLD1

0 Patents (Medical) associated with GPLD1

213

Literatures (Medical) associated with GPLD1

05 Feb 2025·The Journal of Biochemistry

GPLD1+ cancer stem cells contribute to chemotherapy resistance and tumour relapse in intestinal cancer

Article

Author: Mizoo, Taisuke ; Minato, Takafumi ; Nakayama, Keiichi I ; Oka, Takeru ; Sugahara, Osamu ; Higa, Tsunaki

AbstractCancer stem cells (CSCs) play a central role in cancer progression, therapy resistance, and disease recurrence. With the use of a quadruple-mutant mouse intestinal cancer organoid model and single-cell RNA-sequencing analysis, we have now identified glycosylphosphatidylinositol-specific phospholipase D1 (GPLD1), an enzyme that catalyzes the cleavage of glycosylphosphatidylinositol (GPI) anchors of membrane proteins, as a marker of slowly cycling CSCs. Ablation of Gpld1+ cells in combination with 5-fluorouracil treatment greatly attenuated cell viability in and regrowth of the intestinal cancer organoids. In addition, we identified serine protease 8 (PRSS8) as a key substrate of GPLD1 in human colorectal cancer cells. GPLD1 cleaves the GPI anchor of PRSS8 and thereby mediates release of the protease from the plasma membrane, resulting in the activation of Wnt signalling and promotion of the epithelial-mesenchymal transition (EMT) in the cancer cells. Pharmacological inhibition of GPLD1 suppressed Wnt signalling activity and EMT in association with upregulation of the amount of functional PRSS8 at the plasma membrane. Our findings suggest that targeting of GPLD1 in colorectal cancer might contribute to a new therapeutic strategy that is based on suppression of Wnt signalling and EMT-related cancer progression driven by CSCs.

01 Feb 2025·Physiology & Behavior

Plasma proteomic signature of chronic psychosocial stress in mice

Article

Author: O'Connor, Lewis A ; English, Jane A. ; O'Leary, Olivia F ; Scaife, Caitriona ; Golubeva, Anna V ; Golubeva, Anna V. ; Nolan, Yvonne M ; Donoso, Francisco ; O'Connor, Lewis A. ; Nolan, Yvonne M. ; Melo, Thieza G. ; Melo, Thieza G ; English, Jane A ; O'Leary, Olivia F.

Chronic stress significantly impacts both physical and mental wellbeing, increasing risk of cardiovascular disease, immune dysregulation, and psychiatric conditions such as depression and anxiety disorders. The plasma proteome is a valuable source of biomarkers of health and disease, but the limited number of studies exploring the potential of the plasma proteome as a biomarker for stress-related disorders underscores the importance of further investigation of the effects of chronic stress on the plasma proteome. The aim of this study was to examine the effect of a 5-week chronic psychosocial stress paradigm on the plasma proteome in mice and to determine if any affected proteins correlated with stress-induced changes in behaviour and physiology, and thus might represent biomarkers of negative impacts of chronic stress. Using LC-MS/MS proteomic analysis, 38 proteins in the mouse plasma proteome were identified to be affected by chronic psychosocial stress. Functional analysis revealed that these proteins clustered into biological functions including inflammatory response, regulation of the immune response, complement and coagulation cascades, lipid metabolic process, and high-density lipoprotein particles. Correlation analyses of the identified proteins with stress-induced behavioral or physiological changes stress revealed significant correlations between stress-induced anxiety-like behaviour and Phosphatidylinositol-glycan-specific phospholipase D, Complement C2, Epidermal growth factor receptor, Prosaposin, Actin-related protein 2/3 complex subunit 1B, Maltase-glucoamylase, Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA and Fibrinogen-like protein 1. Chronic psychosocial stress blunted acute stress-induced corticosterone release, and this correlated with abundance of Pyrethroid hydrolase Ces2a; N-fatty-acyl-amino acid synthase/hydrolase Pm20d1, Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA, Alpha-2-macroglobulin-P and L-selectin. Finally, stress-induced reductions in both brown and epididymal fat correlated with Phosphatidylinositol-glycan-specific phospholipase D, Complement C2, Epidermal growth factor receptor, Kininogen-1, Apolipoprotein M, Angiopoietin-related protein 3, Proprotein convertase subtilisin/kexin type 9, and Lipopolysaccharide-binding protein. These findings demonstrate that chronic psychosocial stress induces alterations in plasma proteins implicated in key biological processes and pathways related to stress response, immune function, and lipid metabolic regulation. Further investigation into these proteins may provide new avenues for identification of biomarkers or mediators of stress-induced pathology.

01 Jan 2025·Thoracic Cancer

Proteomic Analysis of Plasma Exosomes Enables the Identification of Lung Cancer in Patients With Chronic Obstructive Pulmonary Disease

Article

Author: Wang, Wei ; Li, Weimin ; Wu, Jiaxuan ; Ji, Guiyi ; Song, Tingting ; Liu, Yi ; Yang, Yongfeng ; Zhang, Huohuo ; Gan, Jiadi

ABSTRACTChronic obstructive pulmonary disease (COPD) is confirmed as an independent risk factor for the development of lung cancer. Although low‐dose CT screening significantly reduces the mortality rate of lung cancer, the misdiagnosis and missed diagnosis rates remain high in the COPD population. Additionally, several COPD patients are unable to undergo invasive histological examinations. Therefore, there is an urgent need for minimally invasive biomarkers to screen or diagnose lung cancer in COPD patients. In this study, peripheral blood samples were collected from COPD patients with and without lung cancer. Plasma exosomes (EVs) were extracted for proteomic analysis. Sixteen differentially expressed proteins (DEPs) were preliminarily selected via label‐free quantification (LFQ) proteomic technology and comprehensive bioinformatics analysis. Parallel reaction monitoring (PRM) targeted validation identified five candidate proteins associated with COPD with lung cancer. Compared to the COPD group, KRT1, KRT9, and KRT10 were significantly upregulated in the COPD with lung cancer group, while GPLD1 and TF were downregulated. The biomarkers identified in our study provide a foundation for non‐invasive screening and diagnosis of lung cancer in COPD patients and exploration of the mechanisms shared between COPD and lung cancer.

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GPLD1

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