APOD

Last update 08 May 2025

Basic Info

Synonyms

Apo-D, APOD, apolipoprotein D

Introduction

APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.

100 Clinical Results associated with APOD

100 Translational Medicine associated with APOD

0 Patents (Medical) associated with APOD

747

Literatures (Medical) associated with APOD

01 Jun 2025·Neurobiology of Disease

Apolipoproteins in ischemic stroke progression and recovery: Key molecular mechanisms and therapeutic potential

Review

Author: Dubois, Fatemeh ; Zheng, Ze ; Vivien, Denis ; Etuze, Tamara ; Triniac, Hortense

Ischemic stroke, responsible for 80 % of all strokes, is a leading cause of mortality globally. While altered lipids profiles are recognized as modifiable risk factors, their direct impact on stroke outcomes is less understood due to the brain's distinct lipid metabolism and the selective permeability of the blood-brain barrier for lipoproteins. As key components of lipoproteins, apolipoproteins are essential for lipid transport, redistribution and metabolism in both the central nervous system and peripheral blood circulation. This review provides an updated perspective on the influence of brain-expressed apolipoproteins (such as ApoE, ApoA-I, ApoJ, ApoD, and others) and those that cross the damaged blood-brain barrier following ischemic stroke. We explore hypotheses regarding their involvement in molecular pathways related to lipid metabolism, inflammation, oxidative stress, mitochondrial function and blood-brain barrier integrity. Through this synthesis, we aim to identify potential biomarkers and therapeutic targets, thereby enhancing our understanding of apolipoproteins in ischemic stroke progression and contributing to improved clinical outcomes.

01 May 2025·International Journal of Biological Macromolecules

Comprehensive identification of stone-promoting proteins in the urine of kidney stone formers

Article

Author: Chotikawanich, Ekkarin ; Peerapen, Paleerath ; Rattananinsruang, Piyaporn ; Phuangkham, Somsakul ; Sritippayawan, Suchai ; Hadpech, Sudarat ; Thongboonkerd, Visith ; Detsangiamsak, Sasinun

Urinary proteins have crucial roles in modulating kidney stone formation. While stone-inhibiting urinary proteins are well characterized, stone-promoting urinary proteins are insufficiently explored. This knowledge gap limits our ability to fully comprehend the pathogenic mechanisms underlying nephrolithiasis and hampers the development of targeted therapeutic/preventive interventions. Therefore, we systematically identified stone-promoting proteins from the urine of 30 calcium oxalate (CaOx) nephrolithiatic patients (stone formers). Urinary proteins were fractionated by anion exchange and size-exclusion chromatography. A total of 15 protein fractions (SF1-SF15) were tested for their modulating activities on CaOx crystals by various assays compared with the control. The fractions with net CaOx-promoting activities were then identified by nanoLC-ESI-Qq-TOF MS/MS. From 15 fractions, 9 had net CaOx-promoting activities in all crystal assays. Among 3-99 proteins identified from these fractions, alpha-1acid glycoprotein 2, alpha-1-antitrypsin, apolipoprotein D, CD44 antigen, endosialin, fibrinogen alpha chain, interleukin-18-binding protein, kallikrein-1, retinol-binding protein 4, and titin have been found to increase in the urine of stone formers compared with controls, reinforcing their potential roles as CaOx stone promoters. This study offers the largest collection of CaOx stone-promoting proteins that will shed light on pathogenic mechanisms of nephrolithiasis and may allow further development of new drug targets to treat/prevent nephrolithiasis.

01 May 2025·Diabetes, Obesity and Metabolism

Quantitative proteomics identifies plasma protein alterations that associate with metabolic and thrombotic profile changes after bariatric surgery

Article

Author: Stewart, Alan J. ; Fernandes, Marco F. ; Synowsky, Silvia A. ; Abbas, Kazim ; Ahmed, Hasnain ; Shirran, Sally L. ; Ajjan, Ramzi A.

AbstractObjectiveRoux‐en‐Y gastric bypass (RYGB) surgery has been shown to lead to favourable health outcomes in obese patients. However, the molecular changes that occur and how they relate to clinical measures are poorly understood. Here, we characterise the proteomic alterations that occur in plasma of RYGB patients before and 9 months after surgery using quantitative proteomics.MethodsPlasma proteomics was performed by sequential window acquisition of all theoretical fragment ion spectra mass spectrometry (SWATH‐MS) to identify and quantify differentially abundant proteins. Relationships between significantly altered proteins and clinical markers were examined. A gene set enrichment analysis was also conducted to identify altered pathways.ResultsFrom the proteomic analysis, 27 proteins increased, and 43 proteins decreased in abundance 9 months after surgery, providing insights into the physiological changes that accompany weight loss. Proteins including sex hormone binding globulin (SHBG), inter‐alpha‐trypsin inhibitor heavy chain 3 (ITIH3) and apolipoprotein D (APOD), which increased in abundance post‐surgery, highlight improvements in lipid regulation, insulin sensitivity and inflammation. Proteins involved in coagulation, including α2‐macroglobulin, kallikrein‐B1, prothrombin, and factor (FX, FXI and FXII), exhibited reduced levels, aligning with a decrease in thrombotic potential.ConclusionsThese findings provide a mechanistic understanding of how bariatric surgery leads to systemic changes in metabolic and haemostatic pathways, thus favourably modulating the risk of developing cardiovascular disease.

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APOD

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