Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The process of aging is understood to be associated with the presence of oxidative damage to cells. The development of synthetic prenylated proteins for therapeutic purposes has been a subject of research and development for several decades. The present review encompasses information regarding natural and synthetic prenylated proteins and macropeptides, in addition to the anti-aging effects of these isoprenoids and their underlying mechanisms. Protein prenylation functions as a predominant process for regulating oxidative damage within the cellular system. The reversibility of the aging process underscores the critical importance of regulating protein prenylation to mitigate cellular oxidative stress and reduce the risk of disease development. Several anti-aging mechanisms have been documented in the extant literature. The most well-known of these mechanisms is free radical scavenging via the electron transfer pathway. The regulation of oxidative genes and the inhibition of protein prenylation have been demonstrated to inhibit oxidative damage and subsequently maintain normal cellular function. The regulation of protein prenylation has also been demonstrated to involve the mevalonate pathway and phosphorylation-dependent mechanisms. To a certain degree, prenylated proteins are necessary for establishing a balance of homeostasis and maintaining normal cell function.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.ijbiomac.2025.147005 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Research advances in protein prenylation in cardiovascular diseases.
Eur J Pharmacol
September 2025
Department of Cardiology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, 310003, China. Electronic address:
Protein prenylation is an evolutionarily conserved post-translational modification encompassing farnesylation and geranylgeranylation. This modification is fundamental to the precise regulation of protein localization, activity, and stability, thereby underpinning critical cellular functions. Aberrant prenylation is closely associated with cardiovascular diseases and influences a spectrum of pathological mechanisms in a complex manner.
View Article and Find Full Text PDFA mass spectrometry-based proteomics strategy to detect long-chain -acylated peptides.
Analyst
August 2025
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, Utrecht 3584 CH, The Netherlands.
Long-chain -acylation is the addition of long-chain fatty acids to cysteine residues on proteins. This lipid modification is essential for protein membrane association and signalling but presents analytical challenges due to both its hydrophobicity and the labile nature of thioester bonds. We developed and optimised a bottom-up mass spectrometry workflow tailored for the detection of long-chain -acylated peptides.
View Article and Find Full Text PDFPyrin inflammasome-driven erosive arthritis caused by unprenylated RHO GTPase signaling.
EMBO Mol Med
August 2025
VIB Center for Inflammation Research, VIB, Ghent, Belgium.
Geranylgeranyl pyrophosphate, a non-sterol intermediate of the mevalonate pathway, serves as the substrate for protein geranylgeranylation, a process catalyzed by geranylgeranyl transferase I (GGTase-I). Myeloid-specific deletion of Pggt1b, the gene coding for GGTase-I, leads to spontaneous and severe erosive arthritis in mice; however, the underlying mechanisms remained unclear. In this study, we demonstrate that arthritis in mice with myeloid-specific Pggt1b deficiency is driven by unprenylated GTP-bound small RHO family GTPases, which in turn trigger Pyrin (Mefv) inflammasome activation, GSDMD-dependent macrophage pyroptosis, and IL-1β secretion.
View Article and Find Full Text PDFEngineering protein prenylation: an emerging tool for selective protein modification.
Biochem Soc Trans
August 2025
Department of Chemistry, University of Minnesota, Minneapolis, MN, 55455, U.S.A.
Prenyltransferases catalyze the attachment of isoprenoids to cysteine residues located near the C-termini of proteins including those containing a 'CaaX' tetrapeptide motif. This enzyme family includes farnesyl transferase (FTase), geranylgeranyltransferase type I (GGTase I), and GGTase type II (GGTase II). The CaaX motif broadly consists of cysteine (C), two aliphatic residues (a), and a variable residue (X), which determines substrate specificity for farnesylation and type I geranylgeranylation.
View Article and Find Full Text PDFImpact of protein prenylation inhibition on viability and IL-1β production in infected macrophages.
J Bacteriol
August 2025
Laboratory of Cellular Microbiology, Oswaldo Cruz Institute, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro, Brazil.
Unlabelled: Leprosy is a chronic infectious disease caused by and . Brazil consistently ranks among the countries with the highest number of leprosy cases. Data from our group showed that upregulates the mevalonate pathway (MP), contributing to the accumulation of cholesterol-ester-enriched lipid droplets in infected macrophages, and that the inhibition of this pathway by statins decreases bacterial intracellular viability.
View Article and Find Full Text PDF