Introduction: The secretory phospholipase A(2) (sPLA(2)) family provides a seemingly endless array of potential biological functions that is only beginning to be appreciated. In humans, this family comprises 9 different members that vary in their tissue distribution, hydrolytic activity, and phospholipid substrate specificity. Through their lipase activity, these enzymes trigger various cell-signaling events to regulate cellular functions, directly kill bacteria, or modulate inflammatory responses. In addition, some sPLA(2)'s are high affinity ligands for cellular receptors.
Objective: This review merely scratches the surface of some of the actions of sPLA(2)s in innate immunity, inflammation, and atherosclerosis. The goal is to provide an overview of recent findings involving sPLA(2)s and to point to potential pathophysiologic mechanisms that may become targets for therapy.
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http://dx.doi.org/10.1007/s10557-008-6134-7 | DOI Listing |
mLife
December 2024
State Key Laboratory of Mycology, Institute of Microbiology Chinese Academy of Sciences Beijing China.
Glycosylphosphatidylinositol (GPI) anchoring is one of the conserved posttranslational modifications in eukaryotes that attach proteins to the plasma membrane. In fungi, in addition to plasma membrane GPI-anchored proteins (GPI-APs), some GPI-APs are specifically released from the cell membrane, secreted into the cell wall, and covalently linked to cell wall glucans as GPI-anchored cell wall proteins (GPI-CWPs). However, it remains unclear how fungal cells specifically release GPI-CWPs from their membranes.
View Article and Find Full Text PDFToxins (Basel)
December 2024
School of Biotechnology, Amrita Vishwa Vidyapeetham, Kollam 690 525, Kerala, India.
The intricate combination of organic and inorganic compounds found in snake venom includes proteins, peptides, lipids, carbohydrates, nucleotides, and metal ions. These components work together to immobilise and consume prey through processes such as paralysis and hypotension. Proteins, both enzymatic and non-enzymatic, form the primary components of the venom.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Department of Lymphatic Surgery, Capital Medical University Affiliated Beijing Shijitan Hospital; Clinical Center for Lymphatic Disorders, CMU, China. Electronic address:
This study offers new insights into the dual role of secretory phospholipase A2 (sPLA2) in lymphedema, highlighting its impact on lymphatic endothelial cell (LEC) functionality. Through transcriptomic analyses and co-culture experiments, we observed that sPLA2 has both protective and detrimental effects on human LECs (HLECs), mediated by macrophage activation. Our findings reveal that while low levels of sPLA2 promote LEC health, excessive sPLA2 leads to dysfunction, emphasizing the significance of the sPLA2/PLA2R axis and arachidonic acid metabolism (AA) in lymphedema pathology.
View Article and Find Full Text PDFToxicon
December 2024
Departamento de Farmacologia, Faculdade de Ciências Médicas, Universidade Estadual de Campinas (UNICAMP), Rua Vital Brazil, 80, Cidade Universitária Zeferino Vaz, 13083-888, Campinas, SP, Brazil. Electronic address:
The venom of Colombian specimens of the rear-fanged snake Pseudoboa neuwiedii contains proteolytic and phospholipase A (PLA) activities, but is devoid of esterases. Mass spectrometric analysis of electrophoretic bands indicated that this venom contains C-type lectins (CTL), cysteine-rich secretory proteins (CRiSP), PLA, snake venom metalloproteinases (SVMP), and snake venom matrix metalloproteinases (svMMP). In this investigation, we extended our characterization of P.
View Article and Find Full Text PDFBiochem Biophys Res Commun
January 2025
Department of Biochemistry and Molecular Biology, Shanxi Key Laboratory of Birth Defect and Cell Regeneration, MOE Key Laboratory of Coal Environmental Pathogenicity and Prevention, Shanxi Medical University, Taiyuan, Shanxi, 030001, China. Electronic address:
Secreted phospholipase A2s (sPLA2s) participate in physiological function by their enzyme and receptor binding activity. Muscle-type phospholipase A2 receptor (M-type PLA2R) is the sPLA2 binding protein with the highest affinity so far, and also inhibits the enzyme activity of sPLA2. There is species specificity and pH dependence for the binding of M-type PLA2R to sPLA2.
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