Results 11 to 20 of about 3,296 (190)

Secretory Phospholipase A2s in Insulin Resistance and Metabolism [PDF]

open access: yesFrontiers in Endocrinology, 2021
The phospholipases A2 (PLA2) superfamily encompasses enzymes commonly found in mammalian tissues and snake venom. Many of these enzymes have unique tissue distribution, function, and substrate specificity suggesting distinct biological roles. In the past,
Michael S. Kuefner
doaj   +3 more sources

Lactadherin inhibits secretory phospholipase A2 activity on pre-apoptotic leukemia cells. [PDF]

open access: yesPLoS ONE, 2013
Secretory phospholipase A2 (sPLA2) is a critical component of insect and snake venoms and is secreted by mammalian leukocytes during inflammation. Elevated secretory PLA2 concentrations are associated with autoimmune diseases and septic shock. Many sPLA2'
Steffen Nyegaard   +3 more
doaj   +3 more sources

The electrostatic basis for the interfacial binding of secretory phospholipases A2

open access: yesBiophysical Journal, 1994
Biochemical and structural data suggest that electrostatic forces play a critical role in the binding of secretory phospholipases A2 to substrate aggregates (micelles, vesicles, monolayers, and membranes). This initial binding (adsorption) of the enzyme to the interface is kinetically distinct from the subsequent binding of substrate to the buried ...
Scott, D.L.   +3 more
openaire   +3 more sources

Dynamic Role of Phospholipases A2 in Health and Diseases in the Central Nervous System

open access: yesCells, 2021
Phospholipids are major components in the lipid bilayer of cell membranes. These molecules are comprised of two acyl or alkyl groups and different phospho-base groups linked to the glycerol backbone.
Grace Y. Sun   +6 more
doaj   +2 more sources

Secretory Phospholipases A2 Activate Selective Functions in Human Eosinophils [PDF]

open access: yesThe Journal of Immunology, 2003
Abstract Secretory phospholipases A2 (sPLA2s) are released in large amounts in the blood of patients with systemic inflammatory diseases and accumulate at sites of chronic inflammation, such as the airways of patients with bronchial asthma.
TRIGGIANI, MASSIMO   +6 more
core   +7 more sources

Quercetin as an inhibitor of snake venom secretory phospholipase A2

open access: yesChemico-Biological Interactions, 2011
As polyphenolic compounds isolated from plants extracts, flavonoids have been applied to various pharmaceutical uses in recent decades due to their anti-inflammatory, cancer preventive, and cardiovascular protective activities. In this study, we evaluated the effects of the flavonoid quercetin on Crotalus durissus terrificus secretory phospholipase A2 (
Cotrim, Camila Aparecida   +11 more
openaire   +4 more sources

Human phospholipases A2: a functional and evolutionary analysis

open access: yesВавиловский журнал генетики и селекции, 2023
Phospholipases A2 (PLA2) are capable of hydrolyzing the sn-2 position of glycerophospholipids to release fatty acids and lysophospholipids. The PLA2 superfamily enzymes are widespread and present in most mammalian cells and tissues, regulating metabolism,
I. I. Turnaev   +2 more
doaj   +3 more sources

The secretory phospholipase A2 group IIA: a missing link between inflammation, activated renin-angiotensin system, and atherogenesis?

open access: yesVascular Health and Risk Management, 2008
Dimitar Divchev, Bernhard SchiefferDepartment of Cardiology and Angiology, Medizinische Hochschule Hannover, GermanyAbstract: Inflammation, lipid peroxidation and chronic activation of the renin–angiotensin system (RAS) are hallmarks of the ...
Dimitar Divchev, Bernhard Schieffer
doaj   +1 more source

Assay of phospholipases A2 and their inhibitors by kinetic analysis in the scooting mode [PDF]

open access: yesMediators of Inflammation, 1992
Several cellular processes are regulated by interfacial catalysis on biomembrane surfaces. Phospholipases A2 (PLA2) are interesting not only as prototypes for interfacial catalysis, but also because they mobilize precursors for the biosynthesis of ...
Mahendra Kumar Jain   +3 more
doaj   +2 more sources

Pathways of Protein Secretion in Prokaryotes and Eukaryotes: Molecular Mechanisms, Biological Functions, and Therapeutic Opportunities [PDF]

open access: yesMedComm (2020)
This graphical abstract delineates noncanonical protein secretion systems across eukaryotes and prokaryotes. Eukaryotic UcPS covers four ER–Golgi bypass pathways, enabling rapid leaderless protein export via direct transmembrane translocation or vesicle‐mediated release.
Yang Q   +8 more
europepmc   +2 more sources

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