Enhancing factor protein from mouse small intestines belongs to the phospholipase A2 family

  title={Enhancing factor protein from mouse small intestines belongs to the phospholipase A2 family},
  author={Rita Mulherkar and R. S. Rao and L Rao and Varsha Patki and Virander S. Chauhan and Madhav G. Deo},
  journal={FEBS Letters},
Expression of enhancing factor/phospholipase A2 in ICRC mice
The molecular characterization of the ICRC mouse with respect to the enhancing factor gene is reported, demonstrating that EF from Balb/c and ICRC intestines are either immunologically identical or closely related to each other although, quantitatively, EF was very low in ICRC mice.
Trace amounts of enhancing factor/phospholipase A2 in mouse peritoneal exudate cells
The presence of trace amounts of EF in the peritoneal exudate cells could be a unique mode of transport of growth factor modulator to the site of injury to aid in regeneration/cell proliferation of damaged tissue.
Comparison of the activities of wild type and mutant enhancing factor/mouse secretory phospholipase A2 proteins
Deletion mutation analysis of EF cDNA carried out in the laboratory showed that enhancing activity and phospholipase activity are two separate activities that reside in the same molecule.
Heparin inhibits enhancing factor/phospholipase A2 activity and its binding to the cell surface
Inhibition of binding of EF to cells byHeparin indicates that heparin binding region forms at least part of the receptor binding domain, which suggests that the receptor for EF on the cell surface could be a heparIn sulphate proteoglycan.
A Natural Disruption of the Secretory Group II Phospholipase A2 Gene in Inbred Mouse Strains (*)
The identification of this mutation should not only help define the physiological role of sPLA2 but also has important implications in mouse inflammatory models developed by targeted mutagenesis.
The Human 180-kDa Receptor for Secretory Phospholipases A2
The molecular cloning and expression of one of these sPLA2receptors from human kidney is reported, with results indicating a 1.6:1 ratio between the levels of transcripts encoding for the membrane-bound and soluble forms of the receptor, respectively.
Recombinant production and properties of binding of the full set of mouse secreted phospholipases A2 to the mouse M-type receptor.
Results indicate that the mouse M-type receptor is selective for only a subset of mouse sPLA2s from the group I/II/V/X structural collection.
Bactericidal properties of murine intestinal phospholipase A2.
Findings identify iPLA2 as part of the antimicrobial arsenal that equips Paneth cells to protect the small intestinal crypts from microbial invasion and this enzyme may also contribute to antibacterial defenses elsewhere in the body.
Identification and characterization of several forms of phospholipase A2 in mouse epidermal keratinocytes.
Keratinocytes express several forms of phospholipase A2 that differ in their substrate specificities and mechanisms of activation, resulting in distinct agonist-specific fatty acid release profiles.


Structure and properties of a human non-pancreatic phospholipase A2.
cDNA cloning and sequence determination of rat membrane-associated phospholipase A2.
The primary structure of rat platelet phospholipase A2.
The sequence analysis of the HPLC-separated peptides and the alignment of the sequences showed a tentative primary structure of rat platelet phospholipase A2, which was composed of 125 amino acid residues and showed 47% homology with snake venom Agkistrodon halys blomhoffii.
Novel intestinal phospholipase A2: purification and some molecular characteristics.
A new phospholipase A2 from pig ileum is purified to homogeneity which hydrolyzes phosphatidylglycerol at least 200 times more rapidly than phosph atidylcholine.
Further studies on the enhancing factor and its possible mechanism of action
The role of EF may be to trap EGF and make it available to the cells through its own receptors even in the absence of EGF receptors, which is distinct from the receptor for epidermal growth factor.
Phospholipase A2 is a major component of the salt-extractable pool of matrix proteins in adult human articular cartilage.
Adult human articular cartilage contains a component with an apparent molecular weight of 16 kd, which is extractable with high ionic strength buffers. This protein, which, in addition to lysozyme,
Synovial fluid phospholipase A2s and inflammation.
The general physiology and control of this enzyme and, in particular, the most recent findings on human synovial fluid phospholipase A2s are discussed.