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Nature Chemical Biology Feb 2019
Topics: Biochemical Phenomena; Choline; Phospholipase D; Phospholipases
PubMed: 30659294
DOI: 10.1038/s41589-018-0218-x -
British Journal of Obstetrics and... Apr 1991The activity of phospholipase A2 types 1 and 2 and phospholipase C was measured in the endometrium of women with ovulatory menorrhagia and in those with normal menstrual... (Comparative Study)
Comparative Study
The activity of phospholipase A2 types 1 and 2 and phospholipase C was measured in the endometrium of women with ovulatory menorrhagia and in those with normal menstrual blood loss. In both groups of subjects phospholipase A2 type 1 activity was significantly higher in the secretory phase than in the proliferative phase (P less than 0.001). The median activity (pmol/mg protein/min) for the proliferative phase was 27.6 in normal subjects and 40.4 in women with ovulatory menorrhagia and for the secretory phase the median activity was 144.5 in normal women and 138.1 in women with ovulatory menorrhagia. There was no difference between the two groups of women at either stage of the cycle. Phospholipase A2 type 2 activity was also higher in the secretory phase than in the proliferative phase (P less than 0.05 for normal subjects and P less than 0.001 for women with menorrhagia). The median activity (pmol/mg protein/min) for the proliferative phase was 94.4 (normal subjects) and 56.6 (women with menorrhagia) and for the secretory phase 148.3 (normal subjects) and 142.5 (women with menorrhagia). The activity of phospholipase A2 type 2 was significantly lower in the proliferative phase of women with ovulatory menorrhagia compared with normal subjects (P less than 0.05). Phospholipase C activity (nmol/mg protein/min) was significantly higher in women with ovulatory menorrhagia (median 8.2) compared with women with normal blood loss (median 5.5) (P less than 0.01).
Topics: Endometrium; Female; Humans; Menorrhagia; Menstrual Cycle; Menstruation; Phospholipases; Phospholipases A; Phospholipases A2; Type C Phospholipases
PubMed: 2031895
DOI: 10.1111/j.1471-0528.1991.tb13426.x -
The American Journal of Pathology Jun 1978Cobra venom factor (CoF), the anticomplementary protein in Naja naja cobra venom, is usually purified by sequential ion exchange and gel filtration chromatography. CoF...
Cobra venom factor (CoF), the anticomplementary protein in Naja naja cobra venom, is usually purified by sequential ion exchange and gel filtration chromatography. CoF prepared in this manner contains small but significant quantities of phospholipase A2 activity. This acyl hydrolase activity can be simply and efficiently removed on a large scale by treatment of CoF with p-bromophenacyl bromide (BPB), an irreversible modifier of the histidine residue in the active site of phospholipase A2. BPB treatment does not alter the anticomplementary activity of CoF. In vivo experiments utilizing intratracheal injections of control and BPB-treated CoF, as well as pure phospholipase A2, revealed that contaminating phospholipase A2, and not the anticomplementary protein, was responsible for the observed acute neutrophil-associated lung injury. However, phospholipase A2 had no effect on the hypotensive and thrombocytopenic effects of CoF infected intravenously into rabbits. Depletion of circulating C3-C9 by intraperitoneal injections of CoF was not altered by removal of phospholipase A2 activity with BPB.
Topics: Acetophenones; Animals; Blood Platelets; Blood Pressure; Complement C3; Complement Inactivator Proteins; Elapid Venoms; Enzyme Inhibitors; Female; Lung; Male; Neutrophils; Phospholipases; Pulmonary Alveoli; Rabbits
PubMed: 655262
DOI: No ID Found -
International Journal of Biological... Jan 2020Secreted phospholipases A2 (sPLA2) are water-soluble lipolytic enzymes that act at the interface of organized lipid substrates, where the catalytic step is coupled to...
Secreted phospholipases A2 (sPLA2) are water-soluble lipolytic enzymes that act at the interface of organized lipid substrates, where the catalytic step is coupled to various interfacial phenomena as enzyme penetration, solubilisation of reaction products, lateral packing and loss of mechanical stability of organized assemblies of phospholipid molecule, among others. Using the monomolecular film technique, we compared the interfacial properties of crab digestive sPLA (CDPL) with those of the porcine pancreatic one (PPPL). A kinetic study on the surface pressure dependency of the two sPLA was performed using monomolecular films of three different substrates: di C-PC (1.2-dilauroyl-sn-glycerol-3-phosphocholine); di C-PG (1.2-dilauroyl-sn-glycerol-3-phosphoglycerol) and di C-PE (1.2-dilauroyl-sn-glycerol-3-phosphoethanolamine). The use of a substrate in monolayer state, during the catalytic reactions, allows us to monitor the effect of several physicochemical parameters by altering the "quality of interface". The effect of temperature on the hydrolysis rate of these substrates was also checked. Our results show that activities of both phospholipases were affected by the variation of the subphase temperature. CDPL was irreversibly inactivated by p-bromo-phenacyl bromide, the specific inhibitor of sPLA2. The hyperbolic catalytic behaviour observed was coherent with hopping mode of action, one of the two characteristic mechanisms of interfacial catalysis of sPLA2.
Topics: Animals; Brachyura; Catalysis; Digestion; Hydrolysis; Kinetics; Membrane Lipids; Phase Transition; Phospholipases; Phospholipases A2, Secretory; Phospholipids; Surface Properties; Swine; Transition Temperature
PubMed: 31622722
DOI: 10.1016/j.ijbiomac.2019.10.011 -
Revista Iberoamericana de Micologia 2011The Malassezia genus includes mainly lipophilic yeasts belonging to the cutaneous microbiota of man and other mammals. Some Malassezia species have been associated with... (Comparative Study)
Comparative Study
BACKGROUND
The Malassezia genus includes mainly lipophilic yeasts belonging to the cutaneous microbiota of man and other mammals. Some Malassezia species have been associated with various dermatological diseases. The factors permitting the transformation of yeasts of the Malassezia genus from a commensal organism to a pathogenic agent are still little known but the production of various enzymes such as lipase, phospholipase and lipoxygenase could contribute to the pathogenic activity of these yeasts.
AIMS
Here we have determined and compared the extracellular phospholipase activity of sixty human isolates of Malassezia so as to relate this feature to the species of Malassezia and to the origin (from dermatological diseases or not) of the strains examined.
METHODS
Phospholipase production was determined using the semi-quantitative egg-yolk plate method.
RESULTS AND CONCLUSIONS
Malassezia obtusa, Malassezia slooffiae, Malassezia globosa, Malassezia restricta had difficulty developing in the chosen culture medium so that it was not possible to measure phospholipasic activity. Malassezia pachydermatis showed the highest phospholipase activity. Twenty-nine Malassezia sympodialis strains produced phospholipase; the isolates from patients with pityriasis versicolor had significantly higher phospholipasic activity than those isolated from healthy individuals. This observation suggests that the phospholipasic activity of Malassezia may play a role in the onset of skin lesions, especially in the case of pityriasis versicolor.
Topics: Dermatomycoses; Extracellular Space; Humans; Malassezia; Phospholipases; Tinea Versicolor
PubMed: 21645629
DOI: 10.1016/j.riam.2011.05.002 -
Biochemical Society Transactions 1976
Topics: Penicillium; Phospholipases; Serum Albumin, Bovine
PubMed: 1001665
DOI: 10.1042/bst0040281 -
The Journal of Rheumatology Apr 1990
Topics: Aged; Cartilage, Articular; Humans; Osmolar Concentration; Phospholipases; Phospholipases A; Phospholipases A2; Tissue Distribution
PubMed: 2348443
DOI: No ID Found -
Klinische Wochenschrift Feb 1989Several studies suggest that the activation of pancreatic phospholipase A2 (PLA2) and its release from injured acinar cells play an important role in the pathogenesis of... (Review)
Review
Several studies suggest that the activation of pancreatic phospholipase A2 (PLA2) and its release from injured acinar cells play an important role in the pathogenesis of acute pancreatitis. Elevated catalytic activity of PLA2 in serum is associated especially with severe forms of the disease. PLA2 has been purified from human cadaver pancreas and an antiserum raised against the enzyme in rabbits. Immuno-histochemical localization of PLA2 in pancreatic tissue was abnormal in acute pancreatitis. A time-resolved fluoroimmunoassay for human pancreatic PLA2 has been developed. Increased serum concentrations of immunoreactive PLA2 were found in acute pancreatitis during the first week after hospital admission. The values returned to normal somewhat more slowly than corresponding serum amylase values. The immunochemical determination of PLA2 in serum provides a fast and specific detection of injury to pancreatic acinar cells. The pancreas is not the only source of PLA2 in acute pancreatitis. The nonpancreatic PLA2 may originate from various inflammatory cells, but this hypothesis remains to be proven.
Topics: Acute Disease; Humans; Pancreas; Pancreatitis; Phospholipases; Phospholipases A; Phospholipases A2
PubMed: 2648059
DOI: 10.1007/BF01711349 -
Zeitschrift Fur Medizinische... 1989Several studies suggest that phospholipase A2 (PLA2) plays an important role in the pathology of acute pancreatitis. PLA2 is activated within the pancreas in... (Review)
Review
Several studies suggest that phospholipase A2 (PLA2) plays an important role in the pathology of acute pancreatitis. PLA2 is activated within the pancreas in experimental and human acute pancreatitis. Elevated catalytic activity of PLA2 in serum is associated especially with the severe forms of the disease. The pancreas seems not to be the only source of the enzyme entering the circulation in acute pancreatitis. The source of the non-pancreatic PLA2 may be various inflammatory cells, but this hypothesis remains to be proven. The results of the treatment of experimental acute pancreatitis with PLA2 inhibitors have been promising, but adequate human trials have not been conducted.
Topics: Acute Disease; Humans; Pancreas; Pancreatitis; Phospholipases; Phospholipases A; Phospholipases A2
PubMed: 2683447
DOI: No ID Found -
The British Journal of Dermatology Jun 1975Phospholipase A and lysophospholipase activities have been demonstrated in cow snout epidermis. The phospholipase A activity was dependent on Ca2+ ions and the pH for...
Phospholipase A and lysophospholipase activities have been demonstrated in cow snout epidermis. The phospholipase A activity was dependent on Ca2+ ions and the pH for optimum activity was between 6-1 and 7-4.
Topics: Animals; Calcium; Cattle; Cell-Free System; Chromatography, DEAE-Cellulose; Hydrogen-Ion Concentration; In Vitro Techniques; Lysophosphatidylcholines; Phosphatidylcholines; Phospholipases; Skin; Time Factors
PubMed: 241370
DOI: 10.1111/j.1365-2133.1975.tb03138.x