Disease relevance of Phlpb

• A brush border membrane-associated phospholipase B/lipase was solubilized from the distal two-thirds of rat small intestine by autolysis during storage at -35 degrees C over 1 month, and then the enzyme was purified to homogeneity and characterized enzymatically and structurally [1].
• Increased intestinal phospholipase A(2) activity catalyzed by phospholipase B/lipase in WBN/Kob rats with pancreatic insufficiency [2].

High impact information on Phlpb

• Identification of functional domains of rat intestinal phospholipase B/lipase. Its cDNA cloning, expression, and tissue distribution [3].
• A cDNA encoding a rat intestinal Ca(2+)-independent phospholipase B/lipase (PLB/LIP) was cloned from an ileac mucosa cDNA library using a probe amplified by polymerase chain reaction based on the purified enzyme's sequence [3].
• These results indicate that the purified enzyme is the catalytic domain derived from the second repeat of brush border membrane-associated phospholipase B/lipase [1].
• Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes [1].
• Purification and partial characterization of a retinyl ester hydrolase from the brush border of rat small intestine mucosa: probable identity with brush border phospholipase B [4].

Biological context of Phlpb

• PLB has been identified by molecular studies as a cryptococcal virulence determinant [5].
• Glycerophosphorylcholine was also abundant in cryptococcomas, consistent with hydrolysis of phospholipids in vivo by the cryptococcal enzyme, phospholipase B (PLB) [5].

Anatomical context of Phlpb

• Phospholipase B in the brains and meninges of nonsensitized and sensitized rats after challenge with Angiostrongylus cantonensis [6].
• PLA2, as well as phospholipase C (PLC), treatment of synaptic membranes produced a dose-dependent increase in the specific binding of [3H]HCh-3 whereas neither phospholipase B nor phospholipase D had any effect [7].
• We propose that PLB secreted by cryptococci promotes tissue invasion by hydrolysing host phospholipids, such as dipalmitoyl phosphatidyl choline, which is abundant in pulmonary surfactant, and lung cell membrane phospholipids [5].
• A uniform value of activity per cell was found in all these tissues extending previous histochemical and biochemical evidence that the eosinophil is the carrier cell for the phospholipase B to all major sites of distribution [8].

Associations of Phlpb with chemical compounds

• The relative mobility of the phospholipase B during electrophoresis in sodium dodecyl sulphate gels was dramatically affected by the percentage of acrylamide and the presence or absence of reducing agents in the gels [9].
• Hymenoptera venom contains histamine, vasoactive kinins, serotonin, phospholipase A, phospholipase B, hyaluronidase, antigen 5 and mastoparans [10].

Analytical, diagnostic and therapeutic context of Phlpb

• Gel slices containing the purified phospholipase B were used to generate a polyclonal antiserum in rabbits that could be used for immunoblotting [9].

References