Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of various chemical and enzymatic modifications of low density lipoprotein (LDL) on its ability to activate the isolated human plasma lysolecithin acyltransferase (LAT) was studied. Removal of all lipids from LDL resulted in the complete loss of LAT activation. Removal of only neutral lipids by extraction with heptane retained up to 50% of the original activity, which was not increased further by reconstitution of the LDL with the extracted lipids. Hydrolysis of the diacylphosphoglycerides of the LDL with phospholipases resulted in complete loss of LAT activation which was partially restored by the addition of egg lecithin. Hydrolysis of more than 4% of LDL protein by trypsin led to a linear decrease in activity with complete loss of activity occurring when about 25% of the LDL protein is hydrolyzed. Modification of the arginine groups of LDL reversibly inhibited the activation of LAT. Modification of lysine residues of LDL by acetylation, acetoacetylation or succinylation also abolished its ability to activate lysolecithin acylation.
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PMID:Role of low density lipoprotein in the activation of plasma lysolecithin acyltransferase activity. Effect of chemical and enzymatic modifications of the lipoprotein on enzyme activity. 392 84

The biochemical characteristics of type II alveolar epithelial cells dissociated from adult rabbit lung by instillation of low concentrations of an elastase trypsin mixture are reported. Cells studied immediately (within 4 h) after isolation were found to incorporate the radioactively labelled precursors [U-14C]glucose, [methyl-3H]choline and [3H]palmitate into cellular phosphatidylcholine at rates 2-10-fold higher than previously reported for cells not subject to short-term cell culture. Secretion of phosphatidylcholine was stimulated by beta-adrenergic agonists. Measurement of specific activities of enzymes of phospholipid biosynthesis in subcellular fractions of isolated lung cells showed a significant enrichment of acyl coenzyme A-lysophosphatidylcholine acyltransferase, an enzyme believed to be involved in pulmonary surfactant phosphatidylcholine remodeling, in the endoplasmic reticulum of type II cells. These observations support the utility of freshly isolated type II cells as a model system for the study of the functions of the alveolar epithelium.
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PMID:Properties of freshly isolated type II alveolar epithelial cells. 684 86

1. The transverse localization of palmitoyl-CoA : lysophosphatidylcholine acyltransferase in the membrane of microsomal vesicles isolated from mouse lung adenomas and rat liver was studied by treating intact and deoxycholate-disrupted microsomes with trypsin and pronase. 2. The latency of mannose-6-phosphatase was preserved during protease treatment, suggesting that membrane integrity was not affected. 3. In adenoma microsomes 35-50% and in liver microsomes 35% of lysophosphatidylcholine acyltransferase activity is accessible to the action of the proteases. Our results suggest that at least a sizable portion of the active center of the enzyme that is responsible for remodeling phospholipids is embedded in the membrane interior. 4. Since enzymes involved in de novo lipid synthesis are reported to be located at the cytoplasmic surface of the microsomal membrane, our results support the notion that in lipid metabolism distinct metabolic pools might exist at opposite sides of the microsomal membrane.
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PMID:Transmembrane orientation of palmitoyl-CoA: lysophosphatidylcholine acyltransferase in microsomes isolated from an alveolar type II cell adenoma and rat liver. 732 57

Previous attempts to purify acyl-CoA:1-acyl-lysophosphatidylcholine acyltransferase (EC 2.3.1.23) have been frustrated by difficulties in solubilizing the enzyme without inactivation. Microsomal preparations, from the developing cotyledons of sunflower, in high concentrations of urea retain activity. Gel-filtration liquid chromatography followed by trypsin treatment (minus urea) resulted in the removal of many contaminating proteins without loss of enzyme activity. SDS/PAGE showed the presence of two major peptides with apparent molecular masses of 52 and 59 kDa. These polypeptides cross-reacted with the radiolabelled photoreactive substrate 1-azido-oleoyl-sn-lysophosphatidyl-[N-methyl-(3)H]choline.
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PMID:Partial purification and photoaffinity labelling of sunflower acyl-CoA:lysophosphatidylcholine acyltransferase. 1117 Nov 82