Disease relevance of LAP3

• Special features of intestinal metaplasia and its relation to early gastric carcinoma in man: observation by a method in which leucine aminopeptidase activity is used [1].
• After 6 months of treatment with 40 and 100 mg per kg per day, bile duct proliferation, portal tract inflammation and fibrosis, bile canalicular bleb formation, and hypertrophy of the smooth endoplasmic reticulum were associated with elevated serum levels of oxaloacetic transaminase, glutamic pyruvic transaminase, and leucine aminopeptidase [2].
• The active sites of aminopeptidase A (PepA) from Escherichia coli and leucine aminopeptidase from bovine lens are isostructural, as shown by x-ray structures at 2.5 A and 1.6 A resolution, respectively [3].
• Amniotic-fluid intestinal alkaline phosphatase activity, gamma-glutamyltranspeptidase activity, and leucine-aminopeptidase activity were quantitated to assess their reliability for the prenatal diagnosis of cystic fibrosis [4].
• Recently, the three-dimensional structure of two aminopeptidases, the methionine aminopeptidase from Escherichia coli and the leucine aminopeptidase from Aeromonas proteolytica, have been elucidated by crystallographic studies [5].

Psychiatry related information on LAP3

• Action plan peps up Europe's mental health [6].

High impact information on LAP3

• The degree of intestinal metaplasia and its macroscopic distribution in gastric mucosa were examined by a new method in which leucine aminopeptidase (LAP) activity is used to investigate the relationship between intestinal metaplasia and gastric carcinoma [1].
• Other aminopeptidases, such as leucine aminopeptidase (LAP) and endoplasmic reticulum aminopeptidase 1 (ERAP 1), can trim epitope precursors from the amino terminus to their correct size for MHC class I binding to enhance antigen presentation [7].
• Science renal enzyme excretion (alpha-glucosidase, gamma-glutamyltranspeptidase, leucine aminopeptidase) was not found to be invariably elevated when trypsin/creatinine clearance ratio was increased, tubular damage cannot be assumed as constituting the only reason for an altered clearance ratio [8].
• During the treatment period, most blood tests (e.g., blood count, blood urea nitrogen, albumin, SGOT, lactate dehydrogenase) remained within normal limits, but there was a significant dose-related increase in serum leucine aminopeptidase levels [9].
• Thus, exposure of the liver to increased amounts of lithocholic acid during chenodeoxycholic acid treatment might result in elevation of serum leucine aminopeptidase activity [9].

Chemical compound and disease context of LAP3

• High-dose AA induced glucosuria, proteinuria, and elevated serum creatinine levels and reduced leucine aminopeptidase enzymuria on days 10 and 35, whereas low-dose AA had no significant effect [10].
• Increased activities of cytosol aminopeptidase and lactate dehydrogenase in serum originate from lymphocytes in necrotizing lymphadenitis [11].
• In chronic hepatitis and liver cirrhosis serum sIgA correlated significantly with leucine aminopeptidase (r = 0.69), GOT (r = 0.66), alkaline phosphatase (r = 0.55), and direct bilirubin (r = 0.42) [12].
• The isolates were gram-positive cocci that divided on an irregular plane and produced metabolic lactic acid, pyrrolidonyl arylamidase, and leucine aminopeptidase [13].
• Cystine animopeptidase and leucine aminopeptidase of choriocarcinoma cells grown in culture [14].

Biological context of LAP3

• Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography [15].
• Combining these data with those previously reported, the suggested assignment for the PEPS locus is the 4p11 leads to 4q12 segment of chromosome 4 [16].
• Suggested assignment of peptidase S (PEPS) to 4p11-4q12 by exclusion using gene dosage, accounting for variability in fibroblasts [16].
• The interspecific PEPS cell hybrid phenotype can be resolved into a pattern which suggests that PEPS is composed of five or six identical subunits [17].
• In the present study, prolyl aminopeptidases were purified to apparent homogeneity from pig small intestine mucosa and human liver and their NH2-terminal amino acid sequences were determined together with that of pig kidney leucyl aminopeptidase [18].

Anatomical context of LAP3

• Leucine aminopeptidase was purified from human liver cytosol to homogeneity, 1538-fold, with a yield of 84.4% by immunoaffinity chromatography [19].
• Degree of confluence, site of biopsy, and sex and age of donor did not affect PEPS activity in fibroblasts but generation number did (r = 0.367, P = 0.001) [16].
• PEPS activity was measured in white blood cells from three patients with Wolf-Hirschhorn syndrome (4p-) and 50 controls [16].
• Results are presented supporting assignment of the PEPS locus to chromosome 4 in man using man-mouse and man-Chinese hamster somatic cell hybrids [17].
• Using exclusion from Sepharose 4B as our criterion, we have found a high-molecular-weight form of alkaline phosphatase and of leucine aminopeptidase which are released into the culture media by the FL amnion cell line [20].

Associations of LAP3 with chemical compounds

• A colorimetric assay using leucyl-beta-napthylamide hydrochloride as substrate and fast garnet GBC as the color reagent was developed for these regional mapping studies of peptidase S (PEPS) [16].
• Four other wound-induced, ABA-responsive genes that encode two additional proteinase inhibitors, the proteolytic enzyme leucine aminopeptidase, and the biosynthetic enzyme threonine deaminase were isolated from potato plants [21].
• The mode of binding of bestatin to leucine aminopeptidase may be similar to that of a tetrahedral intermediate that is thought to form during peptide bond hydrolysis [22].
• In both structures, a bicarbonate anion is bound to an arginine side chain (Arg-356 in PepA and Arg-336 in leucine aminopeptidase) very near two catalytic zinc ions [3].
• Ethanol treatment of VL-17A cells also reduced the activity of leucine aminopeptidase (LAP) [23].

Physical interactions of LAP3

• In the second assay method, the MetAP reaction is coupled to a prolyl aminopeptidase reaction using Met-Pro-p-nitroanilide as substrate [24].

Regulatory relationships of LAP3

• IFN-gamma also upregulates leucine aminopeptidase, which should promote the removal of N-terminal flanking residues of antigenic peptides [25].

Other interactions of LAP3

• Previous studies have shown that two homologs of genes on HSA4, PGM2 and PEPS, are located in bovine syntenic group U15 (chromosome 6) [26].
• Through a series of single- and multitrait and single- and multipoint analyses, the QTL was positioned to an interval surrounded by the genes ABCG2 and LAP3 [27].
• The sequence encodes a 960-amino acid protein with significant homology to placental leucine aminopeptidase and adipocyte-derived leucine aminopeptidase [28].
• Adipocyte-derived leucine aminopeptidase (A-LAP, endoplasmic reticulum aminopeptidase ERAP1) is specialized to produce peptides presented on the class I major histocompatibility complex (MHC) by trimming epitopes to eight or nine residues, in addition to its enzymatic activity to degrade angiotensin II [29].
• Lactase and leucyl-aminopeptidase showed a tendency to decrease in CRF, but this difference did not reach statistical significance [30].

Analytical, diagnostic and therapeutic context of LAP3

• The S-carboxymethylated fractions were enzymatically digested with pronase, carboxypeptidase A and B, leucine aminopeptidase and prolidase, and epsilon-(gamma-glutamyl)lysine isolated from digests by gel filtration and cation ion exchange chromatography [31].
• Induction of leucine aminopeptidase by interferon-gamma. Identification by protein microsequencing after purification by preparative two-dimensional gel electrophoresis [32].
• Electron microscopy of leucine aminopeptidase [33].
• Using immunoelectrophoresis and other techniques, we have demonstrated an association between lipoprotein-X and (a) alkaline phosphatase and (b) other enzymes originating from the hepatocyte membrane, namely gamma-glutamyltransferase and leucine aminopeptidase [34].
• We have established reference ranges for three microvillar intestinal enzymes--alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.1), and leucine aminopeptidase (EC 3.4.1.1)--measured in amniotic fluid in a reference population of 1875 women presenting for routine amniocentesis [35].

References