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Results for “LEUCINE AMINOPEPTIDASE”

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PubMed1989

Activity of the gamma-glutamyltransferase, leucine aminopeptidase and alkaline phosphatase enzymes in human tear fluid.

In this work the presence of gamma-glutamyltransferase (GGT), leucine amino-peptidase (LAP) and alkaline phosphatase (AP) is shown in human tear fluid. We studied these levels according to sex, age and some eye refraction defects. The differences between the levels for both sexes are not significant. LAP and AP do not show any differences in either age groups or individuals with some refraction defects. The average level of GGT is higher from 40 years of age upwards (p less than 0.005). In individuals with refraction defects, the enzymatic activity is significantly higher (p less than 0.05) than the activities found in normal subjects. The levels of the three enzymes in serum and tear fluid do not show a significant correlation nor are they significantly modified after the samples have been frozen for a month at -20 degrees C.

Adult↗
PubMed2004

Identification and initial characterization of a putative Mycoplasma gallinarum leucine aminopeptidase gene.

Aminopeptidases (APN) may play a role in host colonization of M. gallinarum. Characterization of endogenous APN activity suggests that the leucine APN (LAP) of M. gallinarum is a metallo-aminopeptidase activated by Mn2+ and is present in the cytosol and possibly associated with the inner leaflet of the membrane. A 1.36-kb open reading frame (ORF) identified from overlapping genomic phage clones showed 68% nucleotide identity and 51% amino acid identity with the M. salivarium LAP gene. This ORF is expressed as a 1.5-kb monocistronic transcript and is present as a single copy in M. gallinarum. This gene sequence was modified to account for codon usage, and expression in E. coli produced a 51-kDa protein, which compares well with the product predicted from the ORF. This ORF is a strong candidate for contributing the LAP activity of M. gallinarum protein extracts.

Amino Acid Sequence↗
PubMed1983

[Effect of melatonin on L-leucine aminopeptidase in the hypothalamus and cerebral cortex of the normal and ovariectomized rat].

The effect of melatonin (500 micrograms/kg weight s.c. for 15 consecutive days) on the L-leucine amino peptidase (LAP) activity of the hypothalamus and brain cortex is studied on castrated and nan castrated rats. There was a significant increase in the LAP activity of hypothalamus (p less than 0.001 v.s. saline group) in the non castrated group, however, no changes were observed in the brain cortex. In the ovariectomized group injected from the 15th to 30th after castration, a very big decrease was recorded in the LAP activity in both the hypothalamus and brain cortex which was not modified by melatonin. This data is studied in relationship to the antigonadotrophic effect of melatonin on the non castrated animals since the changes of this activity in the hypothalamus are inversely related to the gonadotrophin secretion, specially luteinizing hormone.

Animals↗
PubMed1975

[Action of leucine aminopeptidase 1 and 2 (Aspergillus oryzae 410) on various synthetic peptides (author's transl)].

By use of di- or tripeptides as substrates, LAP 1 and LAP 2, 2 fractions from Aspergillus oryzae hydrolyze oligopeptides that possess leucine as N-terminal amino acid. LAP 1 fraction also hydrolyzes the histidyl bond. Both fractions have no activity towards peptides as glutathion, gly-pro-ala; they have low or no activity towards tyrosyl and tryptophanyl bond.

Aspergillus↗
PubMed2006

A novel role for placental leucine aminopeptidase (P-LAP) as a determinant of chemoresistance in endometrial carcinoma cells.

In several recent studies, we have shown that P-LAP can be a poor prognostic factor and a factor of chemoresistance in endometrial carcinoma, especially in the advanced patients. In our study, we investigated whether P-LAP alters the expression of apoptosis regulatory proteins as a mechanism of drug resistance. We transfected P-LAP cDNA into A-MEC cells (endometrial adenocarcinoma cell line), and A-MEC-LAP cells displayed a 1.8-fold, 2.0-fold and 1.7-fold increase in IC(50) against paclitaxel, carboplatin and cisplatin respectively. Translational downregulation by siRNA2 to P-LAP on A-MEC-LAP cells demonstrated 60%, 51% and 58% decrease in IC(50). To investigate the mechanism of P-LAP-induced chemoresistance, we also assessed whether P-LAP transfection had an effect on carboplatin-induced apoptotic death of A-MEC cells. A-MEC and A-MEC-pc (transfected with vector alone) cells exhibited a strong apoptotic response to carboplatin, while A-MEC-LAP cells exhibited a weak apoptotic response. In an attempt to identify the mechanism of the inhibitory effect on apoptotic response to carboplatin, we next assessed the expression of cleaved caspases and PARP cleavage. While treatment of A-MEC-pc cells with carboplatin exhibited increased levels of cleaved caspase 3, caspase 7 and caspase 9 compared to that after no treatment, A-MEC-LAP cells did not show any expression of these caspases. These results suggest that P-LAP reduces sensitivity to anticancer drugs via inhibition of mitochondria-mediated apoptosis, and may be a molecular target for conquering anticancer drug resistance.

Antineoplastic Agents↗