High concentration of neutral endopeptidase (Enkephalinase E.C. 3.4.24.11) in a malignant tumor: Rat hepatoma 3924A

Deddish, Peter A.; Dragovic, T.; Erdös, Ervin G.; Weber, George

doi:10.1016/0006-291x(90)91436-v

“…Since EGF is involved in leiomyomata growth stimulation (Maruo et al, 2000), the up-regulation of CPM observed in this tumor may be involved in this process by increasing the metabolism of EGF. Other studies have already described an increase in CPM activity in cancer samples, as in bronchoalveolar lavage from patients with lung cancer (Dragovic et al, 1995) or in rapidly-growing hepatoma (Deddish et al, 1990). Conversely, CPM activity was measured in lung tumors and shown to be significantly decreased in tumors compared to adjacent uninvolved lung tissue from the same patients (Cohen et al, 1997).…”

Section: Alternative Splicing Of Human Cpm Mrnamentioning

confidence: 94%

Molecular Structure and Alternative Splicing of the Human Carboxypeptidase M Gene

Pessoa¹,

Id²,

Ha³

et al. 2002

Biological Chemistry

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Using RACE technology the 5' and 3' ends of human carboxypeptidase M (CPM) mRNA were determined and found to be divergent from the published sequence. With these results the complete structure of the human CPM gene was established based on the human genome sequence in the GenBank database. The gene was shown to contain 9 exons comprising at least 75 kb of genomic sequence. A novel first exon of 30 bp was identified and an upstream promoter sequence containing several transcription factor binding sites was found by computer analysis. Furthermore, the ATG starting codon was detected defining an open reading frame of 1329 bp that codes for a protein of 443 residues. Additionally, the polyadenylation site was discovered, determining a 3' noncoding region of 2000 nucleotides. The exon-intron boundaries diverged substantially compared to those of the other basic carboxypeptidases, CPD, CPE, CPN, and AEBP1. Cloning and sequencing of RT-PCR products from different tissues revealed alternative splicing of exons 3 and 5, which results in the generation of four different mRNA isoforms. RNA extracted from tumor tissues contained more CPM mRNA than control tissue, suggesting an upregulation of CPM expression in tumors and raising the question of the role of this enzyme in cancer.

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“…Low-level endopeptidase 24.11 activity has also been demonstrated in plasma (7). Recently endopeptidase 24.11 was identified in the liver, where it appears t o be bound t o cell membranes (8).…”

mentioning

confidence: 99%

Plasma endopeptidase 24.11 (enkephalinase) activity is markedly increased in cholestatic liver disease

Swain¹

1993

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Endopeptidase 24.11 (enkephalinase), an enzyme known to be present in plasma and liver, is capable of metabolizing a substantial number of bioactive peptides. We measured plasma endopeptidase 24.11 activity in normal subjects and in patients with chronic hepatocellular disease or chronic cholestatic liver disease. The mean level of plasma endopeptidase 24.11 activity was 13 times higher in cholestatic patients than in controls or patients with hepatocellular disease (p < 0.01). Plasma endopeptidase 24.11 activity in patients correlated closely with traditional serum markers of cholestasis, including levels of alkaline phosphatase, gamma-glutamyltranspeptidase and aminopeptidase (p < 0.01 for all). However, plasma endopeptidase 24.11 activity correlated poorly with serum ALT aminotransferase level (p = NS), indicating that it is not a marker of hepatocellular disease. The lack of overlap between plasma endopeptidase 24.11 activity in cholestatic patients and noncholestatic liver disease controls suggests that this enzyme activity is a useful biochemical marker of cholestasis. In addition, because of the broad spectrum of peptides metabolized by endopeptidase 24.11, increased plasma endopeptidase 24.11 activity may contribute to the pathophysiology of the syndrome of cholestasis.

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Plasma endopeptidase 24.11 (enkephalinase) activity is markedly increased in cholestatic liver disease

Swain

¹

,

Vergalla

²

,

Jones

³

1993

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Endopeptidase 24.11 (enkephalinase), an enzyme known to be present in plasma and liver, is capable of metabolizing a substantial number of bioactive peptides. We measured plasma endopeptidase 24.11 activity in normal subjects and in patients with chronic hepatocellular disease or chronic cholestatic liver disease. The mean level of plasma endopeptidase 24.11 activity was 13 times higher in cholestatic patients than in controls or patients with hepatocellular disease (p < 0.01). Plasma endopeptidase 24.11 activity in patients correlated closely with traditional serum markers of cholestasis, including levels of alkaline phosphatase, gamma-glutamyltranspeptidase and aminopeptidase (p < 0.01 for all). However, plasma endopeptidase 24.11 activity correlated poorly with serum ALT aminotransferase level (p = NS), indicating that it is not a marker of hepatocellular disease. The lack of overlap between plasma endopeptidase 24.11 activity in cholestatic patients and noncholestatic liver disease controls suggests that this enzyme activity is a useful biochemical marker of cholestasis. In addition, because of the broad spectrum of peptides metabolized by endopeptidase 24.11, increased plasma endopeptidase 24.11 activity may contribute to the pathophysiology of the syndrome of cholestasis.

show abstract

High concentration of neutral endopeptidase (Enkephalinase E.C. 3.4.24.11) in a malignant tumor: Rat hepatoma 3924A

Cited by 9 publications

References 20 publications

Molecular Structure and Alternative Splicing of the Human Carboxypeptidase M Gene

Molecular Structure and Alternative Splicing of the Human Carboxypeptidase M Gene

Plasma endopeptidase 24.11 (enkephalinase) activity is markedly increased in cholestatic liver disease

Plasma endopeptidase 24.11 (enkephalinase) activity is markedly increased in cholestatic liver disease

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