Literature DB >> 12559605

Arginase in patients with breast cancer.

Zofia Porembska1, Grzegorz Luboiński, Alicja Chrzanowska, Magdalena Mielczarek, Joanna Magnuska, Anna Barańczyk-Kuźma.   

Abstract

The mean arginase activity in breast cancers (n = 80) was significantly higher than in control tissues and it accounted for 0.31 +/- 0.23 U/g wet tissue and 0.083 +/- 0.061 U/g (P < 0.05), respectively. With the cutoff value of 0.1 U/g wet tissue, raised arginase activity was observed in 74% of tumors. The preoperative arginase activity in blood serum from women with breast cancer was 11.2 +/- 7.9 U/l (n = 115), and it was significantly higher than in 70 healthy controls, where it was 5.7 +/- 2.4 U/l (P < 0.05). With the cutoff value for normal serum arginase activity above 8.0 U/l, the activity was raised in 10% of control individuals, and in 63% of women with breast cancer. The sensitivity and specificity of the arginase test in blood serum were 63% and 60%, respectively. Two isoforms immunologically identical to human kidney arginases (L-arginine amidinohydrolase) were found in both normal and cancerous breast tissues. The level of anionic form was similar in control and cancerous tissues, whereas the cationic isoform predominated in breast cancer. The cationic isoform was the only one present in serum of both ill and healthy women, and its level was higher in patients with breast cancer. Thus, it can be concluded that the cationic isoform is responsible for the increase of arginase activity in serum of patients with breast cancer. Copyright 2002 Elsevier Science B.V.

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Year:  2003        PMID: 12559605     DOI: 10.1016/s0009-8981(02)00391-1

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  17 in total

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Journal:  ACS Med Chem Lett       Date:  2020-03-23       Impact factor: 4.345

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Journal:  Neurochem Res       Date:  2008-07-10       Impact factor: 3.996

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9.  Differential gene-expression profiles associated with gastric adenoma.

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Journal:  Br J Cancer       Date:  2004-01-12       Impact factor: 7.640

10.  Proteomic identification of mitochondrial targets of arginase in human breast cancer.

Authors:  Rajan Singh; Nuraly K Avliyakulov; Melissa Braga; Michael J Haykinson; Luis Martinez; Vikash Singh; Meher Parveen; Gautam Chaudhuri; Shehla Pervin
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