Elastase and Elastase-Inhibitor

J, Balo; Banga, I

doi:10.1038/164491a0

Cited by 123 publications

(30 citation statements)

References 2 publications

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“…described by Balo and Banga (1949), which is a serine proteinase secreted in a zymogen form by pancreatic acinar cells. The second class of mammalian elastase is PMN-E, the neutral proteinase found in the granules of human polymorphonuclear leucocytes (Janoff & Schere, 1968;Baugh & Travis, 1976).…”

Section: Discussionmentioning

confidence: 99%

Production of immunoreactive polymorphonuclear leucocyte elastase in human breast cancer cells: possible role of polymorphonuclear leucocyte elastase in the progression of human breast cancer

Yamashita

Ogawa²,

Ikei³

et al. 1994

Br J Cancer

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SummaryBreast cancer cells are known to express various proteolytic enzymes, which make them invasive and favour their dissemination to distant sites. However, it is unclear whether breast cancer cells have the ability to produce polymorphonuclear leucocyte elastase (PMN-E). We measured immunoreactive (ir) PMN-E content in the conditioned medium of two breast cancer cell lines, MCF-7 and ZR-75-1, and two normal breast epithelial cell lines, HBL-100 and Hs 578Bst, using a highly specific and sensitive enzyme immunoassay. (4.23 ± 3.74 gg 100 mg-' protein) patients. Breast cancer patients with high levels of ir-PMN-E showed significantly shorter disease-free survival and overall survival than those with low levels of ir-PMN-E at the cut-off point of 8.99 lg 100 mg-' protein. In the multivariate analysis, ir-PMN-E content was found to be a significant prognostic factor for disease recurrence and death in human breast cancer.Considerable evidence suggests that proteolytic enzymes are involved in cancer invasion and metastasis (Mignatti et al., 1986;Persky et al., 1986). Production of tumour cell proteinases, including plasminogen activator (Duffy et al., 1987;Reich et al., 1988;Yamashita et al., 1993a), collagenase (Turpeenniemi-Hujanen et al., 1985), and cathepsin B (Recklies et al., 1980) has been implicated in tumour cell invasion into adjacent tissues and metastasis. Another proteinase that has attracted attention as a mediator of these processes is elastase. Elastase is the only proteinase that is able to degrade insoluble elastin (Janoff & Schere, 1968), a structural component of elastic tissues such as blood vessels, skin, lung and breast tissue.An elastinolytic activity has been demonstrated previously by Hornebeck et al. (1977) in tissue extracts from human breast cancer, but in their study it was not determined whether the activity could be attributed to tumour cells. Thereafter, several investigators have reported that elastinolytic activity is found in the culture medium of mouse mammary tumour cells (Grant et al., 1990;Zeydel et al., 1986) and human breast cancer cells (Kao et al., 1982), suggesting that elastinolytic enzymes are produced by the tumour cells themselves.Very recently, a highly specific and sensitive enzyme immunoassay (EIA) was established for the measurement of human polymorphonuclear leucocyte elastase (PMN-E) (Ikei et al., 1992). Labelled antibody in this assay recognises not only PMN-E complexed a,-proteinase inhibitor but also the free form of PMN-E, which may present in the enzyme samples. In the present study, we examined whether breast cancer cells have the ability to produce immunoreactive (ir)-PMN-E. Furthermore, we have determined the concentration of ir-PMN-E in tissue extracts from human breast cancer, and elucidated the relationship between the tissue content of ir-PMN-E and clinicopathological status in human breast cancer. Materials and methods Cell cultureThe human breast cancer cell line MCF-7 was kindly provided by Y. Nomura (National Kyushu Cancer Center Hospital, Fu...

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Section: Discussionmentioning

confidence: 99%

Production of immunoreactive polymorphonuclear leucocyte elastase in human breast cancer cells: possible role of polymorphonuclear leucocyte elastase in the progression of human breast cancer

Yamashita

Ogawa²,

Ikei³

et al. 1994

Br J Cancer

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“…Avogaro et al [1], U termann [46], and Walford and Schneider [47] could not detect any significant variation with age. A decrease in enzyme inhibitory capacity of serum with age was found by Balo and Banga [2], Crepaldi et al [11], Oshima et al [33] and Salvini [39]. Only Pretolani and Coccheri [35] reported a progressive increase with age up to the 6th decade, the inhibitor level remaining constant at still higher ages.…”

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confidence: 75%

Elastolytic Enzymes and Elastin in the Aging Rat

1971

Gerontology

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The age-relationship of antielastoproteinase, antitrypsin, and antichymotrypsin activity of rat serum was studied using alkali-treated elastin as substrate for measuring elasto-proteinase activity and synthetic substrates for measuring trypsin and chymotrypsin activity (trypsin substrate: benzoyl-arginine- p-nitroanalide; chymotrypsin substrate: acetyl-tyrosine-hydrazide). Serum antielastoproteinase levels in both male and female rats increased with age, whereas the levels for ântitrypsin and antichymotrypsin decreased with age. These findings support the hypothesis that the serum contains separate inhibitors for elastoproteinase and trypsin. The effect of age on the antielastoproteinase activity of rat serum was compared with data found in the literature for human serum. Rat serum showed highly significant age-related ‘tryptic and chymotryptic activities’ (both ‘enzyme activities’ increasing with age in both sexes). That these enzymatic activities represent real trypsin and chymotrypsin activities is questioned. Serum amidases and thrombin may be responsible for the measured activities.

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“…nal [3] and Nature [4,5] , and received 375 citations ( table 1 ). One could thus consider that the discovery of pancreatic elastase dates from 1949.…”

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confidence: 99%

Pancreatic Elastase: A Forgotten Hungarian Discovery

Buzás¹

2007

Pancreatology

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Elastase and Elastase-Inhibitor

Cited by 123 publications

References 2 publications

Production of immunoreactive polymorphonuclear leucocyte elastase in human breast cancer cells: possible role of polymorphonuclear leucocyte elastase in the progression of human breast cancer

Production of immunoreactive polymorphonuclear leucocyte elastase in human breast cancer cells: possible role of polymorphonuclear leucocyte elastase in the progression of human breast cancer

Elastolytic Enzymes and Elastin in the Aging Rat

Pancreatic Elastase: A Forgotten Hungarian Discovery

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