Tumour-associated trypsin inhibitor (TATI) in human ovarian cyst fluid. Comparison with CA 125 and CEA

Halila, Hannu; Huhtala, Marja-Liisa; Haglund, Caj; Nordling, Stig; Stenman, Ulf‐Hǎkan

doi:10.1038/bjc.1987.175

Cited by 36 publications

(27 citation statements)

References 20 publications

(16 reference statements)

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“…In other types of ovarian cancer other mechanisms may contribute to the elevation, because high levels of TATI are only occasionally found in the cyst fluid of nonmucinous tumours (Halila et al, 1987). TATI may become elevated not only in cancer but also in connection with severe inflammatory (Huhtala et al, 1983), especially hepatobiliary, disease (Haglund et al, 1986) and postoperatively (Matsuda et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

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Tumour-associated trypsin inhibitor (TATI) in ovarian cancer

Halila

Lehtovirta²,

Stenman³

1988

Br J Cancer

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Summary Tumour-associated trypsin inhibitor (TATI) is a 6 kD peptide isolated from the urine of a patient with ovarian cancer. Increased urinary excretion of TATI has earlier been observed in patients with gynaecological malignancies. The value of TATI in urine and serum as a marker for ovarian cancer was studied in 102 patients. Preoperatively urine TATI was elevated in 55% (18/33) and serum TATI in 27% (12/45) of the patients. In patients with mucinous tumours, elevated preoperative levels of TATI were observed in 6 out of 10 patients, while CA 125 was elevated in 4 and CEA in one of the cases. When assay of TATI was used to predict presence of disease before second-look surgery of 48 patients, the sensitivity and specificity of serum TATI was 19% and 91%, and that of urine TATI 42% and 76%, respectively. Rising TATI levels were observed in progressive disease, whereas regressive disease was not as often associated with falling levels. Serum TATI was elevated in 45% (144/318) and urine TATI in 57% (73/171) of samples from patients with clinical evidence of disease. The TATI assay was found to be of potential value in the management of patients with mucinous ovarian cancer, but in patients with non-mucinous ovarian cancer it did not provide information additional to that obtained from assay of ovarian cancer marker CA 125 alone.

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Section: Discussionmentioning

confidence: 99%

“…The latter tumours regularly contain high levels of CA 125, the levels of which are lower in mucinous tumours (Halila et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Tumour-associated trypsin inhibitor (TATI) in ovarian cancer

Halila

Lehtovirta²,

Stenman³

1988

Br J Cancer

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“…Besides, in tumour tissues, such a proteolytic enzyme and its inhibitor occur together, and the latter could be involved in the inhibition of the former enzymatic activity (Kataoka et al, 1989;Strauli et al, 1980;Turpeinen et al, 1988). Tumour-associated trypsin inhibitor, TATI, is a peptide identified in ovarian cancerous extracts, the N-terminal amino acid sequence of which is very similar to PSTI (Halila et al, 1987). The ability of TATI to inhibit not only trypsin but also some fibrinolytic enzymes, such as plasmin, urokinase, and tissue-type plasminogen activator, has been recently demonstrated in its physiological concentrations, suggesting that TATI has a possible role in proteolytic control involving these proteinases (Turpeinen et al, 1988).…”

Section: Discussionmentioning

confidence: 99%

Expression of pancreatic secretory trypsin inhibitor (PSTI) in colorectal cancer

Higashiyama

Monden²,

Tomita³

et al. 1990

Br J Cancer

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Summary We examined the expression of pancreatic secretory trypsin inhibitor (PSTI) in colorectal cancer by immunohistochemical staining using an anti-PSTI antiserum, an in situ hybridisation technique utilising sulphonated PSTI cDNA probe, and a Northern blot hybridisation method, using a 32P-labelled PSTI Pancreatic secretory trypsin inhibitor (PSTI) consists of a single polypeptide chain, and is known to be a specific trypsin inhibitor in the pancreas. Its physiological role has been considered to prevent the premature activation of trypsin in the pancreatic acini and ducts (Kazal et al., 1948). However, PSTI has also been demonstrated in various malignant cell lines and tissues, including pancreatic cancer, lung cancer, gynaecological cancer, and gastric cancer (Higashiyama et al., 1990;Ogata, 1988;Ogawa et al., 1987;Tomita et al., 1987;Ueda et al., 1989); the physiological role of PSTI in neoplastic tissue remains unknown. Nevertheless, several investigators have recently shown that PSTI may have functions other than the inhibition of trypsin activity, such as growth factor action (Niinobu et al., 1986;Ogawa et al., 1985Ogawa et al., , 1987. In fact, we have shown that the expression of PSTI in gastric cancer may possibly be associated with tumour growth and progression (Higashiyama et al., 1990).Although it has been reported that PSTI may be expressed in villous adenoma of the colon (Bohe et al., 1986;Tomita et al., 1987), there has been-u-study of the expression of PSTI in colorectal cancer, except for the preliminary report (Ogawa et al., 1987). In the present study, we demonstrate that colorectal cancer may also express PSTI, not only by immunohistochemical analysis for detection at the product level but also by in situ hybridisation and Northern blot hybridisation for detection at the transcriptional level. In addition, the possible biological and clinical significance of PSTI expression in colorectal cancer is also discussed. Materials and methods Tissue preparationThe tissues were supplied from surgical specimens resected at the 2nd Dept of Surgery, Osaka University Hospital. Preparation of anti-PSTI antiserum and immunohistochemical study Anti-PSTI antiserum used in this study was produced in rabbits as previously described (Kitahara et al., 1980). Its sensitivity and specificity were also confirmed by radioimmunoassay.Immunohistochemical study was performed according to a modified method of Hsu et al. (1981). Briefly, sections were dewaxed in xylene, rehydrated with a series of ethanol solutions, and endogenous peroxidase activity was blocked using 0.3% hydrogen peroxide in methanol for 30 min. After immersion in 3% normal goat serum for 30 min, in order to block non-specific binding, the sections were incubated with primary anti-PSTI antiserum at a dilution of 1:400 overnight at 4°C, and subsequently with biotinylated goat anti-rabbit IgG (Vector) and avidin-biotin peroxidase complex (Vectastain ABC kit, Vector) for 30 min each at room temperature. They were washed in PBS between each incubation...

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“…During patient monitoring, the serum concentrations of SPINK1 reflect the development of recurrent disease (17 ). Compared to serum concentrations, up to 1000-fold higher concentrations of SPINK1 have been found in cyst fluid from both benign and malignant ovarian cysts, but increased serum concentrations are rare in patients with benign cysts (18 ). A recent study (19 ) of mucinous borderline ovarian tumors showed that increased serum concentrations of SPINK1 were found in these patients and a significant correlation was observed with tissue expression of claudin-5.…”

Section: Ovarian Cancermentioning

confidence: 99%

Emerging Roles of SPINK1 in Cancer

et al. 2016

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BACKGROUND Tumor-associated trypsin inhibitor (TATI) was originally isolated from the urine of a patient with ovarian cancer. It was later shown to be produced by many other tumors and several normal tissues. It had earlier been isolated from the pancreas and was hence called pancreatic secretory trypsin inhibitor (PSTI). It belongs to a family of protease inhibitors presently called serine peptidase inhibitor Kazal type (SPINK). In the SPINK family TATI/PSTI is SPINK1, which is the name used in this review. CONTENT In addition to being a protease inhibitor, SPINK1 also acts as an acute-phase reactant and a growth factor. Furthermore, it has been shown to modulate apoptosis. Overexpression of SPINK1 predicts an unfavorable outcome in several cancers and determination of SPINK1 in serum can be used to identify patients at increased risk of aggressive disease. Thus serum SPINK1 can be used as a prognostic tumor marker. Because SPINK1 acts as a growth factor and an inhibitor of apoptosis in some cancers, it has also been suggested that it can be a therapeutic target in cancer. However, because SPINK1 is the major physiological inhibitor of trypsin, inhibition of SPINK1 may increase the risk of pancreatitis. SUMMARY Taking into account the many functions of SPINK1, assessing the role of SPINK1 in cancer has several potentially important clinical applications ranging from a biomarker to a potential new target for cancer therapy.

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Tumour-associated trypsin inhibitor (TATI) in human ovarian cyst fluid. Comparison with CA 125 and CEA

Cited by 36 publications

References 20 publications

Tumour-associated trypsin inhibitor (TATI) in ovarian cancer

Tumour-associated trypsin inhibitor (TATI) in ovarian cancer

Expression of pancreatic secretory trypsin inhibitor (PSTI) in colorectal cancer

Emerging Roles of SPINK1 in Cancer

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