Sources/Clones
Biogenex (PS2.1), Dako (BC04) and Labvision Corp (PS2.1, R47-94).
Fixation/Preparation
The antigen survives formalin fixation and is enhanced by HIER.
Background
pS2 is a 6660 Dalton, 60 amino acid secretory polypeptide protein that was isolated from the breast carcinoma cell line MCF-7. It belongs to a recently described family of trefoil-shaped growth factors which includes human intestinal trefoil factor (hITF) and human spasmolytic polypeptide (hSP). Although its exact function is unknown, it is believed to be part of a steroid-dependent stimulatory pathway. An estrogen-regulated protein, it has been studied as a marker of an intact estrogen pathway and hence marker hormone sensitivity and favorable prognosis in breast carcinoma. There is growing evidence that members of the trefoil peptide family are involved in active maintenance of the integrity of gastrointestinal mucosa and facilitate its repair (Poulsom, 1996; May & Westley, 1997).
Applications
pS2 positivity is preferentially expressed in hormone-dependent cells in breast cancer. Low concentrations of the protein have been associated with a poor prognosis (Foekens et al, 1990; Predine et al, 1992) while strong expression predicted responsiveness to endocrine treatment (Racca et al, 1995). The five year recurrence-free survival and overall survival were 85% and 95% respectively for estrogen receptor (ER)+/progesterone receptor (PR)+/pS2+ tumors, but only 50% and 54% for patients with ER + /PR + /pS2- tumors (Foekens et al, 1990).
In another study of 72 advanced breast cancer cases, 76% of pS2+ cases had stable disease, complete remission or partial remission as compared with 37% of the pS2- cases. The authors proposed that pS2 may help differentiate the 35-50% of ER+ breast cancer patients who do not clinically respond to hormone therapy and the rare ER - patients who do (Schwartz et al, 1991). However, further studies have found that while pS2 immunostaining correlates with age, estrogen receptor and progesterone receptor status, it is not an independent prognostic factor or an indicator of increased survival in breast cancer (Speider et al, 1994; Wysocki et al, 1994).
pS2 is widely distributed throughout the gastrointestinal tract, particularly adjacent to damaged mucosa (Collier et al, 1995; Poulsom, 1996). It is consistently expressed in superficial and foveolar epithelium of non-neoplastic gastric mucosa and in 66% of gastric carcinomas, but has little value as a prognostic indicator (Machado et al, 1996). Colorectal carcinoma stains with pS2 to a lesser extent but this too lacks statistical significance (Shousha et al, 1993).
Expression in normal pancreas is usually absent but it can be seen focally within occasional ducts in chronic pancreatitis and it is prominent in pancreatic adenocarcinoma and ampullary tumors (Collier et al, 1995).
Comments
We employ clone PS2.1.
References
•Collier JD, Bennet MK, Bassendine MF, Lendrum R 1995. Immunolocalization of pS2, a putative growth factor, in growth factor, in pancreatic carcinoma. Journal of Gastroenterology and Hepatology; 10: 394-400.
•Foekens JA, Riol M-C, Seguin P 1990. Prediction of relapse and survival in breast cancer patients by pS2 protein status. Cancer Research: 50: 3832-3837.
•Machado JC, Carneiro F, Ribeiro P 1996. pS2 protein expression in gastric carcinoma. An immunohistochemical and immunoradiometric study. European Journal of Cancer; 32A: 585-1590.
•May FE, Westley BR 1997. Trefoil proteins: their role in normal and malignant cells. Journal of Pathology; 183: 4-7.
•Poulsom R 1996. Trefoil peptides. Bailli6es Clinical Gastroenterology 10: 113-134.
•Predine J, Spyratos F, Prud'homme JF 1992. Enzyme-linked immunosorbent assay of pS2 in breast cancers, benign tumours, and normal breast tissues: correlation with prognosis and adjuvant hormone therapy. Cancer 69; 2116-2123.
•Racca S, Conti G, Pietribiasi F 1995. Correlation between pS2 protein positivity, steroid receptor status and other prognostic factors in breast cancer. International Journal of Biological Markers 10: 87-93.
•Schwartz LH, Koerner FC, Edgerton SM 1991. pS2 expression and response to hormonal therapy in patients with advanced breast cancer. Cancer Research 51: 624-628.
•Shousha S, Luqmani YA, Sannino P et al 1993. pS2 immunostaining of colorectal carcinoma. Modern Pathology 6: 446-448.
•Speider P, Stolzlechner J, Haider K et al 1994. pS2 protein status fails to be an independent prognostic factor in an average breast cancer population. Anticancer Research 14: 2125-2130.
•Wysocki SJ, Iacopetta BJ, Ingram DM 1994. Prognostic significance of pS2 mRNA in breast cancer. European Journal of Cancer 30A: 1882-1884.
Bibliografia
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
Biogenex (PS2.1), Dako (BC04) and Labvision Corp (PS2.1, R47-94).
Fixation/Preparation
The antigen survives formalin fixation and is enhanced by HIER.
Background
pS2 is a 6660 Dalton, 60 amino acid secretory polypeptide protein that was isolated from the breast carcinoma cell line MCF-7. It belongs to a recently described family of trefoil-shaped growth factors which includes human intestinal trefoil factor (hITF) and human spasmolytic polypeptide (hSP). Although its exact function is unknown, it is believed to be part of a steroid-dependent stimulatory pathway. An estrogen-regulated protein, it has been studied as a marker of an intact estrogen pathway and hence marker hormone sensitivity and favorable prognosis in breast carcinoma. There is growing evidence that members of the trefoil peptide family are involved in active maintenance of the integrity of gastrointestinal mucosa and facilitate its repair (Poulsom, 1996; May & Westley, 1997).
Applications
pS2 positivity is preferentially expressed in hormone-dependent cells in breast cancer. Low concentrations of the protein have been associated with a poor prognosis (Foekens et al, 1990; Predine et al, 1992) while strong expression predicted responsiveness to endocrine treatment (Racca et al, 1995). The five year recurrence-free survival and overall survival were 85% and 95% respectively for estrogen receptor (ER)+/progesterone receptor (PR)+/pS2+ tumors, but only 50% and 54% for patients with ER + /PR + /pS2- tumors (Foekens et al, 1990).
In another study of 72 advanced breast cancer cases, 76% of pS2+ cases had stable disease, complete remission or partial remission as compared with 37% of the pS2- cases. The authors proposed that pS2 may help differentiate the 35-50% of ER+ breast cancer patients who do not clinically respond to hormone therapy and the rare ER - patients who do (Schwartz et al, 1991). However, further studies have found that while pS2 immunostaining correlates with age, estrogen receptor and progesterone receptor status, it is not an independent prognostic factor or an indicator of increased survival in breast cancer (Speider et al, 1994; Wysocki et al, 1994).
pS2 is widely distributed throughout the gastrointestinal tract, particularly adjacent to damaged mucosa (Collier et al, 1995; Poulsom, 1996). It is consistently expressed in superficial and foveolar epithelium of non-neoplastic gastric mucosa and in 66% of gastric carcinomas, but has little value as a prognostic indicator (Machado et al, 1996). Colorectal carcinoma stains with pS2 to a lesser extent but this too lacks statistical significance (Shousha et al, 1993).
Expression in normal pancreas is usually absent but it can be seen focally within occasional ducts in chronic pancreatitis and it is prominent in pancreatic adenocarcinoma and ampullary tumors (Collier et al, 1995).
Comments
We employ clone PS2.1.
References
•Collier JD, Bennet MK, Bassendine MF, Lendrum R 1995. Immunolocalization of pS2, a putative growth factor, in growth factor, in pancreatic carcinoma. Journal of Gastroenterology and Hepatology; 10: 394-400.
•Foekens JA, Riol M-C, Seguin P 1990. Prediction of relapse and survival in breast cancer patients by pS2 protein status. Cancer Research: 50: 3832-3837.
•Machado JC, Carneiro F, Ribeiro P 1996. pS2 protein expression in gastric carcinoma. An immunohistochemical and immunoradiometric study. European Journal of Cancer; 32A: 585-1590.
•May FE, Westley BR 1997. Trefoil proteins: their role in normal and malignant cells. Journal of Pathology; 183: 4-7.
•Poulsom R 1996. Trefoil peptides. Bailli6es Clinical Gastroenterology 10: 113-134.
•Predine J, Spyratos F, Prud'homme JF 1992. Enzyme-linked immunosorbent assay of pS2 in breast cancers, benign tumours, and normal breast tissues: correlation with prognosis and adjuvant hormone therapy. Cancer 69; 2116-2123.
•Racca S, Conti G, Pietribiasi F 1995. Correlation between pS2 protein positivity, steroid receptor status and other prognostic factors in breast cancer. International Journal of Biological Markers 10: 87-93.
•Schwartz LH, Koerner FC, Edgerton SM 1991. pS2 expression and response to hormonal therapy in patients with advanced breast cancer. Cancer Research 51: 624-628.
•Shousha S, Luqmani YA, Sannino P et al 1993. pS2 immunostaining of colorectal carcinoma. Modern Pathology 6: 446-448.
•Speider P, Stolzlechner J, Haider K et al 1994. pS2 protein status fails to be an independent prognostic factor in an average breast cancer population. Anticancer Research 14: 2125-2130.
•Wysocki SJ, Iacopetta BJ, Ingram DM 1994. Prognostic significance of pS2 mRNA in breast cancer. European Journal of Cancer 30A: 1882-1884.
Bibliografia
Manual of diagnostic antibodies for immunohistology / Anthony S.-Y. Leong, Kumarasen Cooper, F. Joel W.-M. Leong.
