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The calcium-binding protein S100P in normal and malignant human tissues.

Parkkila S, Pan PW, Ward A, Gibadulinova A, Oveckova I, Pastorekova S, Pastorek J, Martinez AR, Helin HO, Isola J - BMC Clin Pathol (2008)

Bottom Line: Moderate signals were also detected in the stomach, duodenum, large intestine, prostate and leukocytes.At the protein level, the highest reactions for S100P were seen in the placenta and stomach.Based on our observations, S100P is widely expressed in both normal and malignant tissues.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Medical Technology, University of Tampere and Tampere University Hospital, Tampere, Finland. seppo.parkkila@uta.fi

ABSTRACT

Background: S100P is a Ca2+ binding protein overexpressed in a variety of cancers, and thus, has been considered a potential tumor biomarker. Very little has been studied about its normal expression and functions.

Methods: We examined S100P expression in normal human tissues by quantitative reverse transcription polymerase chain reaction and immunohistochemistry. S100P protein expression was also studied in a series of tumors, consisting of 74 ovarian, 11 pancreatic, 56 gastric, 57 colorectal, 89 breast and 193 prostate carcinomas using a novel anti-S100P monoclonal antibody.

Results: Among the normal tissues, the highest S100P mRNA levels were observed in the placenta and esophagus. Moderate signals were also detected in the stomach, duodenum, large intestine, prostate and leukocytes. At the protein level, the highest reactions for S100P were seen in the placenta and stomach. Immunostaining of tumor specimens showed that S100P protein is expressed in all the tumor categories included in the study, being most prevalent in gastric tumors.

Conclusion: Based on our observations, S100P is widely expressed in both normal and malignant tissues. The high expression in some tumors suggests that it may represent a potential target molecule for future diagnostic and therapeutic applications.

No MeSH data available.


Related in: MedlinePlus

Immunostaining of S100P protein in the breast (A,B), gastric (C), pancreatic (D) and ovarian (E,F) carcinomas.
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Figure 6: Immunostaining of S100P protein in the breast (A,B), gastric (C), pancreatic (D) and ovarian (E,F) carcinomas.

Mentions: The specificity of the 18-9 MAb was also evaluated by immunohistochemistry in comparison with the control MAb in parallel sections of the human stomach antrum (Fig. 3). Both antibodies revealed strong positive immunoreactions in the surface epithelial cells. The control MAb showed slightly stronger reactivity in the glands and lamina propria. All these results clearly demonstrated that the 18-9 MAb is specific for S100P protein and approved its use for the immunohistochemical analysis of S100P expression in human tissues (Figs 4 and 5) and carcinomas including breast (Fig. 6A,B), gastric (Fig. 6C), pancreatic (Fig. 6D), ovarian (Fig. 6E,F), prostate, and colon (Fig. 7) tumors. Immunohistochemical results indicated that the placenta indeed expresses very high levels of S100P protein in trophoblast cells (Fig. 4A,B). In the placenta as well as in all other positive tissues, the immunoreactions were strongest in the nuclei and weaker intracellular staining was also detectable. The normal gastric epithelium was another site which showed high immunoreactivity for S100P protein (Fig. 4C,D). In the body of the stomach, the immunostaining was localized to the mucus producing surface epithelial cells and chief cells of the gastric glands. Intestinal metaplasia was occasionally observed in some specimens of the gastric mucosa. The normal epithelium showed stronger immunostaining than the metaplastic epithelium (Fig. 4E). Esophageal mucosa showed immunopositivity which was mainly located to the most superficial epithelial cells (Fig. 4F). The pancreas and liver were mainly negative for S100P (Fig. 2G,H). In these tissues, some positive cell nuclei were occasionally associated with blood vessels, and by histological examination these cells were identified as granulocytes.


The calcium-binding protein S100P in normal and malignant human tissues.

Parkkila S, Pan PW, Ward A, Gibadulinova A, Oveckova I, Pastorekova S, Pastorek J, Martinez AR, Helin HO, Isola J - BMC Clin Pathol (2008)

Immunostaining of S100P protein in the breast (A,B), gastric (C), pancreatic (D) and ovarian (E,F) carcinomas.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2254630&req=5

Figure 6: Immunostaining of S100P protein in the breast (A,B), gastric (C), pancreatic (D) and ovarian (E,F) carcinomas.
Mentions: The specificity of the 18-9 MAb was also evaluated by immunohistochemistry in comparison with the control MAb in parallel sections of the human stomach antrum (Fig. 3). Both antibodies revealed strong positive immunoreactions in the surface epithelial cells. The control MAb showed slightly stronger reactivity in the glands and lamina propria. All these results clearly demonstrated that the 18-9 MAb is specific for S100P protein and approved its use for the immunohistochemical analysis of S100P expression in human tissues (Figs 4 and 5) and carcinomas including breast (Fig. 6A,B), gastric (Fig. 6C), pancreatic (Fig. 6D), ovarian (Fig. 6E,F), prostate, and colon (Fig. 7) tumors. Immunohistochemical results indicated that the placenta indeed expresses very high levels of S100P protein in trophoblast cells (Fig. 4A,B). In the placenta as well as in all other positive tissues, the immunoreactions were strongest in the nuclei and weaker intracellular staining was also detectable. The normal gastric epithelium was another site which showed high immunoreactivity for S100P protein (Fig. 4C,D). In the body of the stomach, the immunostaining was localized to the mucus producing surface epithelial cells and chief cells of the gastric glands. Intestinal metaplasia was occasionally observed in some specimens of the gastric mucosa. The normal epithelium showed stronger immunostaining than the metaplastic epithelium (Fig. 4E). Esophageal mucosa showed immunopositivity which was mainly located to the most superficial epithelial cells (Fig. 4F). The pancreas and liver were mainly negative for S100P (Fig. 2G,H). In these tissues, some positive cell nuclei were occasionally associated with blood vessels, and by histological examination these cells were identified as granulocytes.

Bottom Line: Moderate signals were also detected in the stomach, duodenum, large intestine, prostate and leukocytes.At the protein level, the highest reactions for S100P were seen in the placenta and stomach.Based on our observations, S100P is widely expressed in both normal and malignant tissues.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Medical Technology, University of Tampere and Tampere University Hospital, Tampere, Finland. seppo.parkkila@uta.fi

ABSTRACT

Background: S100P is a Ca2+ binding protein overexpressed in a variety of cancers, and thus, has been considered a potential tumor biomarker. Very little has been studied about its normal expression and functions.

Methods: We examined S100P expression in normal human tissues by quantitative reverse transcription polymerase chain reaction and immunohistochemistry. S100P protein expression was also studied in a series of tumors, consisting of 74 ovarian, 11 pancreatic, 56 gastric, 57 colorectal, 89 breast and 193 prostate carcinomas using a novel anti-S100P monoclonal antibody.

Results: Among the normal tissues, the highest S100P mRNA levels were observed in the placenta and esophagus. Moderate signals were also detected in the stomach, duodenum, large intestine, prostate and leukocytes. At the protein level, the highest reactions for S100P were seen in the placenta and stomach. Immunostaining of tumor specimens showed that S100P protein is expressed in all the tumor categories included in the study, being most prevalent in gastric tumors.

Conclusion: Based on our observations, S100P is widely expressed in both normal and malignant tissues. The high expression in some tumors suggests that it may represent a potential target molecule for future diagnostic and therapeutic applications.

No MeSH data available.


Related in: MedlinePlus