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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

Specific detection of S100P with 18-9 MAb. A, Western blotting analysis of the recombinant GST-S100P protein versus GST alone and of S100P protein in extracts from MDA-MB 231 breast carcinoma cells, HeLa cervical carcinoma cells, HeLa-R variant cells with reduced tumorigenicity [9], and HeLa-R cells transfected with S100P cDNA. B, RT PCR analysis of the same cell lines for the expression of S100P and S100A4 genes, respectively.
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Figure 2: Specific detection of S100P with 18-9 MAb. A, Western blotting analysis of the recombinant GST-S100P protein versus GST alone and of S100P protein in extracts from MDA-MB 231 breast carcinoma cells, HeLa cervical carcinoma cells, HeLa-R variant cells with reduced tumorigenicity [9], and HeLa-R cells transfected with S100P cDNA. B, RT PCR analysis of the same cell lines for the expression of S100P and S100A4 genes, respectively.

Mentions: In addition to the mRNA analysis, we wanted to elucidate S100P protein expression by immunohistochemistry in various human tissues. For this purpose, we used a newly generated anti-S100P monoclonal antibody 18-9 produced against a recombinant fusion GST-S100P antigen. First, we verified the specificity of the MAb (Fig. 2). In Western blotting, 18-9 MAb reacted well with the purified GST-S100P protein, but not with the GST alone. The MAb also recognized an 11 kDa protein in HeLa cells and HeLa-R cells transfected with S100P cDNA, whereas no protein was detected in MDA-MB 231 cells and mock-transfected HeLa-R cells (Fig. 2A). These negative cell lines do not express S100P, but show expression of S100A4, as described previously [9,15,17] and also clearly demonstrated in Figure 2B by RT PCR.


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)

Specific detection of S100P with 18-9 MAb. A, Western blotting analysis of the recombinant GST-S100P protein versus GST alone and of S100P protein in extracts from MDA-MB 231 breast carcinoma cells, HeLa cervical carcinoma cells, HeLa-R variant cells with reduced tumorigenicity [9], and HeLa-R cells transfected with S100P cDNA. B, RT PCR analysis of the same cell lines for the expression of S100P and S100A4 genes, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 2: Specific detection of S100P with 18-9 MAb. A, Western blotting analysis of the recombinant GST-S100P protein versus GST alone and of S100P protein in extracts from MDA-MB 231 breast carcinoma cells, HeLa cervical carcinoma cells, HeLa-R variant cells with reduced tumorigenicity [9], and HeLa-R cells transfected with S100P cDNA. B, RT PCR analysis of the same cell lines for the expression of S100P and S100A4 genes, respectively.
Mentions: In addition to the mRNA analysis, we wanted to elucidate S100P protein expression by immunohistochemistry in various human tissues. For this purpose, we used a newly generated anti-S100P monoclonal antibody 18-9 produced against a recombinant fusion GST-S100P antigen. First, we verified the specificity of the MAb (Fig. 2). In Western blotting, 18-9 MAb reacted well with the purified GST-S100P protein, but not with the GST alone. The MAb also recognized an 11 kDa protein in HeLa cells and HeLa-R cells transfected with S100P cDNA, whereas no protein was detected in MDA-MB 231 cells and mock-transfected HeLa-R cells (Fig. 2A). These negative cell lines do not express S100P, but show expression of S100A4, as described previously [9,15,17] and also clearly demonstrated in Figure 2B by RT PCR.

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