Immunohistochemical expression of heparanase isoforms and syndecan-1 proteins in colorectal adenomas

Submitted: 23 November 2015
Accepted: 8 February 2016
Published: 17 February 2016
Abstract Views: 1358
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The proteoglycan syndecan-1 and the endoglucuronidases heparanase-1 and heparanase-2 are involved in molecular pathways that deregulate cell adhesion during carcinogenesis. Few studies have examined the expression of syndecan-1, heparanase-1 and mainly heparanase-2 proteins in non-neoplastic and neoplastic human colorectal adenoma tissues. The aim of this study was to analyze the correlation among the heparanase isoforms and the syndecan-1 proteins through immunohistochemical expression in the tissue of colorectal adenomas. Primary anti-human polyclonal anti-HPSE and anti-HPSE2 antibodies and primary anti-human monoclonal anti-SDC1 antibody were used in the immunohistochemical study. The expressions of heparanase-1 and heparanase-2 proteins were determined in tissue samples from 65 colorectal adenomas; the expression of syndecan-1 protein was obtained from 39 (60%) patients. The histological type of adenoma was tubular in 44 (67.7%) patients and tubular-villous in 21 (32.3%); there were no villous adenomas. The polyps were <1.0 cm in size in 54 (83.1%) patients and ≥1.0 cm in 11 (16.9%). The images were quantified by digital counter with a computer program for this purpose. The expression index represented the relationship between the intensity expression and the percentage of positively stained cells. The results showed that the average of heparanase-1, heparanase-2 and syndecan-1 expression index was 73.29 o.u./µm², 93.34 o.u./µm², and 55.29 o.u./µm², respectively. The correlation between the heparanase-1 and syndecan-1 expression index was positive (R=0.034) and significant (P=0.035). There was a negative (R= -0.384) and significant (P=0.016) correlation between the expression index of heparanase-1 and heparanase-2. A negative (R= -0.421) and significant (P=0.008) correlation between the expression index of heparanase-2 and syndecan-1 was found. We concluded that in colorectal adenomas, the heparanase-1 does not participate in syndecan-1 degradation; the heparanase-2 does not stimulate syndecan-1 degradation by the action of heparanase-1, and the heparanase-2 may be involved in the modulation of the heparanase-1 activity.

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J. Waisberg, ABC Medical School

Department of Surgery

Full Professor

 

T.R. Theodoro, ABC Medical School
Department of Biochemistry, ABC Medical School
L.L. Matos, ABC Medical School
Department of Community Health and Epidemiology, ABC Medical School
F.B. Orlandi, ABC Medical School
 
R.L. Serrano, ABC Medical School
 
M.A.S. Pinhal, ABC Medical School

Department of Biochemistry

Full professor

How to Cite

Waisberg, J., Theodoro, T., Matos, L., Orlandi, F., Serrano, R., Saba, G., & Pinhal, M. (2016). Immunohistochemical expression of heparanase isoforms and syndecan-1 proteins in colorectal adenomas. European Journal of Histochemistry, 60(1). https://doi.org/10.4081/ejh.2016.2590