Observational studyEuropean journal of histochemistry : EJH2016
Immunohistochemical expression of heparanase isoforms and syndecan-1 proteins in colorectal adenomas.
Observational study in European journal of histochemistry : EJH, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.
- Elevated heparanase expression is associated with poor prognosis in breast cancer: a study based on systematic review and TCGA data.Oncotarget · 2017Pooled it
- Novel approach for quantification of multiple immunofluorescent signals using histograms and 2D plot profiling of whole-section panoramic images.Scientific reports · 2021Article
- Heparanase modulation by Wingless/INT (Wnt).Molecular biology reports · 2021Article
- Salvianolic acid B attenuates renal interstitial fibrosis by regulating the HPSE/SDC1 axis.Molecular medicine reports · 2020Article
- Histochemistry as a versatile research toolkit in biological research, not only an applied discipline in pathology.European journal of histochemistry : EJH · 2018Article
- Histochemistry today: Detection and location of single molecules.European journal of histochemistry : EJH · 2017Article
- Heparanase overexpression down-regulates syndecan-1 expression in a gallbladder carcinoma cell line.The Journal of international medical research · 2017Article
- Is there still room for novelty, in histochemical papers?European journal of histochemistry : EJH · 2016Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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