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ORIGINAL ARTICLE Table of Contents   
Year : 2009  |  Volume : 26  |  Issue : 4  |  Page : 134-139
Significance of a galactose specific plant lectin for the differential diagnosis of adenocarcinoma cells in effusion

1 Division of Cytopathology, Regional Cancer Centre, Trivandrum, Kerala, India
2 Division of Cancer Research, Regional Cancer Centre, Trivandrum, Kerala, India

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Date of Web Publication5-Apr-2010


Background : Distinguishing adenocarcinoma cells from reactively proliferated mesothelial cells and macrophages is one of the greatest challenges in the cytodiagnosis of effusions. Aberrant glycosylation of cell surface glycoconjugates is emblematic to malignancy, and lectins being an important class of probes to demonstrate these aberrations, lectin cytochemistry is of great interest to differentiate adenocarcinoma cells from reactive mesothelial cells.
Aim : The present study analyzed the potential of a plant lectin to distinguish malignant cells from reactive mesothelial cells and macrophages.
Materials and Methods : Snake gourd lectin (SGL) was isolated, purified and conjugated to horse radish peroxidase (HRP) and incubated with the cells of benign (46) as well as malignant (39) effusions using the standard immunocytochemical method with diaminobenzidine as the chromogen. The lectin-bound areas were quantitatively assessed as mild, moderate and intense binding.
Statistical Analysis : The mean score for benign and malignant effusions were statistically analyzed. Student's 't'-test was performed to assess the significance.
Results : The lectin HRP complex bind to the cytoplasm of benign and malignant cells as well as macrophages. A significantly higher score for intense binding (P = 0.001) was found to differentiate malignant cells from reactive mesothelial cells. Macrophages showed intense irregular binding.
Conclusions : SGL binding assay can play a role in the differential diagnosis of metastatic adenocarcinoma in effusions.

Keywords: Effusion cytology; adenocarcinoma; differential diagnosis; lectin binding

How to cite this article:
Sujathan K, Jayasree K, Remani P. Significance of a galactose specific plant lectin for the differential diagnosis of adenocarcinoma cells in effusion. J Cytol 2009;26:134-9

How to cite this URL:
Sujathan K, Jayasree K, Remani P. Significance of a galactose specific plant lectin for the differential diagnosis of adenocarcinoma cells in effusion. J Cytol [serial online] 2009 [cited 2022 Jan 17];26:134-9. Available from:

   Introduction Top

Cytological examination can often help in the diagnostic distinction between benign and malignant effusions. But, it fails to allow a definite diagnosis in about 15% of the cases. [1],[2],[3] The changing therapy and the different laboratory processing methods cause the reactively proliferated mesothelial cells to appear so atypical that differentiation from metastatic adenocarcinoma becomes difficult. [4] The conventional histochemical stains such as Periodic acid Schiffs (PAS)-diastase and alcian blue hyluronidase are not reliable discriminents. [5] Another approach is to supplement the conventional cytological evaluation of effusions with the utilization of immunocytochemical demonstration of the tumor-associated antigens. A very wide variety of antibodies against markers of epithelial differentiation are available for immunocytochemistry, including antibodies against intermediate filaments, epithelial membrane, oncofetal proteins, secretary markers, neuroendocrine proteins and organ-related antigens. [6],[7],[8],[9],[10] But, it is still not known which antibody is the most suitable one for this purpose, as normal and reactively proliferated mesothelial cells also express most of these markers. [11] The sensitivity for the detection of malignant cells in serous effusion ranges from 20% to >90% in different reports. Interest has therefore been focused on identifying reliable methods to supplement the conventional cytologic method to differentiate malignant cells from benign reactive cells. Earlier, we had reported the advantages of a combined approach to morphological features in Papanicolaou (PAP) and May-Grünwald-Giemsa (MGG)-stained smears and a modified cell block technique in the cytodiagnosis of effusions [4] and the significance of silver-stained nuclear organiser regions in discriminating reactive mesothelial cells from metastatic adenocarcinoma cells in effusions. [12] Lectin cytochemistry is another area under investigation.

Lectins are proteins or glycoproteins of nonimmune origin, extracted from plants and animals. Lectins have been used in many areas of diagnostic investigations, especially those related to changes in the expression of membrane and cytoplasmic glycoconjugates. [13],[14],[15],[16],[17],[18] As neoplastic transformation of cells is associated with altered cell surface glycoconjugates, a large number of studies have been performed to differentiate malignant cells from benign cells using different lectins. [19],[20],[21],[22] N-acetyl-D-galactosamine-specific jackfruit lectin (JFL) has been reported to be useful in the diagnosis of various tumors. [23] Recently, we have reported the potential of JFL in discriminating reactive mesothelial cells from metastatic adenocarcinoma cells. [24] In the present study, a 56 kD galactose-specific plant lectin isolated from the seeds of snake gourd was conjugated to horse radish peroxidase (HRP) and the cellular binding patterns of this lectin-HRP complex were studied in benign reactively proliferated mesothelial cells, macrophages and in metastatic adenocarcinoma cells to evaluate its potential in the differential diagnosis of adenocarcinoma cells in effusions.

   Materials and Methods Top

Isolation of lectin

Lectin from the seeds of snake gourd was isolated, purified and conjugated to HRP type IV according to the technique described elsewhere. [15] In short, the deskinned seeds were ground to flour. The flour was defatted by soaking in petroleum ether for 24 hours at room temperature. The defatted flour was stirred well on a magnetic stirrer with 250 ml of 0.01 M phosphate-buffered saline (PBS) overnight at 4°C. Thereafter, all procedures were carried out at 4°C. The extract was filtered through a nylon gauze and spun for 30 min at 20,000 g. The supernatant was collected and ammonium sulphate was added with constant stirring to a concentration of 40% saturation and was kept overnight. The precipitate was removed by centrifugation at 20,000 g for 30 min. The clear supernatant was then adjusted to 60% saturation by further addition of ammonium sulphate, with constant stirring and was kept overnight. The precipitate thus formed was collected by centrifugation as above, dissolved in 20 ml of PBS and was then dialyzed extensively against three changes of PBS (pH 7.2). Any precipitate formed was removed by centrifugation and the clear supernatant was collected. The isolated lectin was then purified by affinity chromatography on cross-linked guar gum. The molecular weight of the lectin was determined by gel filtration on Sephadex G-100 (Sigma Chemical Company, St. Louis, Missouri, USA). The purity of the lectin was confirmed on electrophoretic analysis.

Conjugation of snake gourd lectin to HRP type IV

Ten milligrams of the purified lectin was dissolved in bicarbonate buffer (pH 9.5) and sufficient amount of the specific sugar (0.4 mg of b galactose in 1 ml) to get a 20 M concentration and was kept at room temperature for 1 hour. Activated HRP was added to this and mixed gently for 3 hours at room temperature. Ten milligrams of sodium borohydride was then added and left for 1 hour at room temperature. Then, the pH was reduced to 6.9 by adding 1N HCl and was kept in the refrigerator overnight. The lectin HRP mixture was then allowed to run through the column containing Sephadex G-200 and the effluents with peak absorbance at 280 nm were kept at 4°C until used for staining.

Selection of samples for lectin binding assay

Alcohol-fixed smears from 90 serous effusions received during the year 2007-2008 were used for this study. The study was approved by the institute review board as well as the ethical committee. The study subjects included 63 samples of pleural effusions and 27 peritoneal fluids. Informed consents were obtained from all subjects. The samples were concentrated by routine centrifugation at 2000 rpm for five minutes. Three smears from each of the samples were prepared, one for the routine Papanicolaou staining, one for lectin staining and the other for special stains such as PAS/alcian blue, etc. The rest of the cell buttons were used for cellblock preparation for further study if required. Cytologically, the samples were grouped into three categories: malignant, benign and atypical. The malignant group contained 39 samples of adenocarcinoma from histologically diagnosed cases of primary adenocarcinoma. This group included carcinomas of the ovary (21), breast (9), lungs (5), stomach (2) and endometrium (2). The cytologically negative samples (46) were from patients in whom a benign cause of effusion had been known. Among these, 28 samples were obtained from patients with pulmonary tuberculosis referred from the sanatorium for chest diseases and 18 from patients with liver cirrhosis referred from the medical gastroenterology department of the medical college. The cytologically atypical group contained five samples, of which four pleural fluids were from patients with pulmonary tuberculosis and one ascitic fluid from a known case of carcinoma of the ovary. All such atypical samples were further studied in cell block sections and were followed-up with cytology of the repeat tap, except one sample.

Lectin staining method

The smears were rehydrated and immersed in 0.3% hydrogen peroxide in methanol for 30 minutes to block the endogenous peroxidase activity. Incubating with 3% bovine serum albumin for 30 min at room temperature blocked the nonspecific binding. After removing the bovine serum albumin by blotting, the smears were incubated with snake gourd lectin (SGL) to a final concentration of 0.06 mg/ml overnight at 4°C. Negative controls were included in each batch of the slides. The smears were stained with 30 mg% 3'-3'-Diaminobenzidine-containing hydrogen peroxide for five minutes, washed with distilled water (three changes) and counter-stained with Harris hematoxylin for 1 minute. The slides were then dehydrated and mounted in DPX.

The slides were observed under 10× objective first and subsequently confirmed under 40× objective. In malignant effusions, unequivocal malignant cells, and in benign effusions, the benign mesothelial cells were studied for their lectin reaction. In effusions that were categorized as atypical, the atypical-looking cells alone were studied. One hundred cells were studied in each sample. The intensity of staining was assessed as mild (+), moderate (++) and intense (+++). Statistical analysis was carried out to determine the mean score for each category and Student's 't'-test was performed to assess the significance.

   Results Top

The SGL-HRP conjugate-bound cells were stained brown in color [Figure 1]b, d, f. The negative controls did not give this brown color. Smears that were incubated with galactose solution also failed to give the brown color. The SGL binding was confined to the cytoplasm of malignant and benign cells. It was not able to appreciate membrane and cytoplasmic binding distinctly. None of the cells showed nuclear staining. No background staining was observed. No significant differences in staining pattern were observed between cells of pleural and peritoneal fluids. The quantitative difference in the staining pattern of benign mesothelial and malignant cells is shown in [Table 1] and [Figure 2].

Univariate analysis of the different grades of SGL binding pattern in reactive and malignant effusion is shown in [Table 1]. A higher percentage of cells with mild grade of staining (+) were observed in benign effusions. The mean value for mild grade of binding was 71.36, with a standard deviation of 23.97 for benign effusions, whereas it was only 5.36 with a standard deviation of 8.72 for malignant effusions. The percentage of cells with moderate (++) grade of staining was higher in malignant effusions, but the difference was not very significant as that of the other two grades of binding. The mean values were 26.64 and 37.7, with standard deviations of 21.95 and 25.42, respectively. Intense grade of staining was found to be very high in malignant effusions, with a mean value of 3.11 and a standard deviation of 15.06 for benign effusions and with a mean value of 58.54 and a standard deviation of 28.16 for malignant effusions. A higher number of cells with mild grade of staining favors a diagnosis of benign (P value <0.001) and intense grade of staining for malignancy (P value <0.001). The percentage of cells with moderate and intense grade was found to vary in malignant effusions. Among the samples with atypical cells suspicious of malignancy, two showed a higher percentage of cells with moderate and intense grade of staining, of which one showed cells with an irregular coarse granular staining pattern, similar to that observed in macrophages. The other one was an ascitic fluid sample from a known case of carcinoma of the ovary, which was demonstrated to have malignant cells in cell block sections and in cytology of the repeat tap. The remaining atypical samples showed SGL binding similar to that of benign effusions. The pattern of SGL binding was diffuse and uniform in both malignant and benign cells. The intensity of binding was significantly higher in malignant cells [Figure 1]d. In macrophages, the SGL binding was intense, as observed in malignant cells, but the pattern was irregular and granular [Figure 1]f. Samples with mucinous adenocarcinoma showed a predominantly intense grade of staining.

   Discussion Top

The cytomorphological changes during the process of malignant transformation are either preceded or accompanied by biochemical alterations in the neoplastic cells. Among these alterations, expression of cell surface glycoproteins plays a vital role because this is mainly involved in signal transduction phenomena. The ability of plant lectins to make such alterations visible to distinguish normal and neoplastic cells was reported as early as 1963. [20],[21],[22],[25] The present study substantiates the significance of another plant lectin in diagnostic cytopathology. In several reports referred above, the lectin binding has been described as membrane and cytoplasmic binding. In cytology smears, it is difficult to differentiate membrane and cytoplasmic staining distinctly as seen in tissue sections owing to the presence of plasma membrane all over the cell. Moreover, lectins show a greater affinity to cell surface glycoproteins. The reactively proliferated mesothelial cells in benign effusions for which a benign cause of effusion had been known showed a mostly mild grade of staining. A similar finding for the reactive mesothelial cells have been reported with HRP-conjugated JFL also. [24] The number of cells with mild grade of staining was significantly lower and cells with a moderate and intense binding pattern were higher in all samples of malignancies.

Another study of effusions using a panel of ten lectins has also reported that the lectin binding pattern with Helix pomatia agglutinin (HPA), soybean agglutinin (SBA) and Ulex europeaus agglutinin (UEA) are likely to be useful markers for identification of reactive mesothelial cells and adenocarcinoma cells in cytology. [26] However, they could not define the pattern of lectin expression in the normal mesothelium. The present study also could not analyse the SGL binding pattern in the normal mesothelium as it is quite difficult to obtain normal mesothelial cells. The cells present in most of the benign effusions are considered to have some sort of reactive changes.

Abramenko et al. [27] included a battery of five lectins in his panel of markers of monoclonal antibodies for cell identification in pleural effusion and found that the panel was found effective in identifying malignant cells in all cytologically positive samples as well as in 13 samples from 21 cytologically negative malignant effusions, peanut agglutinin (PNA), HPA, SBA, Laburnum alpinum agglutinin and Lathyrus ciceria isolectins were the lectins he has included in his panel. In the present study, none of the cytologically negative samples could be diagnosed to have malignancy by analyzing the lectin binding pattern, but two of the cytologically atypical samples showed a significantly higher number of cells with a moderate and intense grade of staining. The staining pattern in one of these cases was irregular and granular. Cell block, PAS-diastase and mucin studies of this sample were negative. Review of the PAP-stained slide revealed that this sample contained a large number of macrophages, and that the atypical-looking cells were macrophages. This sample was from a case of pulmonary tuberculosis. The SGL-binding intensity in the macrophages was similar to that of malignant cells, but the pattern was totally different. Macrophages showed intense irregular coarse granular binding. A similar binding pattern has been reported for pulmonary macrophages [28] and in effusions [24] with HRP-conjugated JFL. PNA has been reported to be useful in identifying macrophages/histiocytes. [29],[30] Another cytologically atypical sample in which a higher number of cells showed moderate and intense staining was reported to have malignant cells in the cell block study. Repeat sample was positive in cytology also. This sample was from a known case of carcinoma of the ovary. Of the other three atypical samples that gave SGL binding similar to that of benign effusions, two were negative in follow-up with repeat tap. The remaining one case was not available for follow-up. Thus, SGL binding analysis helped to make a definite diagnosis in four of the five cytologically atypical cases.

Among the adenocarcinomas, the intensity of SGL binding was not uniform in all the samples. The number of cells with a moderate and intense binding pattern was found to vary owing to the different origin of the cells. Samples from carcinoma of the ovary cases showed a slight predominance of moderate grade of binding, except for two samples that contained cells from mucinous cystadenocarcinoma, which showed predominance of intense grade of binding. Of the nine samples containing cells from carcinoma of the breast, four showed mainly moderate grades of binding, whereas the other five samples from this group showed predominantly intense grade of binding. All these samples (9) were from cases of infiltrating duct carcinoma. Among the five samples containing cells from adenocarcinoma of the lungs, four showed a predominance of moderate grade of binding and the remaining one showed intense binding, which was from a case of mucinous adenocarcinoma. Samples from known cases of gastric carcinomas and enodometrium showed a predominantly intense grade of binding. Another interesting finding we observed was the difference in intensity of SGL binding in mucinous adenocarcinoma from other types. The intensity of staining was found to be higher in mucin-secreting adenocarcinoma, suggesting that SGL mainly recognizes intracytoplasmic mucin. This information may help in differentiating mucin-secreting adenocarcinoma from other types. As no uniform pattern could be observed for any specific type of tumors other than mucinous adenocarcinoma, SGL binding pattern cannot be suggested for identification of the primary. Leven et al. [31] have used a panel of lectins comprising Con A, Dolichos biflorus agglutinin, soybean agglutinin, UEA and wheat germ agglutinin (WGA) to differentiate metastatic adenocarcinoma cells from reactive mesothelial cells in effusions. They also used the standard avidin-biotin peroxidase complex technique. Even though their sample size was only 15, they found that the UEA is helpful in distinguishing between benign and malignant effusions. Sixty per cent of the adenocarcinomas showed intense staining whereas none of the cells in benign effusions showed a positive staining, suggesting that UEA positivity is indicative of malignancy. The present study observed positive SGL binding for both benign and malignant cells, but the intensity of the binding was different. However, intense SGL binding was observed in a few of the reactively proliferated mesothelial cells of some of the reactive effusions also, which were not sufficient enough to show statistical significance. The morphological difference between static mesothelial cells and reactive mesothelial cells are likely to be due to the differences in the cytoskeletal composition, with accompanying changes in the cell surface lectin-binding pattern. [26] Such an explanation can be offered for the overlapping intense binding pattern found in a few of the reactive mesothelial cells of the reactive effusions. It is reasonable to assume that the changes caused to the cytoskeletal composition might have enhanced the lectin receptor status.

The difficulty in the cytodiagnosis of effusions is mainly in differentiating metastatic adenocarcinoma cells from reactive mesothelial cells. The present study has demonstrated the value of SGL binding to differentiate benign cells from malignant cells. A significantly higher number of cells with moderate and intense, regular, uniform SGL binding in the cytoplasm favors a diagnosis of malignancy. The intense SGL binding in malignant cells may be due to the fact that SGL may be able to identify incomplete nonsialated forms of membrane glycoconjugates expressed more at the surface of malignant cells, as reported earlier by Ross et al. [32] This technique is relatively simple and inexpensive compared to any of the immunocytochemical methods. Even though a few of the reactively proliferated mesothelial cells and macrophages showed SGL binding similar to that of adenocarcinoma cells, only malignant effusions showed a statistically significant difference. Macrophages can be differentiated by their coarse irregular granular binding pattern. Hence, the present study suggests that SGL binding analysis can have some value in the differential diagnosis of adenocarcinoma in effusions even though this cannot be suggested as a single reliable marker. It is relatively a new area of application in the field of cytopathology. Studies with a larger sample size and follow-up are required to assess the sensitivity and specificity of this method. Also, studies with different lectins of different carbohydrate specificities may help in identifying new epitopes on malignant cells, which may provide a further insight into the biology of malignant cells.

   References Top

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Correspondence Address:
K Sujathan
Assistant Professor, Molecular Pathology, Division of Cytopathology, Regional Cancer Centre, Medical College Campus, Thiruvananthapuram, Kerala
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Source of Support: None, Conflict of Interest: None

DOI: 10.4103/0970-9371.62181

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