Top

Published in:

01-09-2012

Galectin Labeling of Cells from Paraffinized Tissues May Serve as a Diagnostic Tool in the Detection and Classification of Thyroid Carcinomas

Authors: Rebeca Palacios-Corona, Francisco González-Salazar, Ricardo M. Cerda-Flores, Javier Vargas-Villarreal, Eduardo González-Murillo, Hugo Gutiérrez-Hermosillo, Hugo Gómez-Rueda, Lorena Tamez-Peña, Gerardo Rivera-Silva, Héctor Eloy Tamez-Pérez

Published in: Endocrine Pathology | Issue 3/2012

Abstract

This study seeks to determine whether the relative levels of attachment to galectins 1 and 3 of cells from thyroid tissues embedded in paraffin blocks can differentiate thyroid tumors from normal tissues. A total of 48 thyroid paraffin sample blocks from 4 groups of patients were analyzed: 12 samples served as controls, 12 samples were from patients with thyroid adenoma, 12 samples were from patients with thyroid follicular carcinoma, and 12 samples were from patients with thyroid papillary carcinoma. The relative attachment of cells to galectins 1 and 3 antigens was determined using the InnoCyte™ ECM Cell Adhesion kit at different cell sample concentrations. All of the samples from thyroid tissue preparations showed attachment to galectins 1 and 3. The samples from tissues with a diagnosis of adenoma, follicular and papillary carcinoma showed an increased adherence to galectins 1 and 3 relative to the controls. Significant differences were found between the means of the adherent cells from the adenomas compared with the follicular and papillary carcinoma samples. When the outcomes from the galectins 1 and 3 cell surface binding were compared, no statistical differences were found. The cells from adenoma and carcinoma samples show more adhesion to galectins 1 and 3 than cells from the control samples. The samples prepared from follicular and papillary carcinomas show more cells adherent to galectins 1 and 3 than those from the adenomas.

Rabinovich GA. (1999) Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy. Cell Death Differ 6:711-21.PubMedCrossRef

Barondes SH, Cooper DNW, Gitt MA and Leffler H (1994) Galectins: structure and function of a large family of animal lectins. J. Biol. Chem 269: 20807- 20810.PubMed

Leffler H, Carlsson S, Hedlund M, Qian Y, Poirier F. (2004) Introduction to galectins. Glycoconj J.;19:433-40.PubMedCrossRef

Dumic J, Dabelic S, Flögel M. (2006) Galectin-3: an open-ended story. Biochim Biophys Acta 1760: 616–635.PubMedCrossRef

Patterson RJ, Wang JL. (2002) Intracellular function of galectins. Biochim Biophys Acta 1572: 263–270.PubMedCrossRef

Cooper D. (2002) Galectinomics: finding themes in complexity. Biochim Biophys Acta 1572: 209–231.PubMedCrossRef

Henderson NC, Sethi T. (2009) The regulation of inflammation by galectin-3. Immunol Rev 230:160–171.PubMedCrossRef

Camby I, Le Mercier M, Lefranc F, Kiss R. (2006) Galectin-1: a small protein with major functions. Glycobiology 16: 137–157.CrossRef

Raimond J, Zimonjic DB, Mignon C, Mattei M, Popescu NC, Monsigny M, Legrand A. (1997) Mapping of the galectin-3 gene (LGALS3) to human chromosome 14 at region 14q21-22. Mamm Genome 8: 706-7.PubMedCrossRef

10.

Liu FT, Yang RY, Saegusa J, Chen HY, Hsu DK. (2011) Galectins in regulation of apoptosis. Adv Exp Med Biol 705: 431-42.PubMedCrossRef

11.

Du C, Wang Y. (2011) The immunoregulatory mechanisms of carcinoma for its survival and development. J Exp Clin Cancer Res 30: 12.PubMedCrossRef

12.

Nakahara S, Raz A. (2007) Regulation of cancer-related gene expression by galectin-3 and the molecular mechanism of its nuclear import pathway. Cancer Metastasis Rev 26: 605-10.PubMedCrossRef

13.

Balan V, Nangia-Makker P, Avraham A. (2010) Galectins as Cancer Biomarkers Cancer 2: 592-610.

14.

Xu XC, Nl-Naggar AK, Lotan R. (1995) Differential expression of galectin-1 and galectin-3 in thyroid tumors: potential diagnostic implications. Am J Pathol 147: 815-22.PubMed

15.

Chiu CG, Strugnell SS, Griffith OL, Jones SJ, Gown AM, Walker B, Nabi IR, Wiseman SM. (2010) Diagnostic utility of galectin-3 in thyroid cancer. Am J Pathol 176: 2067-81.PubMedCrossRef

16.

Ríos Moreno MJ, Galera-Ruiz H, De Miguel M, López MI, Illanes M, Galera-Davidson H. (2011) Inmunohistochemical profile of solid cell nest of thyroid gland. Endocr Pathol 22: 35-9.PubMedCrossRef

17.

Levy R, Grafi-Cohen M, Kraiem Z, Kloog Y. (2010) Galectin-3 promotes chronic activation of K-Ras and differentiation block in malignant thyroid carcinomas. Mol Cancer Ther 9:2208-19.PubMedCrossRef

18.

Išić T, Savin S, Cvejić D, Marečko I, Tatić S, Havelka M, Paunović I. (2010) Serum Cyfra 21.1 and galectin-3 protein levels in relation to immunohistochemical cytokeratin 19 and galectin-3 expression in patients with thyroid tumors. J Cancer Res Clin Oncol 136:1805-12.PubMedCrossRef

19.

Kaliszewski K, Łukieńczuk T, Dobosz T, Rzeszutko M, Sadakierska-Chudy A. (2006) Analysis of expression of LGALS3BP gene in thyroid tissues and peripheral blood lymphocytes in patients with papillary thyroid cancer].Endokrynol Pol 57 Suppl A:38-44.PubMed

20.

Saussez S, Glinoer D, Chantrain G, et al. (2008) Serum galectin-1 and galectin-3 levels in benign and malignant nodular thyroid disease. Thyroid 18:705-712.PubMedCrossRef

21.

Fernández PL, Merino MJ, Gómez M, et al. (1997) Galectin-3 and laminin expression in neoplastic and non-neoplastic thyroid tissue. J Pathol 181: 80-86.PubMedCrossRef

22.

Hill M, Mazal D, Biron VA, Pereira L, Ubillos L, Berriel E, Ahmed H, Freire T, Rondán M, Vasta GR, Liu FT, Iglesias MM, Osinaga E. (2010) A novel clinically relevant animal model for studying galectin-3 and its ligands during colon carcinogenesis. J Histochem Cytochem. 58:553-65.PubMedCrossRef

23.

Hedinger C, Dillwyn-Williams E, Sobin LH. (1989) The WHO histologicalclassification of thyroid tumors: A commentary on the second edition. Cancer 63: 908–911.PubMedCrossRef

24.

Arteel GE. (2008) Alcohol-induced oxidative stress in the liver: in vivo measurements. Methods Mol Biol 447:185-97.PubMedCrossRef

25.

Rabinovich GA, Rubinstein N. (2001) [Galectins: a novel family of proteins involved in the regulation of the immune response. Implications in immunopathological processes]. Medicina (B Aires) 61: 85-92.

26.

Barroeta JE, Baloch ZW, Lal P, Pasha TL, Zhang PJ, LiVolsi VA. (2006) Diagnostic value of differential expression of CK19, Galectin-3, HBME-1, ERK, RET, and p16 in benign and malignant follicular-derived lesions of the thyroid: an immunohistochemical tissue microarray analysis. Endocr Pathol 17: 225-34.PubMedCrossRef

27.

Martins L, Matsuo SE, Ebina KN, Kulcsar MA, Friguglietti CU, Kimura ET. (2002) Galectin-3 messenger ribonucleic acid and protein are expressed in benign thyroid tumors. J Clin Endocrinol Metab 87: 4806-10.PubMedCrossRef

28.

Kaliszewski K, Łukieńczuk T, Dobosz T, Rzeszutko M, Sadakierska-Chudy A (2006) [Analysis of expression of LGALS3BP gene in thyroid tissues and peripheral blood lymphocytes in patients with papillary thyroid cancer]. Endokrynol Pol 57 Suppl A: 38-44.PubMed

29.

Song X, Xia B, Stowell SR, Lasanajak Y, Smith DF, Cummings RD. (2009) Novel fluorescent glycan microarray strategy reveals ligands for galectins. Chem Biol 16: 36-47.PubMedCrossRef

30.

Ohannesian DW, Lotan D, Lotan R. (1994) Concomitant increases in galectin-1 and its glycoconjugate ligands (carcinoembryonic antigen, lamp-1, and lamp-2) in cultured human colon carcinoma cells by sodium butyrate. Cancer Res 54: 5992-6000.PubMed

31.

Ohannesian DW, Lotan D, Thomas P, Jessup JM, Fukuda M, Gabius HJ, Lotan R. (1995) Carcinoembryonic antigen and other glycoconjugates act as ligands for galectin-3 in human colon carcinoma cells. Cancer Res 55: 2191-9.PubMed

32.

Bresalier RS, Byrd JC, Wang L, Raz A. (1996) Colon cancer mucin: a new ligand for the beta-galactoside-binding protein galectin-3. Cancer Res 56: 4354-7.PubMed

33.

Greco C, Vona R, Cosimelli M, Matarrese P, Straface E, Scordati P, Giannarelli D, Casale V, Assisi D, Mottolese M, Moles A, Malorni W. (2004) Cell surface overexpression of galectin-3 and the presence of its ligand 90 k in the blood plasma as determinants in colon neoplastic lesions. Glycobiology. 14: 783-92.PubMedCrossRef

34.

Kopitz J, von Reitzenstein C, Burchert M, Cantz M, Gabius HJ. (1998) Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture. J Biol Chem 273:11205-11.PubMedCrossRef

35.

Kopitz J, von Reitzenstein C, André S, Kaltner H, Uhl J, Ehemann V, Cantz M, Gabius HJ. (2001) Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3. J Biol Chem 276: 35917-23.PubMedCrossRef

36.

Wester K, Wahlund E, Sundström C, et al. (2000) Paraffin section storage and immunohistochemistry. Effects of time, temperature, fixation, and retrieval protocol with emphasis on p53 protein and MIB1 antigen. Appl Immunohistochem Mol Morphol 8: 61-70.PubMedCrossRef

37.

Atkins D, Reiffen KA, Tegtmeier C, Winther H, Bonato M, Storkel S. (2004) Immunohistochemical Detection of EGFR in Paraffin-embedded Tumor Tissues : Variation in Staining Intensity Due to Choice of Fixative and Storage Time of Tissue Sections. J Histochem Cytochem 52: 893-901.PubMedCrossRef

Title: Galectin Labeling of Cells from Paraffinized Tissues May Serve as a Diagnostic Tool in the Detection and Classification of Thyroid Carcinomas
Authors: Rebeca Palacios-Corona
Francisco González-Salazar
Ricardo M. Cerda-Flores
Javier Vargas-Villarreal
Eduardo González-Murillo
Hugo Gutiérrez-Hermosillo
Hugo Gómez-Rueda
Lorena Tamez-Peña
Gerardo Rivera-Silva
Héctor Eloy Tamez-Pérez
Publication date: 01-09-2012
Publisher: Springer US
Published in: Endocrine Pathology / Issue 3/2012
Print ISSN: 1046-3976
Electronic ISSN: 1559-0097
DOI: https://doi.org/10.1007/s12022-012-9215-x

Live Webinar | 27-06-2024 | 18:00 (CEST)

Keynote webinar | Spotlight on medication adherence

Reserve your place

Live: Thursday 27th June 2024, 18:00-19:30 (CEST)

WHO estimates that half of all patients worldwide are non-adherent to their prescribed medication. The consequences of poor adherence can be catastrophic, on both the individual and population level.

Join our expert panel to discover why you need to understand the drivers of non-adherence in your patients, and how you can optimize medication adherence in your clinics to drastically improve patient outcomes.

Prof. Kevin Dolgin

Prof. Florian Limbourg

Prof. Anoop Chauhan

Developed by: Springer Medicine

Obesity Clinical Trial Summary

At a glance: The STEP trials

A round-up of the STEP phase 3 clinical trials evaluating semaglutide for weight loss in people with overweight or obesity.

Developed by: Springer Medicine

Keynote webinar | Spotlight on medication adherence

Springer Medicine

Abstract

Please log in to get access to this content

Other articles of this Issue 3/2012

Necrotizing Infundibuloneurohypophysitis: Case Report and Literature Review

Relapse of Acute Myeloid Leukemia at the Pituitary Gland: A Case Report and Review of Literature

Fine Needle Aspiration Biopsy of an Unusual Follicular Adenoma with Sebaceous-Like Features

ACTH-Secreting Pheochromocytoma with False-Negative ACTH Immunohistochemistry

True Mixed Medullary Papillary Carcinoma of the Thyroid: a Case Report with Low Blood Calcitonin Levels

Correlation Between Histological Subtypes and MRI Findings in Clinically Nonfunctioning Pituitary Adenomas

Keynote webinar | Spotlight on medication adherence

Live: Thursday 27th June 2024, 18:00-19:30 (CEST)

At a glance: The STEP trials