Galectin-3 and CD44v6 isoforms in the preoperative evaluation of thyroid nodules.

PURPOSE Thyroid cancer is the most frequently occurring endocrine malignancy; however, preoperative diagnosis of some lesions, in particular those with follicular histology, is difficult, and a consistent number of not otherwise-specified "follicular nodules" are surgically resected more for diagnosis than therapeutic purposes. In this study, we investigated whether the lectin-related molecules CD44v6 and galectin-3, the expression of which is altered during deregulated cell growth and malignant transformation, could be potential markers for improving the diagnostic accuracy of conventional cytology. MATERIALS AND METHODS A comparative immuno-chemical and molecular analysis was performed on 157 thyroid specimens representative of normal, benign, and malignant tissues, and on 36 cytologic samples obtained preoperatively by fine-needle aspiration biopsy from nonselected patients with palpable thyroid nodules. RESULTS Normal thyrocytes did not express galectin-3 nor CD44v6. Although the expression of CD44v6 isnegligible in thyroiditis, these molecules are variably detected in benign and malignant proliferative lesions. Interestingly, galectin-3 is never expressed in benign lesions, but it is invariably detected in cancers. A comparative evaluation of CD44v6 and galectin-3 expression in thyroid malignancies demonstrated that these molecules are coexpressed at the messenger RNA and protein level in almost all lesions. CONCLUSION Our findings suggest that CD44v6 and galectin-3 could be potential markers to preoperatively identify malignant transformed thyrocytes. Immunodetection of these molecules on cytologic specimens obtained by fine-needle aspiration biopsy is an accurate and improved method for selecting, on a molecular basis, those nodular lesions of the thyroid gland that need to be surgically resected.

[1]  M. P. Martegani,et al.  Structural variability of CD44v molecules and reliability of immunodetection of CD44 isoforms using mAbs specific for CD44 variant exon products. , 1999, The American journal of pathology.

[2]  P. De Giuli,et al.  Galectin-3 is a presurgical marker of human thyroid carcinoma. , 1998, Cancer research.

[3]  M. Hirashima,et al.  Human Ecalectin, a Variant of Human Galectin-9, Is a Novel Eosinophil Chemoattractant Produced by T Lymphocytes* , 1998, The Journal of Biological Chemistry.

[4]  K. Kashima,et al.  Expression of splice variants of CD44 in thyroid neoplasms derived from follicular cells , 1998, Pathology international.

[5]  E. Campo,et al.  GALECTIN‐3 AND LAMININ EXPRESSION IN NEOPLASTIC AND NON‐NEOPLASTIC THYROID TISSUE , 1997, The Journal of pathology.

[6]  Ronit Vogt Sionov,et al.  CD44: structure, function, and association with the malignant process. , 1997, Advances in cancer research.

[7]  J. Figge,et al.  Restricted patterns of CD44 variant exon expression in human papillary thyroid carcinoma. , 1996, Cancer research.

[8]  J. Figge,et al.  Deregulated alternative splicing of CD44 messenger RNA transcripts in neoplastic and nonneoplastic lesions of the human thyroid. , 1995, Cancer research.

[9]  R. Lotan,et al.  Differential expression of galectin-1 and galectin-3 in thyroid tumors. Potential diagnostic implications. , 1995, The American journal of pathology.

[10]  S. Agrawal Diagnostic accuracy and role of fine needle aspiration cytology in management of thyroid nodules , 1995, Journal of surgical oncology.

[11]  M. Posada,et al.  Improved method for mRNA extraction from paraffin-embedded tissues. , 1995, BioTechniques.

[12]  S. Barondes,et al.  Galectins. Structure and function of a large family of animal lectins. , 1994, The Journal of biological chemistry.

[13]  Richard D. Cummings,et al.  Galectins: A family of animal β-galactoside-binding lectins , 1994, Cell.

[14]  H. Gharib,et al.  Fine-needle aspiration biopsy of thyroid nodules: advantages, limitations, and effect. , 1994, Mayo Clinic proceedings.

[15]  Hedinger Ce Problems in the classification of thyroid tumors. Their significance for prognosis and therapy , 1993 .

[16]  A. Bartolazzi,et al.  Integrin expression in cutaneous malignant melanoma: Association of the α3/β1 heterodimer with tumor progression , 1993 .

[17]  J. Bell,et al.  Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[18]  N. Berger,et al.  Increased expression of the negative growth factor, galactoside-binding protein, gene in transformed thyroid cells and in human thyroid carcinomas. , 1992, Oncogene.

[19]  Martin Hofmann,et al.  A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cells , 1991, Cell.

[20]  V. Hogan,et al.  Evidence for the role of 34‐kDa galactoside‐binding lectin in transformation and metastasis , 1990, International journal of cancer.

[21]  I. Stamenkovic,et al.  CD44 is the principal cell surface receptor for hyaluronate , 1990, Cell.

[22]  C. Núñez,et al.  Fine-needle aspiration and needle biopsy of the thyroid gland. , 1989, Pathology annual.

[23]  A. Thor,et al.  Expression of ras oncogene p21 antigen in normal and proliferative thyroid tissues. , 1987, The American journal of pathology.