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Function of HSP90 and p23 in the telomerase complex of thyroid tumors.
Pathol Res Pract. 2003; 199(9):573-9.PR

Abstract

Recently, studies on endocrine tumors revealed a potential role of telomerase in the dedifferentiation and/or malignant transition of these tumors. Telomerase is a ribonucleoprotein complex that includes the telomerase RNA component (hTR), the telomerase-associated protein (TP1), and the telomerase catalytic subunit (hTERT). Previously, the chaperones p23 and HSP90 have been described as additional telomerase regulators. To test whether the interactions of these genes are reflected in the dedifferentiation of thyroid tumors, we determined their mRNA and/or protein expression in 30 normal (tumor-free) thyroid tissues (NT), 35 follicular adenomas (FAD), 42 papillary carcinomas (PTC), 38 follicular carcinomas (FTC), 25 poorly differentiated carcinomas (PDTC), and 34 undifferentiated carcinomas (UTC). We then compared the results with telomerase activity. RT-PCR analysis revealed that TP1 was ubiquitously expressed. hTR was found in 50-94% of malignant tumors, in contrast to 7% of NT and 26% of FAD. hTERT was clearly associated with aggressive biological behavior. Ninety-two to 100% of the malignant tumors were positive for hTERT protein, whereas NT and FAD were negative in 100% and 94%, respectively. HSP90 mRNA and protein showed a close relationship to hTERT. p23 protein was negative in NT and positive in 3% of FAD, 39% of FTC, 40% of PTC, 44% of PDTC and 47% of UTC. High telomerase activity was measurable in hTERT and HSP90-positive tissues only. Our data show that the common expression of hTERT and HSP90 regulates telomerase activity in thyroid carcinomas. Chaperone p23 is involved in the telomeric complex to a lesser extent, but its expression is stronger in carcinomas than in non-malignant thyroid tissues. The expression profile of telomerase components represents an additional prognostic marker that may identify more aggressive thyroid tumors.

Authors+Show Affiliations

Department of Pathology, Otto-von-Guericke-University and 2 City Hospital, Magdeburg, Germany. carsten.boltze@medizin.uni-magdeburg.deNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

14621192

Citation

Boltze, Carsten, et al. "Function of HSP90 and P23 in the Telomerase Complex of Thyroid Tumors." Pathology, Research and Practice, vol. 199, no. 9, 2003, pp. 573-9.
Boltze C, Schneider-Stock R, Roessner A, et al. Function of HSP90 and p23 in the telomerase complex of thyroid tumors. Pathol Res Pract. 2003;199(9):573-9.
Boltze, C., Schneider-Stock, R., Roessner, A., Quednow, C., & Hoang-Vu, C. (2003). Function of HSP90 and p23 in the telomerase complex of thyroid tumors. Pathology, Research and Practice, 199(9), 573-9.
Boltze C, et al. Function of HSP90 and P23 in the Telomerase Complex of Thyroid Tumors. Pathol Res Pract. 2003;199(9):573-9. PubMed PMID: 14621192.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Function of HSP90 and p23 in the telomerase complex of thyroid tumors. AU - Boltze,Carsten, AU - Schneider-Stock,Regine, AU - Roessner,Albert, AU - Quednow,Claudia, AU - Hoang-Vu,Cuong, PY - 2003/11/19/pubmed PY - 2004/6/23/medline PY - 2003/11/19/entrez SP - 573 EP - 9 JF - Pathology, research and practice JO - Pathol Res Pract VL - 199 IS - 9 N2 - Recently, studies on endocrine tumors revealed a potential role of telomerase in the dedifferentiation and/or malignant transition of these tumors. Telomerase is a ribonucleoprotein complex that includes the telomerase RNA component (hTR), the telomerase-associated protein (TP1), and the telomerase catalytic subunit (hTERT). Previously, the chaperones p23 and HSP90 have been described as additional telomerase regulators. To test whether the interactions of these genes are reflected in the dedifferentiation of thyroid tumors, we determined their mRNA and/or protein expression in 30 normal (tumor-free) thyroid tissues (NT), 35 follicular adenomas (FAD), 42 papillary carcinomas (PTC), 38 follicular carcinomas (FTC), 25 poorly differentiated carcinomas (PDTC), and 34 undifferentiated carcinomas (UTC). We then compared the results with telomerase activity. RT-PCR analysis revealed that TP1 was ubiquitously expressed. hTR was found in 50-94% of malignant tumors, in contrast to 7% of NT and 26% of FAD. hTERT was clearly associated with aggressive biological behavior. Ninety-two to 100% of the malignant tumors were positive for hTERT protein, whereas NT and FAD were negative in 100% and 94%, respectively. HSP90 mRNA and protein showed a close relationship to hTERT. p23 protein was negative in NT and positive in 3% of FAD, 39% of FTC, 40% of PTC, 44% of PDTC and 47% of UTC. High telomerase activity was measurable in hTERT and HSP90-positive tissues only. Our data show that the common expression of hTERT and HSP90 regulates telomerase activity in thyroid carcinomas. Chaperone p23 is involved in the telomeric complex to a lesser extent, but its expression is stronger in carcinomas than in non-malignant thyroid tissues. The expression profile of telomerase components represents an additional prognostic marker that may identify more aggressive thyroid tumors. SN - 0344-0338 UR - https://www.unboundmedicine.com/medline/citation/14621192/Function_of_HSP90_and_p23_in_the_telomerase_complex_of_thyroid_tumors_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0344-0338(04)70462-8 DB - PRIME DP - Unbound Medicine ER -