Publication: Nuclear envelope organization in papillary thyroid carcinoma
Authors
Fischer, A.H. ; Taysavang, P. ; Weber, C.J. ; Wilson, K.L.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Papillary thyroid carcinomas (PTCs) have
characteristic nuclear shape changes compared to
follicular-type thyroid epithelium. We tested the
hypothesis that the altered nuclear shape results from
altered distribution or expression of the major structural
proteins of the nuclear envelope. Lamin A, lamin B1,
lamin C, lamin B receptor (LBR), lamina-associated
polypeptide 2 (LAP2), emerin, and nuclear pores were
examined. PTC7s with typical nuclear features by H&E
were compared to non-neoplastic thyroid and follicular
neoplasms using confocal microscopy, and semiquantitative
immunoblotting. Lamin A/C, lamin B1,
LAP2, emerin, and nuclear pores al1 extend throughout
the grooves and intranuclear inclusions of PTC. Their
distribution and fluorescent intensity is not predictably
altered relative to nuclear envelope irregularities. By
immunoblotting, the abundance (per cell) and
electrophoretic mobilities of lamin A, lamin B1, lamin
C, emerin, and LAP2 proteins do not distinguish PTC,
normal thyroid, or follicular neoplasms. These results do
not support previously published predictions that lamin
A/C expression is related to a loss of proliferative
activity. At least three LAP2 isoforms are identified in
normal and neoplastic thyroid. LBR is sparse or
undetectable in al1 the thyroid samples. The results
suggest that the irregular nuclear shape of PTC is not
determined by these nuclear envelope structural proteins
per se. We review the structure of the nuclear envelope,
the major factors that determine nuclear shape, and the
possible functional consequences of its alteration in
PTC.
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