Abstract
BackgroundParalemmin-1 is a phosphoprotein lipid-anchored to the cytoplasmic face of membranes where it functions in membrane dynamics, maintenance of cell shape, and process formation. Expression of paralemmin-1 and its major splice variant (Δ exon 8) as well as the extent of posttranslational modifications are tissue- and development-specific. Paralemmin-1 expression in normal breast and breast cancer tissue has not been described previously.ResultsParalemmin-1 mRNA and protein expression was evaluated in ten breast cell lines, 26 primary tumors, and 10 reduction mammoplasty (RM) tissues using real time RT-PCR. Paralemmin-1 splice variants were assessed in tumor and RM tissues using a series of primers and RT-PCR. Paralemmin-1 protein expression was examined in cell lines using Western Blots and in 31 ductal carcinomas in situ, 65 infiltrating ductal carcinomas, and 40 RM tissues using immunohistochemistry. Paralemmin-1 mRNA levels were higher in breast cancers than in RM tissue and estrogen receptor (ER)-positive tumors had higher transcript levels than ER-negative tumors. The Δ exon 8 splice variant was detected more frequently in tumor than in RM tissues. Protein expression was consistent with mRNA results showing higher paralemmin-1 expression in ER-positive tumors.ConclusionsThe differential expression of paralemmin-1 in a subset of breast cancers suggests the existence of variation in membrane dynamics that may be exploited to improve diagnosis or provide a therapeutic target.
Highlights
Paralemmin-1 is a phosphoprotein lipid-anchored to the cytoplasmic face of membranes where it functions in membrane dynamics, maintenance of cell shape, and process formation
We found paralemmin-1 to be more frequently expressed in breast cancers than in reduction mammoplasty tissues and more highly expressed in estrogen receptor (ER)-positive breast cancer as compared to ER-negative cancers
To investigate the relationship between paralemmin-1 expression and ER status, in the present study we examined the expression of paralemmin-1 in additional breast cancer and non-tumorigenic breast cell lines (Table 1)
Summary
Paralemmin-1 is a phosphoprotein lipid-anchored to the cytoplasmic face of membranes where it functions in membrane dynamics, maintenance of cell shape, and process formation. Paralemmin-1 is a phosphoprotein first identified in brain tissue and is thought to play a role in controlling cell shape, plasma membrane dynamics, and cell motility [1,2]. The Δ exon 8 splice variant has been shown to interact with the third intracellular loop of the D3 dopamine receptor in the hippocampus and cerebellum in rat brain as well as in glial and neuronal cell cultures [2,3,4]. These studies suggest that the Δ exon 8 splice variant may have distinct functions in specific tissues
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