(Her-2) expression statuses were determined by immunohistochemistryĪnalysis in the hospital's pathology department. Progesterone receptor (PR) and Erb-B2 receptor tyrosine kinase 2 Joint Committee on Cancer staging system ( 9, 10). Tumor stage was pathologically determined according to the American Had received chemotherapy or radiotherapy prior to surgery. The specimens were obtainedĭuring surgical resection, cut into 0.3–0.5 cm 2 sectionsĪnd stored in liquid nitrogen prior to experimentation. The age of patients ranged fromģ7–81, with an average age of 56 years. Patients of breast invasive ductal carcinoma treated at theĪffiliated Hospital of Guilin Medical University (Guangxi, China)īetween August 2013 and June 2014. Materials and methods Clinical breast tumor tissuesīreast tumor tissues were collected from 33 female Variant (ER-α30), was identified, which is encoded by a distinctĮR-α mRNA and enhanced the malignant biological behaviors of humanīreast cancer MDA-MB-231 cells. In the present study, a novel 30 kDa hER-α splice Potentially promoting the progression of breast cancer to moreĪggressive phenotypes, including loss of responsiveness to These variants may be induced during theįormation and progression of breast cancer, influencing theīehavior of breast cancer cells via uncharacterized mechanisms, and Protein products of which cannot be detected using commerciallyĪvailable ER-α antibodies. Splicing resulting in the expression of variant isoforms, the
These patients, but that its pre-mRNA undergoes alternative This general pattern, a proportion of ER-α-negative patients withīreast cancer are responsive to anti-estrogen treatment ( 6). Respond effectively to anti-estrogens, including tamoxifen, whereasĮR-α-negative patients do not ( 4, 5). (anti-estrogen) therapy in patients with breast cancer ( 3).
Widely accepted predictive marker of the effectiveness of endocrine
Reported to serve significant roles in the development, clinicalĭiagnosis and treatment of cancer ( 2).
Variants from the same gene thus, a limited number of genes canĮncode a variety of different proteins ( 1). The results of the present study indicated that ER‑α30 might represent a potential biomarker for breast cancer.Īlternative splicing produces multiple mRNA splice The 30 kDa protein was expressed in stably transfected MDA‑MB‑231 cells, and the overexpression of ER‑α30 in MDA‑MB‑231 cells enhanced malignant biological behaviors, including cellular proliferation, migration and invasion in vitro. The expression of ER‑α30 was associated with ER‑α66‑negative and progesterone receptor‑negative breast cancer. The ER‑α30 sequence lacked a ligand‑binding domain and a ligand‑dependent transcriptional activation domain but retained the N‑terminal transcriptional activation domain, the DNA‑binding domain and a partial hinge domain, and possesses a unique 10‑amino‑acid domain. In the present study, a novel hER‑α splice variant, ER‑α30, was identified and cloned from clinical breast cancer tissue. Since the early 1990s, multiple human estrogen receptor‑α (hER-α) splice variants have been identified, of which the majority contain ≥1 deleted exon, and some are expressed as proteins with modified functions from the wild‑type 66 kDa hER-α (ER‑α66).
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