Endometrial cancer is the fourth-most-common cancer in women in western Europe and
USA. The majority of cases occur in post-manopausal women. Uncontrolled inflammation,
associated with increased production of prostaglandins (PG) in endometrial tissue, can lead
to development of endometrial cancer. The prostaglandins stimulate cell proliferation, cell
adhesion, cell migration and angiogenesis and therefore accelerate tumor growth. Retinoid
acid by binding to the retinoic acid receptor (RAR) and the retinoid X receptor (RXR)
stimulates cell differentiation, and thus has protective role.
Enzyme AKR1B1is involved in synthesis of inflammatory mediators and it acts as a PG
synthase that convert PGH2 to PGF2α. AKR1B1 catalyzes the reduction of lipid
peroxidation products, such as 4-hydroxynonenal (HNE) and indirectly stimulates
transcription factor NF-κB, which then stimulates expression of cytokines and
inflammatory mediators, such as cyclooxygenease-2 (COX-2). Enzyme AKR1B10
catalyzes the reduction of retinals to retinols and indirectly prevents synthesis of retinoid
acid, which is involved in cell proliferation and cell diferentiation. AKR1B10 catalyzes
also reduction of isoprenyl aldehydes and is involved in prenylation of small GTPases,
which regulate cell proliferation and apoptosis. In this research we analyzed presence of
AKR1B1 and AKR1B10 in samples of cancerous and adjacent noncancerous endometrial
tissues.
We investigated the AKR1B1 and AKR1B10 protein levels in 30 paired samples by SDS –
PAGE electrophoresis, western blot analysis and chemiluminiscence detection. Both
protein levels were significantly decreased in tumorous tissues, compared to controls. We
confirmed presence of both proteins in endometrial cancer also at the cellular level with
immunohistochemical staining. AKR1B1 and AKR1B10 were located predominantly in
the cytoplasm of the epithelial cells of cancerous endometrial tissue.
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