Abstract
Secretory leukocyte protease inhibitor is a multifunctional protein with a variety of activities attributed to it. A significant increase in the expression of Secretory leukocyte protease inhibitor was noticed in syncytiotrophoblasts following differentiation of cytotrophoblasts in to syncytiotrophoblasts by addition of Forskolin. Using the BeWo cells which are derived from choriocarcinoma, the effect of addition of progesterone and estradiol on the expression of Secretory leukocyte protease inhibitor by Reverse Transcription Polymerase Chain Reaction was assessed. It was found that while addition of low concentration of progesterone resulted in a significant increase in expression of Secretory leukocyte protease inhibitor, addition of estradiol even at high concentration had no effect. The specificity of effect of progesterone was established by the observation that addition of Progesterone along with progesterone receptor antagonist (RU484) resulted in decrease in the level of expression of Secretory leukocyte protease inhibitor. These results suggest that Secretory protease leukocyte protease inhibitor is a progesterone regulated gene.
Highlights
Secretory Leukocyte Protease Inhibitor (SLPI) is a nonglycosylated hydrophobic cationic 12 kDa protein with a variety of activities attributed to it
In view of the apparent differential regulation of SLPI in rodents and human and considering the fact that SLPI structure is highly conserved, it was of interest to investigate the regulation of SLPI by P4 in BeWo cells which is derived from human choriocarcinoma
A time course study on the effect of incubation of BeWo cells with and without P4 (1 μM) for 0, 6, 12 and 24h on the expression of SLPI was carried out to assess the expression of SLPI by RT-PCR
Summary
Secretory Leukocyte Protease Inhibitor (SLPI) is a nonglycosylated hydrophobic cationic 12 kDa protein with a variety of activities attributed to it. It is known that it exhibits a variety of activities, which includes anti-protease, anti-inflammatory, anti-bacterial activities [2]. SLPI is a highly conserved protein and murine SLPI appears to be structurally highly similar to human SLPI [3]. It is reported that while the human SLPI is regulated by progesterone (P4) [4], in the case of rat, it is regulated by estrogen [5]. In view of the apparent differential regulation of SLPI in rodents and human and considering the fact that SLPI structure is highly conserved, it was of interest to investigate the regulation of SLPI by P4 in BeWo cells which is derived from human choriocarcinoma
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