S100 protein family is small calcium-binding proteins with two EF-hand motifs and comprises more than 20 proteins in human. Although S100A proteins are known to play important roles in proinflammatory responses including damage-associated molecular pattern (DAMP) signaling and in the establishment of pregnancy, the expression of S100As have not been determined in the uterine endometrium during the estrous cycle in pigs. Thus, this study was performed to investigate expression and localization of S100A8, S100A9, and S100A12 in the uterine endometrial tissues during the estrous cycle in pigs. Real-time RT-PCR analysis showed that S100A8, S100A9, and S100A12 mRNAs were expressed in the uterine endometrium during the estrous cycle with higher levels on days 15 and 18 of the estrous cycle than the other days of cycle. Immunohistochemistry analysis showed that S100A9 and S100A12 proteins were mainly localized to the immune cells in the uterine endometrium. Especially, S100A9- and S100A12-positive immune cells were detected in the uterine blood vessels on day 15 of the estrous cycle, and also localized to stroma near to luminal epithelium on days 0 and 18 of the estrous cycle. These results showed that S100As were expressed in the uterine endometrium during the estrous cycle in a cyclic stage-specific manner, and these proteins were localized to the immune cells in the endometrium. These suggest that immune cells expressing S100A proteins may be recruited into the endometrium during the estrous cycle and play an important role in regulating endometrial function in pigs.

저활용 단백질로부터 칼슘 결합물질을 분리하기 위해 돼지 육골분과 진주담치 단백질을 단백질 분해 효소인 alcalase를 이용하여 가수분해물을 제조하였고, 체내 흡수가 용이한 3 kDa 이하로 한외여과 하였다. 돼지 육골분 가수분해물은 Mono Q 컬럼을 통해 분리하였고, 진주담치가수분해물의 경우 Q-Sepharose로 분리 하여 각각 2개, 3개의 peptide fraction을 얻어 각 fraction의 칼슘 결합력을 측정하였다. 그 결과 MBM F2와 Mussel F3에서 가장 높은 칼슘결합력을 나타내었고, 따라서 본 연구 결과로 얻어진 가수분해물들은 칼슘 보충 소재로 활용될 수 있다고 판단된다.

To prepare calcium-binding peptides as calcium supplement, barley proteins were hydrolyzed using Flavourzyme for 18 h and the hydrolysates were ultra-filtered under 3 kDa as a molecular weight. The resultant filtered peptides were fractionated using ion exchange and normal-phase high performance liquid chromatography. Then each fraction that was obtained was determined for its calcium-binding activity to isolate the calcium-binding peptides. As a result, the highest calcium-binding peptide fraction was obtained, and the results suggest that barley protein hydrolysates can be used as a calcium supplement.

청미래덩굴 뿌리(Smilacis rhizoma)로부터 칼슘과 결합하는 물질을 분리하고자 열수로 추출한 추출물을 ion exchange, normal-phase HPLC 및 gel filtration chromatogarphy를 이용하여 칼슘 결합 물질을 순차적으로 분리하였다. 그 결과 ion exchange chromatography에서 7개의 major peaks를 얻었으며, 이 중 F6 fraction이 0.083 mM로 칼슘과 가장 높은 결