인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
Mucus hydrogels, formed by enormous “mucin” glycoproteins, protect vulnerable epithelial tissues from pathogens and chemical/physical damage. Mucins use natively disordered, heavily O-glycosylated segments thousands of amino acids in length to form physical barriers and trap foreign particles. Recently, unexpected functions of other, folded regions of mucins have been revealed. By determining high-resolution structures of key mucin regions, we discovered specific copper binding sites. Most notably, the intestinal mucin, MUC2, has two juxtaposed copper binding sites, one for Cu2+ and the other for Cu1+. Respiratory mucins, in turn, have only a single, Cu2+ binding site. We showed in biochemical and cell culture assays that MUC2 prevents copper toxicity by blocking futile redox cycling and the squandering of dietary antioxidants. Nevertheless, the presence of MUC2 does not prevent uptake of copper, an important nutritional trace metal, into cells. To further explore the physiological role of copper binding by mucins, we have constructed a transgenic mouse with MUC2 mutations compromising both Cu1+ and Cu2+ binding. This tool enables research into the role of MUC2 copper binding in copper uptake, copper signaling, mucosal immunity, and excretion of excess metal. This research was funded by the U.S.-Israel Binational ScienceFoundation.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
최근 본 자료 전체보기
