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
Resolving spatial protein dynamics in native human epithelial tissues presents a significant technical challenge, particularly in inherently curved or unevenly mounted specimens. Here, we introduce an image processing pipeline for high-resolution, compartment-based analysis of protein localization, using the native three-dimensional architecture of the human anterior lens epithelium and capsule complex as a robust ex vivo proof-of-principle platform for precise cell segmentation and quantitative analysis. This platform integrates whole-mount immunostaining, 3D confocal imaging, computational tissue flattening, digital segmentation, and spatial regression to quantitatively map subcellular protein distributions at the tissue scale. To demonstrate the utility of this approach, we examined the spatial distribution of αB-crystallin (CRYAB), a stress-associated small heat shock protein, and βB2-crystallin (CRYBB2), a predominantly structural lens protein, in specimens obtained during cataract surgery. We observed a marked accumulation of CRYAB in epithelial cells at the capsule edge following both laser and manual capsulorhexis, indicating a localized stress response to surgical intervention. In contrast, CRYBB2 distribution remained unaffected. Furthermore, both proteins exhibited consistent cytoplasmic localization, while only CRYBB2 occasionally showed exclusive nuclear accumulation. This pipeline offers a scalable framework for quantitatively resolving protein localization in native epithelial architectures, using CRYAB and CRYBB2 as examples of how stress-associated changes can be spatially mapped in situ within the human lens.
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.
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