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Epithelial Biophysics at Molecular and Sub-Tissue Scales.
Epithelial Biophysics at Molecular and Sub-Tissue Scales.
- 자료유형
- 학위논문
- Control Number
- 0017162973
- International Standard Book Number
- 9798384336495
- Dewey Decimal Classification Number
- 612
- Main Entry-Personal Name
- Vachharajani, Vipul Tushar.
- Publication, Distribution, etc. (Imprint
- [S.l.] : Stanford University., 2024
- Publication, Distribution, etc. (Imprint
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- Physical Description
- 104 p.
- General Note
- Source: Dissertations Abstracts International, Volume: 86-03, Section: B.
- General Note
- Advisor: Dunn, Alexander.
- Dissertation Note
- Thesis (Ph.D.)--Stanford University, 2024.
- Summary, Etc.
- 요약Cell-cell adhesion and apicobasal polarity are defining characteristics of epithelial tissues that enabled the development of multicellular life. In this thesis, I describe two projects that aim to address questions about each of these fundamental processes.First, I present work using live-cell imaging to study the physical mechanism of lumen formation in Madin-Darby Canine Kidney (MDCK) cell spheroids, a canonical cell-culture model for lumenogenesis. We find that in this system, lumen shape reflects basic geometrical considerations tied to the establishment of apico-basal polarity. A physical model incorporating both cell geometry and intraluminal pressure can account for our observations as well as cases in which pressure plays a dominant role.Next, I present a study characterizing the single-molecule mechanics of an understudied class of cell adhesion molecules. Afadin is an essential actin-binding protein that is associated with both adherens and tight junctions. Using a single-molecule magnetic tweezers assay, we probed the mechanical stability of the bonds between the Afadin PDZ domain and the intracellular domains of two of its binding partners, Nectin-1 and JAM-A. We found that both ligands formed remarkably stable bonds with Afadin-PDZ at forces up to 10 pN. Our data suggest that the relatively-understudied complexes of afadin with JAM-A and Nectin-1 may function in parallel with cadherin-based adhesions to transmit forces across cell-cell junctions.
- Subject Added Entry-Topical Term
- Physiology.
- Subject Added Entry-Topical Term
- Pathogens.
- Subject Added Entry-Topical Term
- Fourier transforms.
- Subject Added Entry-Topical Term
- Cell adhesion & migration.
- Subject Added Entry-Topical Term
- Disease.
- Subject Added Entry-Topical Term
- Permeability.
- Subject Added Entry-Topical Term
- Microscopy.
- Subject Added Entry-Topical Term
- Extracellular matrix.
- Subject Added Entry-Topical Term
- Spheroids.
- Subject Added Entry-Topical Term
- Bond strength.
- Subject Added Entry-Topical Term
- Morphogenesis.
- Subject Added Entry-Topical Term
- Biophysics.
- Subject Added Entry-Topical Term
- Cellular biology.
- Subject Added Entry-Topical Term
- Developmental biology.
- Subject Added Entry-Topical Term
- Mathematics.
- Added Entry-Corporate Name
- Stanford University.
- Host Item Entry
- Dissertations Abstracts International. 86-03B.
- Electronic Location and Access
- 로그인을 한후 보실 수 있는 자료입니다.
- Control Number
- joongbu:657322