Cell Biology. Please Help. ^3 How can epithelial cells serve to modulate mechani
ID: 180552 • Letter: C
Question
Cell Biology. Please Help.
^3 How can epithelial cells serve to modulate mechanical stress through the usage of various adhesion junctions and cytoskeletal proteins; how is this dependent on signaling relays associated with the actin cytoskeleton?^4 For cell-cell adhesions, discuss why cells utilize adhesions (i.e. desmosome; cadherin) molecules linked to the cell cytoskeleton; in your answer, explain how the cell regulates intracellular activities and calcium responses based on events that happen in neighboring cells?Explanation / Answer
Ques-19:
Epithelial cells of animals are connected together by various cell junctions such as tight junctions, adhering junctions and gap junctions. Gap junctions allow the passage of ions and some specific molecules across one cell to another, thus they provide cell-to-cell communication. Connexins are a group of proteins that form gap junctions.
Epithelial cells serve to modulate mechanical stress through the usage of various adhesion junctions and cytoskeletal proteins. Integrins are the main cell surface glycoproteins mediate the “receptor activity” for extracellular matrix mediators such as collagen & laminin. These integrins are going to interact with adaptor proteins the intercellular adhesion molecule, I (ICAM-1)) to attach with “cytoskeltal microfilaments” and actin cytoskeltal filaments via signaling pathway at the time of mechanism stress on the epithelial cell. Finally, these vents are going to trigger movement in the cell to mediate extravasation of leukoctyes - mediated “cell proliferation or apoptosis” during stress via organization of actin cytoskeletal elements. The signaling is mainly bidirectional & trigger generation of collagen and proteoglycan to compensate the tissue loss due to mechanical stress. Cytoskeletal movement and proteins involved in the cell movement during stress as described below
The Arp2/3 complex and cofilin: These are the two components that meticulously function together to reorganize actin filaments by forming a complex result in nucleation of a novel F-actin branch followed by the cofilin mediated depolymerisation associated with disassembly. This depolymerisation takes place as soon as the Arp2/3 complex dissociated from actin filaments followed by reorganization of microtubules for continuation of filamental growth.
Katanin has more affinity towards microtubules via oligomerisation and ATPase activity associated with meticulous ATP hydrolysis thereby leading to mechanical stress on tubulin proteins produced by conformational alteration. This is going to disassemble and destabilize microtubule interactions followed by lower levels of affinity of katanin with tubulin protein. This phenomenon is result in disassembly of the katanin ring structure.
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