Calponin is an actin-binding protein found in a variety of cells that is well known for its inhibition of actin-activated myosin ATPase. We hypothesize that calponin inhibits cellular secretion by two mechanisms. One mechanism is to prevent the cleavage of actin in the cytoskeleton, a gel-like mesh that acts as a physical barrier to vesicles travelling to the membrane, by gelsolin and other actin-severing proteins that cut paths for vesicles to travel. The other mechanism is to assist in the bundling and cross-linking of actin, creating smaller pores in the mesh that are more difficult for the vesicles to move through. This project conducted necessary background research, designed study and future experiments, and amplified pET and pCMV-HA vectors that will be used in the experiments.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Rollins, Christopher Thomas

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-043009-043917

Advisor

• Rulfs, Jill

Year

• 2009

Sponsor

• Sutherland Maciver

Date created

• 2009-04-30

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright