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Dissertation
The role of transglutaminase enzymes in cerebrovascular amyloid deposition
Doctor of Philosophy (Ph.D.), Allegheny University of the Health Sciences
Nov 1998
DOI:
https://doi.org/10.17918/00009106
Abstract
We investigated whether the [beta]-amyloid peptide, 1-40 sequence, (A[beta]₄₀) found in the Alzheimer brain could be covalently cross-linked by Factor XIIIa, plasma transglutaminase (E. C. 2.3.2.13, glutaminyl-peptide-gamma-glutamytransferase) to the common extracellular matrix proteins surrounding numerous blood vessels in the human brain. This mechanism of [beta]-amyloid accumulation, in addition to the aggregation of [beta]-pleated sheets, may help to explain the process by which cerebrovascular amyloid is deposited. Factor XIIIa and combinations of A[beta]₄₀ and ECM proteins were incubated in vitro and analyzed by SDS-PAGE, Western blotting and electron microscopy. These experiments revealed that, in the presence of Factor XIIIa, A[beta]₄₀ formed polymeric structures with itself as well as in association with collagen type IV, fibronectin and laminin. Western blotting revealed high molecular weight complexes of A[beta]₄₀ and ECM proteins following transfer to PVDF membranes from denaturing polyacrylamide gels.
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Details
- Title
- The role of transglutaminase enzymes in cerebrovascular amyloid deposition
- Creators
- Timothy C. Baradet
- Contributors
- Brian J. Balin (Advisor) - Drexel University, Allegheny University of the Health Sciences (1996-1998)
- Awarding Institution
- Allegheny University of the Health Sciences
- Degree Awarded
- Doctor of Philosophy (Ph.D.)
- Publisher
- Allegheny University of the Health Sciences; Philadelphia, Pennsylvania
- Number of pages
- ix, 97 pages
- Resource Type
- Dissertation
- Language
- English
- Academic Unit
- Allegheny University of the Health Sciences (1996-1998); School of Medicine (1996-1998); Pathology (and Laboratory Medicine) [Historical]
- Other Identifier
- 991021889014604721