Advanced search options

Advanced Search Options 🞨

Browse by author name (“Author name starts with…”).

Find ETDs with:

in
/  
in
/  
in
/  
in

Written in Published in Earliest date Latest date

Sorted by

Results per page:

Sorted by: relevance · author · university · dateNew search

You searched for subject:(proteolytic degradation). Showing records 1 – 2 of 2 total matches.

Search Limiters

Last 2 Years | English Only

No search limiters apply to these results.

▼ Search Limiters


Cornell University

1. Rowland, Elden Ernest. PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS.

Degree: PhD, Plant Biology, 2017, Cornell University

Proteolysis is crucial for the maturation, regulation and recycling of the chloroplast proteome. Although several dozen chloroplast proteases are known, information concerning their substrates and functions is limited. In particular, little is known about the structural features of substrates that trigger their proteolysis. Most chloroplast proteins are nuclear encoded and are targeted through an N-terminal chloroplast transit peptide (cTP) that is removed by stromal processing peptidase (SPP). To better understand proteolytic maturation, the soluble N-terminal proteome of the Arabidopsis thaliana chloroplast was characterized. A cTP cleavage motif was observed that suggests other peptidases, in addition to SPP, are involved in chloroplast protein maturation. There was a clear preference for small uncharged amino acids at the processed protein N-terminus suggesting the existence of a chloroplast specific ‘N-end rule’. The soluble chloroplast peptidases PREP and OOP have been shown to degrade small polypeptides in vitro and are thought to be responsible for removal of cTP fragments and other degradation products. The CLP protease system can degrade intact protein substrates with the aid of ATP dependent (AAA+) CLPC chaperones that unfold and feed substrates into the CLP proteolytic core. An array of proteomic tools were used to compare Arabidopsis mutants deficient in the above peptidases with wild type. Degradation products, including cTPs, were found to accumulate in peptidase mutants indicative, of rate-limited or blocked degradation pathways. Incomplete or altered N-terminal maturation for chloroplast proteins was dependent on the type and severity of the peptidase deficiency. These results provide molecular details to help explain dwarf, chlorotic mutant phenotypes and demonstrate the interplay between protein import, proteolytic processing and the downstream degradation of damaged or unwanted proteins in the chloroplast. Substrate and sequence cleavage specificity was determined for soluble chloroplast glutamyl-endopeptidase (CGEP) and the plastoglobule localized metallopeptidase PGM48. Structural models were used to predict peptidase substrate binding mechanisms. Advisors/Committee Members: Van Wijk, Klaas (chair), Hanson, Maureen R. (committee member), Owens, Thomas G. (committee member), Cilia, Michelle (committee member).

Subjects/Keywords: Plant sciences; Biochemistry; Arabidopsis; chloroplast; N-terminal proteome; protease; proteolytic degradation; proteolytic maturation

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Rowland, E. E. (2017). PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS. (Doctoral Dissertation). Cornell University. Retrieved from http://hdl.handle.net/1813/58987

Chicago Manual of Style (16th Edition):

Rowland, Elden Ernest. “PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS.” 2017. Doctoral Dissertation, Cornell University. Accessed November 29, 2020. http://hdl.handle.net/1813/58987.

MLA Handbook (7th Edition):

Rowland, Elden Ernest. “PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS.” 2017. Web. 29 Nov 2020.

Vancouver:

Rowland EE. PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS. [Internet] [Doctoral dissertation]. Cornell University; 2017. [cited 2020 Nov 29]. Available from: http://hdl.handle.net/1813/58987.

Council of Science Editors:

Rowland EE. PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS. [Doctoral Dissertation]. Cornell University; 2017. Available from: http://hdl.handle.net/1813/58987


University of Ottawa

2. Chatterjee, Cynthia. Purinergic Signaling and Autophagy Regulate the Secretion of High-Density Lipoprotein and Hepatic Lipase .

Degree: 2013, University of Ottawa

Dyslipidemia can be a comorbidity of both insulin-resistance and atherosclerosis. Hypertriglyceridemia is common in hyperglycemia and is associated with hypoalphalipoproteinemia (low HDL) and with altered nucleotide or purinergic signaling. We therefore hypothesized that extracellular nucleotides may affect hepatic lipoprotein metabolism. Our studies confirm this view and show that nucleotides regulate cellular proteolytic pathways in liver cells and thereby control lipoprotein secretion and their metabolism by hepatic lipase (HL). Treatment of liver cells with the nucleotide, adenosine diphosphate (ADP), stimulates VLDL-apoB100 and apoE secretion, but blocks HDL-apoA-I and HL secretion. ADP functions like a proteasomal inhibitor to block proteasomal degradation and stimulate apoB100 secretion. Blocking the proteosome is known to activate autophagic pathways. The nucleotide consequently stimulates autophagic degradation in liver cells and increases cellular levels of the autophagic proteins, LC3 and p62. Confocal studies show that ADP increases cellular LC3 levels and promotes co-localization of LC3 and apoA-I in an autophagosomal degradation compartment. ADP acts through the G-protein coupled receptor, P2Y13, to stimulate autophagy and block both HDL and HL secretion. Overexpression of P2Y13 increases cellular LC3 levels and blocks the induction of both HDL and HL secretion, while P2Y13 siRNA reduce LC3 protein levels and cause up to a ten-fold stimulation in HDL and HL secretion. P2Y13 gene expression regulates autophagy through the insulin receptor (IR-β). A reduction in P2Y13 expression increases the phosphorylation of IR-β and protein kinase B (Akt) >3-fold, while increasing P2Y13 expression inhibits the activation of IR-β and Akt. Experiments with epitope-labeled apoA-I and HL show that activation of purinergic pathways has no effect on the internalization and degradation of extracellular apoA-I and HL, which confirms the view that nucleotides primarily impact intracellular protein transport and degradation. In conclusion, elevated blood glucose levels may promote dyslipidemia by stimulating purinergic signaling through P2Y13 and IR-β and perturbing the intracellular degradation and secretion of both HDL and VLDL.

Subjects/Keywords: High-Density Lipoprotein; Hepatic Lipase; Triglyceride; Coronary Heart Disease; Dyslipidemia; Inflammation; Autophagy; Proteolytic Degradation; Purinergic Signaling; Insulin Signaling; Metabolic Disease; Lipoprotein Metabolism; P2Y13; Adenosine Diphosphate

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Chatterjee, C. (2013). Purinergic Signaling and Autophagy Regulate the Secretion of High-Density Lipoprotein and Hepatic Lipase . (Thesis). University of Ottawa. Retrieved from http://hdl.handle.net/10393/24027

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Chatterjee, Cynthia. “Purinergic Signaling and Autophagy Regulate the Secretion of High-Density Lipoprotein and Hepatic Lipase .” 2013. Thesis, University of Ottawa. Accessed November 29, 2020. http://hdl.handle.net/10393/24027.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Chatterjee, Cynthia. “Purinergic Signaling and Autophagy Regulate the Secretion of High-Density Lipoprotein and Hepatic Lipase .” 2013. Web. 29 Nov 2020.

Vancouver:

Chatterjee C. Purinergic Signaling and Autophagy Regulate the Secretion of High-Density Lipoprotein and Hepatic Lipase . [Internet] [Thesis]. University of Ottawa; 2013. [cited 2020 Nov 29]. Available from: http://hdl.handle.net/10393/24027.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Chatterjee C. Purinergic Signaling and Autophagy Regulate the Secretion of High-Density Lipoprotein and Hepatic Lipase . [Thesis]. University of Ottawa; 2013. Available from: http://hdl.handle.net/10393/24027

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.