1 option
Ubiquitin dependent degradation of proteins modified by oxidation, deamidation and glycation : role in vision / Allen Taylor.
- Format:
- Video
- Author/Creator:
- Taylor, Allen, author.
- Language:
- English
- Subjects (All):
- Amyloidosis.
- Free radicals (Chemistry).
- Physical Description:
- 1 streaming video file (52 min.) : digital, mono, SWF file, sound, color
- Other Title:
- Ubiquitin dependent degradation of proteins modified by oxidation, deamidation and glycation
- Place of Publication:
- London : Henry Stewart Talks Ltd, 2017.
- System Details:
- video file
- Summary:
- Audio-visual presentation : Talk to be added shortly Description of cataract and AMD as the ultimate protein misfolding diseases ; Lens development: a model for aging research ; Photo-oxidative stress to the retina ; Etiology ; Environmental factors ; Pathophysiology ; Protein quality control ; Ubiquitin pathway selectivity for oxidatively modified, glutathiolated, deamindated and glycated substrates ; Clinical relevance.
- Contents:
- Introduction
- Talk outline
- Normal eye illustration
- Mouse lens cataract range
- Normal clear lens vs. cataract lens
- Lens brunescence and clarity vary independently
- Lens development: a model for aging research
- Protein precipitation disease
- Cataract prevalence increases with age
- The retina
- The structure of the human retina
- Photo-oxidative stress to the retina
- The life cycle of the RPE
- Progress of retinal degeneration
- Distorted central vision due to AMD
- View through AMD-damaged retina
- AMD prevalence increases exponentially by age
- AMD and cataract will increase within two decades
- Loss of sight - second greatest fear of the elderly
- Therapeutic opportunities
- Etiology, environmental factors, pathophysiology
- The eye deals with different kinds of stress
- Smoking and AMD
- Proteins are damaged upon oxidative stress
- Oxidative damage to lens proteins
- Formation of protein carbonyls
- Oxidation reactions and sequela reaction products
- Cataract, decreased P-SH and increased carbonyl
- Glycoprotein vs. age in human lens
- Lens protein distribution with age
- Modifications to proteins/proteases in older tissues
- Active proteases remove damaged proteins
- Ubiquitin pathway selectivity for substrates
- The ubiquitin-proteasome pathway (UPP)
- Ubiquitin chain linkage and function
- Oxidatively modified proteins in HLEC
- Could we isolate ubiquitin conjugates?
- K6W-Ub is conjugation competent
- Selectivity of ubiquitination for oxidized proteins
- Impairing the UPP by expression of K6W-Ub
- Protease inactivation and damaged proteins
- Lens clearity depends on a functional Ub pathway
- Glutathiolation and gammaC-crystallin degradation
- Glutathiolation enhances protein degradation rate
- Proteolysis of GSH-modified gamma-C-crystallin
- Degradation of glutathiolated gamma-C-crystallin
- Glutathiolation and CAIII degradation
- Minor CAIII structural alteration upon GSH
- E1 and E2 are thiol enzymes
- Thiolation of E1 following exposure to H2O2
- Control of the UPP by GSSG:GSH
- Oxidative inactivation of the proteasome
- Protein deamidation progresses with age
- Methylglyoxal reacts with Lys and Arg of proteins
- Glycation/MGO decreases degradation
- Clinical relevance
- Simple sugars might cause cataract and AMD
- High dietary glycemic index - risk for early ARM
- Antioxidants can delay aging
- What happens upon aging in the Ub pathway?
- Summary.
- Notes:
- Description based on publisher supplied metadata and other sources.
- Retrieved April 17, 2024, from https://hstalks.com/bs/393/.
The Penn Libraries is committed to describing library materials using current, accurate, and responsible language. If you discover outdated or inaccurate language, please fill out this feedback form to report it and suggest alternative language.