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Molecular Mechanism of αAN101D-Transgene-Induced Age-Related Cataract

Award Number: R01EY031303
ORGANIZATION: NATIONAL EYE INSTITUTE
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 04/01/2020
PERIOD OF PERFORMANCE END DATE: 03/31/2026

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Molecular Mechanism of αAN101D-Transgene-Induced Age-Related Cataract - The proposal has the overall goal to determine the molecular mechanisms of an age-related cortical cataract development. Cataracts are principally a lens structural proteins' (crystallins) aggregation and subsequent precipitation disease that are inducible by genetic mutations, and occurs due to aging. During cataract development, the increased sizes of aggregated and cross-linked crystallin multimers become so large that they finally become water insoluble and cause lens opacity. Several post-translational modifications (PTMs) of crystallins are known to cause age-related cataracts, and the deamidation of crystallins (the most abundant among post-translational modifications) is considered as a major cataract-causative factor. In spite of voluminous literature on in vitro studies of effects of crystallins' deamidation leading to cataract-development, no clear molecular mechanism has emerged that could implicate the deamidation-induced link of the in vitro effects to in vivo changes. Therefore, the PI's-generated unique αA-N101D mouse model, where asparagine 101 is deamidated to aspartic acid, provides an opportunity to directly link the in vitro studies to in vivo changes in phenotypic and crystallins' properties to the cortical cataract development. The model would provide information about the molecular mechanism of age-related cataract development. Based on our extensive results, we have hypothesized that the cataract in αAN101D mouse model is caused by the altered crystallin properties, cellular defects and synergistically increased deposit of αAN101D with membrane, resulting in membrane disruption and ionic imbalance. We plan to test the above hypothesis by seeking answers the following three questions using the above mouse model: (A) Aim 1: Does deamidated αAN101D causes temporal alterations in crystallin- crystallin interactions leading to aggregation among crystallins and their insolubilization in vivo? (B) Aim 2: What are the temporal sequence of lens phenotypes that cause cellular defects during the cortical cataract development? (C) Aim 3: Does temporal increase in binding of deamidated αAN101D to membrane leads to membrane disorganization and intracellular ionic imbalance? The results will be of significant therapeutic value to delay the development and progression of age-related cataracts.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2025 ( Subtotal = $0 )
2025	2023	UNIVERSITY OF ALABAMA AT BIRMINGHAM	701 S 20TH STREET	BIRMINGHAM	AL	35294	JEFFERSON	USA	Vision Research	000	4	3/3/2025	NON-COMPETING CONTINUATION	$0
														Subtotal = $0

Issue Date FY: 2023 ( Subtotal = $394,771 )
2023	2023	UNIVERSITY OF ALABAMA AT BIRMINGHAM	701 S 20TH ST	BIRMINGHAM	AL	35294	JEFFERSON	USA	Vision Research	000	4	3/30/2023	NON-COMPETING CONTINUATION	$394,771
														Subtotal = $394,771

Issue Date FY: 2022 ( Subtotal = $382,927 )
2022	2022	UNIVERSITY OF ALABAMA AT BIRMINGHAM	701 S 20TH ST	BIRMINGHAM	AL	35294	JEFFERSON	USA	Vision Research	000	3	3/28/2022	NON-COMPETING CONTINUATION	$382,927
														Subtotal = $382,927

Issue Date FY: 2021 ( Subtotal = $382,927 )
2021	2021	UNIVERSITY OF ALABAMA AT BIRMINGHAM	701 S 20TH ST	BIRMINGHAM	AL	35294	JEFFERSON	USA	Vision Research	000	2	3/22/2021	NON-COMPETING CONTINUATION	$382,927
														Subtotal = $382,927

Issue Date FY: 2020 ( Subtotal = $394,587 )
2020	2020	UNIVERSITY OF ALABAMA AT BIRMINGHAM	701 S 20TH ST	BIRMINGHAM	AL	35294	JEFFERSON	USA	Vision Research	000	1	3/26/2020	NEW	$394,587
														Subtotal = $394,587

Grand Total All Awards = $1,555,212

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Molecular Mechanism of αAN101D-Transgene-Induced Age-Related Cataract

Award Number: R01EY031303

ORGANIZATION: NATIONAL EYE INSTITUTE

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 04/01/2020

PERIOD OF PERFORMANCE END DATE: 03/31/2026

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