NDLI: Cell kinetic status of mouse lens epithelial cells lacking αA- and αB-crystallin

Content Provider	Springer Nature Link
Author	Bai, Fang Xi, Jinghua Higashikubo, Ryuji Andley, Usha P.
Copyright Year	2004
Abstract	αA- and αB-crystallins are small heat shock proteins and molecular chaperones that are known to prevent non-specific aggregation of denaturing proteins. Recent work indicates that αA-/- lens epithelial cells grow at a slower rate than wild-type cells, and cultured αB-/- cells demonstrate increased hyperproliferation and genomic instability, suggesting that these proteins may exert a direct effect on the cell cycle kinetics, and influence cell proliferation. However, the cell cycle parameters of αA/αBKO (double knockout) cells have not been analyzed. Here we investigate the cell cycle kinetics of synchronized mouse lens epithelial cultures derived from wild-type and αA/αB double knockout (αA/αBKO) mice using BrdU labeling of proliferating cells, and flow cytometric analysis. We also provide data on the changing pattern of expression of HSP25, a small heat shock protein in αA/αBKO and wild-type cells during the cell cycle. Using serum starvation to synchronize cells in the quiescent G0 phase, and restimulation with serum followed by BrdU labeling and flow cytometry, the data indicated that as compared to wild-type cells, a <50% smaller fraction of the αA/αBKO cells entered the DNA synthetic S phase of the cell cycle. Furthermore, there was a delay in cell cycle transit through S phase in αA/αBKO cells, suggesting that although capable of entering S phase, the αA/αBKO cells are blocked in G1 phase, and are delayed in their cell cycle progression. Immunoblot analysis with antibodies to the small heat shock protein HSP25 indicated that although HSP25 increased in G1 phase of wild-type cells, and remained elevated on further progression through the cell cycle, HSP25 accumulation was delayed to S phase in αA/αBKO cells. These data can be interpreted to indicate that mouse lens epithelial cell progression through the cell cycle is significantly affected by expression of αA and αB-crystallin. (Mol Cell Biochem 265: 115–122, 2004)
Starting Page	115
Ending Page	122
Page Count	8
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	265
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2004-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cardiology Medical Biochemistry Oncology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin

Role of the specifically targeted lysine residues in the glycation dependent loss of chaperone activity of αA- and αB-crystallins

Quaternary structural parameters of the congenital cataract causing mutants of αA-crystallin

Reversal of chaperone activity loss of glycated αA-crystallin by a crosslink breaker

Examination of the molecular basis for the lack of αB-crystallin expression in L929 cells

αA-Crystallin and αB-Crystallin Reside in Separate Subcellular Compartments in the Developing Ocular Lens

Pyruvate modulates antioxidant status of cultured human lens epithelial cells under hypergalactosemic conditions

Intrapolypeptide disulfides in human αA-crystallin and their effect on chaperone-like function

Cataract mutation P20S of αB-crystallin impairs chaperone activity of αA-crystallin and induces apoptosis of human lens epithelial cells

Cell kinetic status of mouse lens epithelial cells lacking αA- and αB-crystallin

Similar Documents

C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin

Role of the specifically targeted lysine residues in the glycation dependent loss of chaperone activity of αA- and αB-crystallins

Quaternary structural parameters of the congenital cataract causing mutants of αA-crystallin

Reversal of chaperone activity loss of glycated αA-crystallin by a crosslink breaker

Examination of the molecular basis for the lack of αB-crystallin expression in L929 cells

αA-Crystallin and αB-Crystallin Reside in Separate Subcellular Compartments in the Developing Ocular Lens

Pyruvate modulates antioxidant status of cultured human lens epithelial cells under hypergalactosemic conditions

Intrapolypeptide disulfides in human αA-crystallin and their effect on chaperone-like function

Cataract mutation P20S of αB-crystallin impairs chaperone activity of αA-crystallin and induces apoptosis of human lens epithelial cells

Cell kinetic status of mouse lens epithelial cells lacking αA- and αB-crystallin