Literature DB >> 12790344

Crystallins, genes and cataract.

Suraj P Bhat1.   

Abstract

Far from being a physical entity, assembled of inanimate structural proteins, the ocular lens epitomizes the biological ingenuity that sustains an essential and near-perfect physical system of immaculate optics. Crystallins (alpha, beta, and gamma) provide transparency by dint of their high concentration, but it is debatable whether proteins that provide transparency are any different, biologically or structurally, from those that are present in non-transparent structures or tissues. It is becoming increasingly clear that crystallins may have a plethora of metabolic and regulatory functions, both within the lens as well as outside of it. Alpha-crystallins are members of a small heat shock family of proteins and beta/gamma-crystallins belong to the family of epidermis-specific differentiation proteins. Crystallin gene expression has been studied from the perspective of the lens specificity of their promoters. Mutations in alpha-, beta-, and gamma-crystallins are linked with the phenotype of the loss of transparency. Understanding catalytic, non-structural properties of crystallins may be critical for understanding the malfunction in molecular cascades that lead to cataractogenesis and its eventual therapeutic amelioration.

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Year:  2003        PMID: 12790344     DOI: 10.1007/978-3-0348-8012-1_7

Source DB:  PubMed          Journal:  Prog Drug Res        ISSN: 0071-786X


  34 in total

1.  Secretion of αB-Crystallin via exosomes: New clues to the function of human retinal pigment epithelium.

Authors:  Suraj P Bhat; Rajendra K Gangalum
Journal:  Commun Integr Biol       Date:  2011-11-01

2.  AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells.

Authors:  Rajendra K Gangalum; Ivo C Atanasov; Z Hong Zhou; Suraj P Bhat
Journal:  J Biol Chem       Date:  2010-11-19       Impact factor: 5.157

3.  AlphaB-crystallin: a Golgi-associated membrane protein in the developing ocular lens.

Authors:  Rajendra K Gangalum; Suraj P Bhat
Journal:  Invest Ophthalmol Vis Sci       Date:  2009-02-14       Impact factor: 4.799

Review 4.  Ca2+-binding motif of βγ-crystallins.

Authors:  Shanti Swaroop Srivastava; Amita Mishra; Bal Krishnan; Yogendra Sharma
Journal:  J Biol Chem       Date:  2014-02-24       Impact factor: 5.157

Review 5.  Small heat-shock proteins: important players in regulating cellular proteostasis.

Authors:  Teresa M Treweek; Sarah Meehan; Heath Ecroyd; John A Carver
Journal:  Cell Mol Life Sci       Date:  2014-10-29       Impact factor: 9.261

6.  αA-crystallin and αB-crystallin reside in separate subcellular compartments in the developing ocular lens.

Authors:  Rajendra K Gangalum; Joseph Horwitz; Sirus A Kohan; Suraj P Bhat
Journal:  J Biol Chem       Date:  2012-10-15       Impact factor: 5.157

7.  Characterization of O-phosphohydroxyproline in rat {alpha}-crystallin A.

Authors:  Axel Kühlberg; Mark Haid; Sabine Metzger
Journal:  J Biol Chem       Date:  2010-08-03       Impact factor: 5.157

8.  Alphab-crystallin-assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding.

Authors:  M Satish Kumar; P Yadagiri Reddy; B Sreedhar; G Bhanuprakash Reddy
Journal:  Biochem J       Date:  2005-10-15       Impact factor: 3.857

9.  HSF4 is required for normal cell growth and differentiation during mouse lens development.

Authors:  Mitsuaki Fujimoto; Hanae Izu; Keisuke Seki; Ken Fukuda; Teruo Nishida; Shu-Ichi Yamada; Kanefusa Kato; Shigenobu Yonemura; Sachiye Inouye; Akira Nakai
Journal:  EMBO J       Date:  2004-10-14       Impact factor: 11.598

10.  Inhibition of the Expression of the Small Heat Shock Protein αB-Crystallin Inhibits Exosome Secretion in Human Retinal Pigment Epithelial Cells in Culture.

Authors:  Rajendra K Gangalum; Ankur M Bhat; Sirus A Kohan; Suraj P Bhat
Journal:  J Biol Chem       Date:  2016-04-27       Impact factor: 5.157

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