The two lens structure proteins, αA-Crystallin (HspB4) and αB-Crystallin (HspB5), control apoptosis through regulation of multiple signaling transduction pathways

David W. Li, Lili Gong, Mi Deng, Jinping Liu, Mugen Liu, Ying Wei Mao

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)

Abstract

α-Crystallins are major lens structural proteins, belonging to the family of the small heat shock proteins (HSPs). α-Crystallins consist of two polypeptides, αA and αB that share 55% amino acid sequence identity. The two 20-kDa subunits form soluble aggregates with an average molecular mass of 600-800 kDa and can be isolated from lens fiber cells as a heteroaggregate containing αA- and αB-peptides in a ratio of 3 to 1. αAcrystallin (HspB4) is predominantly expressed in the ocular lens with small amounts present in spleen and thymus. In contrast, αB-crystallin (HspB5) is expressed mainly in the lens but also expressed outside of the lens in a number of tissues such as skeletal and cardiac muscle and to lesser extent in skin, brain, and kidney. Besides their structural role, α-crystallins are important chaperones in the ocular lens, act as autokinases, and also play important roles in suppressing both developmental and stress-induced apoptosis to guard the lens differentiation and prevent pathogenesis in the lens as well as several other tissues. In this chapter, we will focus on the current knowledge regarding the molecular mechanisms by which αA- and αB-crystallins suppress apoptosis in both lens and non-lens tissues.

Original languageEnglish (US)
Title of host publicationSmall Stress Proteins and Human Diseases
PublisherNova Science Publishers, Inc.
Pages89-116
Number of pages28
ISBN (Electronic)9781616685348
ISBN (Print)9781616681982
StatePublished - Jan 1 2010

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Crystallins
Staphylococcal Protein A
Lenses
Apoptosis
Crystalline Lens
Tissue
Small Heat-Shock Proteins
Thymus Gland
Thymus
Amino Acid Sequence
Myocardium
Skeletal Muscle
Spleen
Molecular mass
Kidney
Skin
Peptides
Muscle
Brain
Amino Acids

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Li, D. W., Gong, L., Deng, M., Liu, J., Liu, M., & Mao, Y. W. (2010). The two lens structure proteins, αA-Crystallin (HspB4) and αB-Crystallin (HspB5), control apoptosis through regulation of multiple signaling transduction pathways. In Small Stress Proteins and Human Diseases (pp. 89-116). Nova Science Publishers, Inc..

The two lens structure proteins, αA-Crystallin (HspB4) and αB-Crystallin (HspB5), control apoptosis through regulation of multiple signaling transduction pathways. / Li, David W.; Gong, Lili; Deng, Mi; Liu, Jinping; Liu, Mugen; Mao, Ying Wei.

Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc., 2010. p. 89-116.

Research output: Chapter in Book/Report/Conference proceedingChapter

Li, DW, Gong, L, Deng, M, Liu, J, Liu, M & Mao, YW 2010, The two lens structure proteins, αA-Crystallin (HspB4) and αB-Crystallin (HspB5), control apoptosis through regulation of multiple signaling transduction pathways. in Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc., pp. 89-116.
Li DW, Gong L, Deng M, Liu J, Liu M, Mao YW. The two lens structure proteins, αA-Crystallin (HspB4) and αB-Crystallin (HspB5), control apoptosis through regulation of multiple signaling transduction pathways. In Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc. 2010. p. 89-116
Li, David W. ; Gong, Lili ; Deng, Mi ; Liu, Jinping ; Liu, Mugen ; Mao, Ying Wei. / The two lens structure proteins, αA-Crystallin (HspB4) and αB-Crystallin (HspB5), control apoptosis through regulation of multiple signaling transduction pathways. Small Stress Proteins and Human Diseases. Nova Science Publishers, Inc., 2010. pp. 89-116
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