Tissue distribution and developmental profiles of immunoreactive αB crystallin in the rat determined with a sensitive immunoassay system

Kato, Kanefusa; Shinohara, Haruo; Kurobe, Naomi; Inaguma, Yutaka; Shimizu, Kikuo; Ohshima, Kunihiro

doi:10.1016/0304-4165(91)90062-l

Cited by 186 publications

(122 citation statements)

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“…For the small heat shock proteins (sHSPs), which are ubiquitous and range in size from [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30], cellular thermoresistance provided by their overexpression has been reported [6][7][8]. A striking sequence similarity exists between the C-terminal parts of proteins belonging to this group of HSPs and the uA-and aB-crystallins [5,9].…”

Section: Introductionmentioning

confidence: 99%

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αA‐crystallin confers cellular thermoresistance

et al. 1994

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The bovine eye lens protein aA-crystallin has been overexpressed both by stable transfection of HeLa cells and by transient transfection of NIH 3T3 cells. In both experimental systems aA-crystallin overexpression results in an increased cellular thermoresistance as judged by different clonal survival assays. In contrast, similar overexpression of another stable lens protein,BB2-crystallin, does not confer thermoresistance. These results indicate that the structural relationship of aA-crystallin to the small heat shock proteins HSP25127 and to aB-crystallin is sufficient for the shared thermoprotective function of all of these molecules and strongly suggests that the chaperone-like properties that they have in common are responsible for the conferred cellular thermoresistance.

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Section: Introductionmentioning

confidence: 99%

“…Expression of cxB-crystallin was found in many tissues, reaching levels of up to 2% in soleus muscle [15], and is increased in neuro-degenerative diseases [16,17], in brain tumors [18] or during oncogene expression [19]. In addition, expression of aB-crystallin can be induced by heat, osmotic and arsenite stress [20,21].…”

Section: Introductionmentioning

confidence: 99%

αA‐crystallin confers cellular thermoresistance

et al. 1994

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“…Initially considered to be lens-specific, ␣B-crystallin (␣B) 2 was the first ubiquitous crystallin that was reported to be expressed outside of the lens (5); it was later joined by ␣A-crystallin (␣A) (6,7). ␣A and ␣B are two prominent members of the small heat shock family of proteins.…”

mentioning

confidence: 99%

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

Gangalum

Horwitz

Kohan

et al. 2012

Journal of Biological Chemistry

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Background:The small heat shock proteins, ␣A-crystallin and ␣B-crystallin are considered to be two subunits of one single monolithic lens protein, ␣-crystallin. Results: ␣A-Crystallin and ␣B-crystallin fractionate independent of each other and in two separate membrane compartments. Conclusion: ␣A-Crystallin and ␣B-crystallin are two independent proteins in the lens. Significance: These data provide functional insight into why ␣A-crystallin and ␣B-crystallin null mice have disparate phenotypes.

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“…In addition to being a lens protein, aB-crystallin is also expressed in many different tissues. Relatively high levels are found in heart, striated muscle, kidney and brain tissue [4,56,57].…”

Section: The Chaperone-like Function Of A-crystallinsmentioning

confidence: 99%

α-Crystallins, versatile stress-proteins

Boelens

Jong

1995

Mol Biol Rep

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Introductionpost-translational modifications [12] of a-crystallins we refer to other recent reviews. a-Crystallins owe their name to the fact that they are major eye lens proteins in vertebrates. They are abun dantly present in the lens and have a prominent role in maintaining the transparency and retractile properties of the lens (reviewed in [1][2][3]). There are two types of related subunits, aA and aB, each of about 20 kDa, of which aB is also expressed at significant levels in many different tissues outside the lens [4], a-Crystallins exist as large homo-or hetcromeric complexes, contain ing about 30-40 subunits. Their tertiary and quater nary structures are unknown. Initially it was observed that» on ihe basis of sequence homology, a-crystallins belong to the family of small heat shock proteins (hsps) [5], This family is characterized by the presence of an approximately 100 amino acid long conserved domain, often called the a-crystallin domain. a-Crystallins and small hsps arc not only evolutionarily related but they also behave very similarly in many respects. They actu ally can form mixed complexes in tissues were both proteins are expressed [6 , 7], a-Crystallins, like oth er small hsps, have chaperone-like properties in that they can prevent stress-induced aggregation of pro teins [8], Furthermore, mammalian aB-crystallin is stress-inducible, and the presence of a-crystallins in cultured cells leads to an enhanced survival of these cells after a period of stress [9]. aB-Crystallin is also implicated in the pathogenesis of various degenerative diseases.In this mini review we will mainly discuss the struc tural and functional aspects of a-crystallins. For gene regulation [10], evolutionary relationships [11] and

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Tissue distribution and developmental profiles of immunoreactive αB crystallin in the rat determined with a sensitive immunoassay system

Cited by 186 publications

References 28 publications

αA‐crystallin confers cellular thermoresistance

αA‐crystallin confers cellular thermoresistance

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

α-Crystallins, versatile stress-proteins

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