Early changes of αB-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation

Atomi, Yoriko; Yamada, Shigeru; Nishida, Tsutomu

doi:10.1016/0006-291x(91)92083-v

Cited by 55 publications

(52 citation statements)

References 19 publications

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“…Moreover, it was shown that the amount of aLB-crystallin mRNA in muscles was regulated by mechanical tension and denervation (4). These results suggest that aB-crystallin is a myofibril-stabilizing protein which may regulate myofibril structures depending on nerve innervation and mechanical stimuli in muscles (4,5). During development, aB-crystallin seems to be associated with major morphological changes of tissues.…”

Section: Discussionmentioning

confidence: 77%

“…The model that aB-crystallin is a molecular chaperone-like protein seems to fit our results best. It is known that aB-crystallin multimerizes to form a large complex (33,67) which can associate with architectural proteins such as myofibrils, actin, and desmin filaments (4)(5)(6)41). Large protein complex formation is a characteristic of some of the molecular chaperons such as the prokaryotic chaperonin GroEL, eukaryotic cytoplasmic chaperonin, and mitochondrial chaperonin hsp6O (14).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection.

Aoyama¹,

Fröhli²,

Schäfer³

et al. 1993

Mol. Cell. Biol.

115

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ocB-crystallin, a major soluble protein of vertebrate eye lenses, is a small heat shock protein which transiently accumulates in response to heat shock and other kinds of stress in mouse NIH 3T3 fibroblasts. Ectopic expression of an aeB-crystallin cDNA clone renders NIH 3T3 cells thermoresistant. avB-crystallin accumulates in response to the synthetic glucocorticoid hormone dexamethasone. Dexamethasone-treated NIH 3T3 cells become thermoresistant to the same extent as they accumulate cvB-crystallin. A cell clone in which ciB-crystallin is superinduced upon heat shock acquires augmented thermotolerance. Expression of the ras oncogene causes a rapid but transient accumulation of cfB-crystallin within 1 day. Later, sustained ras oncogene expression suppresses the dexamethasone-mediated aB-crystallin accumulation. Thus, oncogenic transformation triggered by the ras oncogene interferes with hormone-mediated accumulation of oaB-crystallin and concomitant acquisition of thermoresistance. Other known heat shock proteins do not accumulate in response to ectopic csB-crystallin expression or to dexamethasone treatment. These results indicate that aB-crystallin can protect NIH 3T3 fibroblasts from thermal shock.Studies on oncogene-induced alterations in cellular gene expression and their association with the transformation phenotype are essential for understanding the mechanisms by which oncogenes mediate the malignant phenotype (for a review, see reference 3). In an attempt to define specific cellular responses toward accumulation of oncoproteins, we have previously studied the effects of the ras and mos oncoproteins on cellular gene expression in mouse NIH 3T3 fibroblasts (34). We found that high amounts of aB-crystallin rapidly accumulate in NIH 3T3 cells in response to the expression of the c-Ha-ras and v-mos oncogenes controlled by the glucocorticoid-inducible promoter of mouse mammary tumor virus (MMTV) (32).aB-crystallin is one of the major soluble proteins of vertebrate eye lenses (for reviews, see references 51, 52, and 67). The protein shares 60% amino acid sequence homology with oA-crystallin (62). atB-crystallin is also expressed in nonocular tissues such as heart muscle, skeletal muscle, kidney, lung, brain, spermatocyte, and placenta (5, 8, 12, 23-25, 31, 40). Moreover, evidence has been accumulating that elevated levels of aB-crystallin are associated with various pathological conditions in the brain and other tissues (13,24,26,27,43,44,48). The ot-crystallins share amino acid sequence similarity with small heat shock proteins (hsps) of diverse organisms, including mycobacteria, fruit flies, plants, and mammals (for reviews, see references 39, 51, 52, 65, 66, and 67). The homology between mouse aB-crystallin (32) and hsp25 (unpublished data; 17) reaches approximately 40%. These observations suggest a possible functional relationship between a-crystallins and small hsps (11). Recently we have shown that oxB-crystallin is indeed a bona fide small hsp (33). The characteristic features shared by aB-crystallin a...

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Section: Discussionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 99%

Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection.

Aoyama¹,

Fröhli²,

Schäfer³

et al. 1993

Mol. Cell. Biol.

115

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“…Thus, myosin heavy chain, muscle creatine kinase, ␣B-crystallin, as well as glyceraldehyde-3-phosphate dehydrogenase have been reported to be four earlier markers of muscle disuse (52,53), while induction of carbonic anhydrase III (54) as well as effect on muscle specific enolase (55) have been demonstrated in muscle after denervation. This could indicate that the OGlcNAc modifications are involved in the muscle plasticity and rapid adaptation to new physiological conditions.…”

Section: Discussionmentioning

confidence: 99%

Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry

Cieniewski-Bernard

Bastide²,

Lefebvre

et al. 2004

Molecular & Cellular Proteomics

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O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation. O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide ␤-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose. Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach. Fourteen proteins were identified as being O-GlcNAc modified. These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain). A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction. These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.

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“…To prepare the expression vector encoding the ␣B-crystallin deletion mutant lacking the N-terminal domain, ␣B-⌬N67-expressing clones were amplified by polymerase chain reaction (PCR) with pUC118-␣B-crystallin (GenBank accession P23928) (Atomi et al 1991) as a template and custom primers (EcoRI and XbaI restriction sites underlined) synthesized by Espec oligo (Tsukuba, Japan). Primers used were for the ␣B-⌬N67 mutant: top, 5Ј-GCGAAT TCATGCGTATGGAGAAGGACAG-3Ј; bottom, 5Ј-TACT CGAGCTACTTCTTAGGGGCTGCAG-3Ј.…”

Section: Cloning Of the Deletion Mutant Lacking The N-terminal Domainmentioning

confidence: 99%

Analysis of the αB-crystallin domain responsible for inhibiting tubulin aggregation

2007

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The cytoskeleton has a unique property such that changes of conformation result in polymerization into a filamentous form. ␣B-Crystallin, a small heat shock protein (sHsp), has chaperone activities for various substrates, including proteins constituting the cytoskeleton, such as actin; intermediate filament; and tubulin. However, it is not clear whether the ''␣-crystallin domain'' common to sHsps also has chaperone activity for the protein cytoskeleton. To investigate the possibility that the C-terminal ␣-crystallin domain of ␣B-crystallin has the aggregation-preventing ability for tubulin, we constructed an N-terminal domain deletion mutant of ␣B-crystallin. We characterized its structural properties and chaperone activities. Far-ultraviolet (UV) circular dichroism measurements showed that secondary structure in the ␣-crystallin domain of the deletion mutant is maintained. Ultracentrifuge analysis of molecular masses indicated that the deletion mutant formed smaller oligomers than did the full-length protein. Chaperone activity assays demonstrated that the N-terminal domain deletion mutant suppressed heat-induced aggregation of tubulin well. Comparison of chaperone activities for 2 other substrates (citrate synthase and alcohol dehydrogenase) showed that it was less effective in the suppression of their aggregation. These results show that ␣B-crystallin recognizes a variety of substrates and especially that ␣-crystallin domain binds free cytoskeletal proteins. We suggest that this feature would be advantageous in its functional role of holding or folding multiple proteins denatured simultaneously under stress conditions.

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Early changes of αB-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation

Cited by 55 publications

References 19 publications

Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection.

Alpha B-crystallin expression in mouse NIH 3T3 fibroblasts: glucocorticoid responsiveness and involvement in thermal protection.

Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry

Analysis of the αB-crystallin domain responsible for inhibiting tubulin aggregation

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