Abstract:
:Previous studies have shown that calpains are autolytically cleaved during the disease process of mdx dystrophy, a mouse model for Duchenne muscular dystrophy, indicating that calpains may be activated and play a role in proteolysis that occurs in muscular dystrophy (J. Biol. Chem. 270(18), 10909-10914, 1995). In the present study, we investigated the location of calpain in dystrophic muscle fibers over the course of mdx dystrophy, to relate the protease distribution to its state of activation, and to determine whether calpain translocation was an early event in mdx dystrophy. Immunolabeling of health, fully differentiated muscle fibers showed calpain present throughout the cytosol, but more concentrated near the plasma membrane. However, degenerating mdx fibers did not contain higher concentrations of calpain at the plasma membrane and showed only a homogeneous, cytosolic distribution. Calpain distribution was similarly diffuse in young myotubes and regenerating fibers with increased cytosolic concentration in early myotubes. Calpain distribution in adult mdx tissue was similar to that occurring in healthy, fully differentiated fibers, although adult mdx fibers displayed higher concentrations of membrane-associated calpain than those observed in C57 controls. The association of calpain with the plasma membrane was verified by immunoblots of isolated sarcolemmal membrane from adult mdx and control muscle which showed calpain present predominantly in the cytosol along with some membrane association. Thus, changes in calpain distribution coincide with changes in enzymatic cleavage over the course of mdx dystrophy shown previously. Furthermore, the stages of pathology at which calpain cleavage is least coincides with those stages when calpain is most concentrated at the cell membrane, suggesting that calpain is retained in an inactive form at the plasma membrane.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Spencer MJ,Tidball JGdoi
10.1006/excr.1996.0227subject
Has Abstractpub_date
1996-08-01 00:00:00pages
264-72issue
2eissn
0014-4827issn
1090-2422pii
S0014-4827(96)90227-Xjournal_volume
226pub_type
杂志文章abstract::In low serum (0.2%) medium, ascorbate stimulates primary avian tendon cells to increase procollagen synthesis from 12 to 50% of total protein synthesis. This is reversibly blocked by an increase of serum levels from 0.2 to 3%. Ascorbate in low serum medium has been shown previously to stimulate the procollagen pathway...
journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
pub_type: 杂志文章
doi:10.1016/0014-4827(91)90087-b
更新日期:1991-02-01 00:00:00
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journal_title:Experimental cell research
pub_type: 杂志文章
doi:10.1016/0014-4827(84)90174-5
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journal_title:Experimental cell research
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更新日期:1998-12-15 00:00:00
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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journal_title:Experimental cell research
pub_type: 杂志文章
doi:10.1006/excr.1997.3913
更新日期:1998-03-15 00:00:00
abstract::The large zinc finger protein KRC regulates transcription of target genes via the kappaB gene enhancer element. As an attempt to investigate the cellular function of KRC, we have established cell lines stably transfected with KRC expression vectors. Introduction of a vector directing expression of a transcript antisen...
journal_title:Experimental cell research
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更新日期:2000-11-01 00:00:00