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Studies on the assembly and topography of proteins in the muscle myofibrilTurner, Robert Craig. January 1980 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1980. / Typescript. Vita. Description based on print version record. Includes bibliographical references.
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Quantitative relationships of the myofibrillar proteins myosin, actin and the troponin subunitsYates, Lawrence Davis. January 1982 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1982. / Typescript. Vita. Includes bibliographical references (leaves 61-67).
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Immunofluorescence studies of normal and hyperthyroxic chicken skeletal muscle using anti-myosinsCarpenter, Charles Edward. January 1984 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1984. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 94-101).
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Analysis of Bves function through identification of interacting proteinsSmith, Travis Kirk. January 2007 (has links)
Thesis (Ph. D. in Cell and Developmental Biology)--Vanderbilt University, May 2007. / Title from title screen. Includes bibliographical references.
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Molecular dissection of myosin light chain functionRowe, Tony January 1993 (has links)
No description available.
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Protein isoform-function relationships of single skeletal muscle fibers from weight-bearing and hindlimb suspended miceStelzer, Julian E. (Julian Emanuel) 20 May 2002 (has links)
The goals of this research were to a) characterize the protein-function
relationships of skeletal muscle single fibers from the mouse hindlimb b) examine
mouse-strain related differences in myosin heavy chain composition (MHC) and
single fiber contractile function, and c) quantify changes in fiber size and
contractile function in response to 7 days of non-weight bearing. This research is
significant because mechanistic approaches to understanding relationships between
muscle protein expression, contractile function, and mechanical loading will likely
benefit from a transition from the traditional laboratory rat to genetically modified
mouse models.
The methods used in this research feature an in vitro skinned-fiber
preparation and single-fiber gel electrophoresis. Hindlimb muscles of mice were
excised, and dissected into smaller bundles from which single muscle fibers were
isolated. Single fibers were placed in skinning solution that permeabilized the
fiber's membrane. The ends of skinned single muscle segments were attached to
stainless steel troughs, which were connected to an isometric force transducer and a
direct-current position motor. This system allowed the measurement of the fiber's
cross-sectional area (CSA), peak isometric force (P���), and unloaded maximal
shortening velocity (V���) during maximal Ca�����-activating. The identification of the
fiber's MHC content was subsequently achieved by electrophoresis of a sample of
each fiber segment.
The results showed that the C57BL/6 mouse soleus muscle contains a
MHC composition (20% type I) that is dramatically different than the ICR and
CBA/J mouse strains (50% type I, respectively). Type I fibers from the C57BL/6
mouse had V��� that was 25% lower than type I fibers from ICR and CBA/J mice.
Following 7 days of hindlimb suspension (HS) all strains experienced significant
soleus muscle and single-fiber atrophy and decreases in the absolute and specific
(force/fiber CSA) of type I and II fibers. However, type I fibers from C57BL/6
mice showed no change in V��� whereas type I fibers from ICR and CBA/J showed
increased V���.
In conclusion, this research demonstrates that unlike the rat and human
models of non-weight bearing, mouse soleus type I and II fibers are equally
affected by HS with respect to decreases in fiber CSA and force. However, type I
fiber V��� was elevated only in mouse strains with solei containing at least 50% type
I MHC. These findings challenge the current view that non-weight bearing affects
slow fibers more than fast fibers, and suggests that changes in single fiber
contractile function with HS may be influenced in part by the MHC distribution of
the muscle. / Graduation date: 2003
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Control of muscle protein degradation and steady-state poly(ADP-ribose) polymerase concentration by calpainHuang, Jing, 1961- 13 April 1998 (has links)
The first goal of this study was to understand the role of calpains in skeletal muscle
protein degradation in cultured cells. We have developed a genetic approach to inhibit
endogenous calpain activity through over-expressing dominant negative m-calpain (DN),
antisense m-calpain (AS) and calpastatin inhibitory domain (CID). We observed that,
under conditions of accelerated degradation (serum withdrawal), inhibition of m-calpain
through DN-m-calpain over-expression caused a 30% inhibition of total protein
degradation whereas CID over-expression reduced degradation by 63%. These
constructs did not significantly affect degradation in the presence of serum. These data
indicate that calpains participate in the accelerated degradation associated with serum
withdrawal. Inhibition of calpain also stabilized nebulin, a major structural protein of the
sarcomere. These observations indicate that calpains play significant roles in muscle
protein turnover. Finally, over-expression of antisense m-calpain caused a transient
reduction in m-calpain concentration after which normal m-calpain concentration was
quickly re-established. These observations indicate that m-calpain is a short half-life
protein in muscle cells.
The second goal of this study is to investigate the role of calpain in the mediation
of PARP protein level in differentiating myoblasts. Poly(ADP-ribosyl)ation, catalyzed by
PARP, is involved in various physiological events, such as DNA excision repair, DNA
recombination, DNA replication, cell differentiation, cell growth and transformation, and
apoptosis. A protease participating in PARP turnover could be a significant regulator to the events which PARP is involved. A relationship between apoptosis and myofibrillar
protein degradation via a common protease might suggest the basis for muscle wasting
and atrophy which characterize in many muscle diseases. We established a genetic
approach to inhibit endogenous calpain activity through over-expressing calpastatin
inhibitory domain (CID). We observed that (1) inhibition of calpain activity increased
PARP concentration when post-confluent myoblasts were cultured with 2% HS medium,
an inducer of differentiation and (2) inhibition of calpain activity prevented PARP
degradation induced by A23187 and etoposide in differentiating myoblasts. These data
demonstrate that calpain is involved in regulation of PARP in cultured cells. / Graduation date: 1998
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Fluorescence labeling and computational analysis of the strut of myosin's 50 kDa cleftGawalapu, Ravi Kumar. Root, Douglas, January 2007 (has links)
Thesis (Ph. D.)--University of North Texas, Aug., 2007. / Title from title page display. Includes bibliographical references.
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A comparative proteomics approach to studying skeletal muscle mitochondria from myostatin knockout micePuddick, Jonathan. January 2006 (has links)
Thesis (M.Sc. Biological Sciences)--University of Waikato, 2006. / Title from PDF cover (viewed March 18, 2008) Includes bibliographical references (p. 98-112)
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Molecular characterization of the amino-terminal region of the large Drosophia muscle protein projectin /Daley, John Kevin, January 1998 (has links)
Thesis (Ph. D.)--Lehigh University, 1998. / Includes vita. Bibliography: leaves 111-118.
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