Role of Parvalbumin in Relaxation of Frog Skeletal Muscle

Hou, Tien-Tzu; Johnson, Jillian; Rall, Jack A.

doi:10.1007/978-1-4615-2872-2_13

Cited by 22 publications

(21 citation statements)

References 23 publications

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“…The high concentrations of adenylate kinase (1.6 g liter Ϫ1 ) and phosphocreatine kinase (6.6 g liter Ϫ1 ), also listed in Table III, are not surprising because these enzymes play an important role in buffering MgATP and fueling contraction in fast twitch skeletal muscles (29 -31). The presence of the soluble calcium-binding protein parvalbumin (Table III) is consistent with the well established role of parvalbumin in facilitating relaxation in fast twitch muscles (32). However, its concentration (0.7 g liter Ϫ1 ) is only a tenth of that found in frog semitendinosus muscle (7.4 Ϯ 0.8 g liter Ϫ1 (19)), suggesting that its role in relaxing fast twitch skeletal muscles may be less important in rabbits than it is in frogs (32).…”

Section: Resultssupporting

confidence: 86%

“…The presence of the soluble calcium-binding protein parvalbumin (Table III) is consistent with the well established role of parvalbumin in facilitating relaxation in fast twitch muscles (32). However, its concentration (0.7 g liter Ϫ1 ) is only a tenth of that found in frog semitendinosus muscle (7.4 Ϯ 0.8 g liter Ϫ1 (19)), suggesting that its role in relaxing fast twitch skeletal muscles may be less important in rabbits than it is in frogs (32).…”

Section: Resultssupporting

confidence: 86%

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Concentrations of Glycolytic Enzymes and Other Cytosolic Proteins in the Diffusible Fraction of a Vertebrate Muscle Proteome

Maughan

Henkin

Vigoreaux

2005

Molecular & Cellular Proteomics

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We used a novel microvolumetric technique based on protein diffusion to characterize the subproteome of muscle that consists of diffusible proteins, including those involved in cell metabolism. Muscle fiber segments were mechanically demembranated under mineral oil and transferred into drops of relaxing solution. After the fiber segment was depleted of diffusible proteins, the content of each drop and residual segment was analyzed by onedimensional polyacrylamide gel electrophoresis. Proteins were identified through peptide mass fingerprinting and quantified using purified protein standards. Ten of the most abundant cytosolic proteins, distinguished by their ability to readily diffuse out of the skinned fiber, were glycolytic enzymes whose concentrations ranged from 2.6 ؎ 1.0 g liter ؊1 (phosphoglucose isomerase) to 12.8 ؎ The advent of proteomics, the experimental approach to assess global protein function, has introduced new techniques for studying important subproteomes of cellular proteins that operate in a coordinated fashion. One such subproteome is the entire complement of metabolic enzymes found in a selected muscle cell at any given time. Among these enzymes are those involved in glycolysis, a process by which ATP is generated during the enzymatic breakdown of glucose to pyruvate.Glycolysis is important in fast twitch muscles where ATP, produced at intermediate steps of the glycolytic pathway, fuels contraction and a variety of other ATP-dependent cellular processes. Information about the subcellular distribution, concentrations, and mutual interactions of the glycolytic enzymes and their metabolites is important for a complete understanding of metabolism in fast twitch muscles.In vertebrate fast twitch skeletal muscle fibers the glycolytic enzymes are regarded as soluble components of the fluid myoplasm because they are present in the supernatant fraction recovered after homogenization and centrifugation of the tissue sample (1). However, this assignment has often been a matter of dispute because the supernatant fraction may be only a rough approximation of the cytosol in situ (2-4). Not only are proteins in dilute slurries isolated under conditions far different from those in intact cells, additional information about their interactions may be lost using conventional methods of fractionation. Enzyme-enzyme interactions constitute an area of intense interest in structural genomics and enzymology (5, 6). Clearly studies in these areas would benefit from new approaches for isolation of proteins and determining their concentrations and stoichiometric relationships under conditions more closely approximating their native state. This information could help settle some controversial points debated over the past 50 years, such as whether large supramolecular complexes exist for glycolytic enzymes in the native cytosol (for a summary, see Ref. 5).Warmke et al. (7) pioneered a microvolumetric method of subcellular protein enrichment and fractionation in which cytosolic constituents of muscle were distinguished ...

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Section: Resultssupporting

confidence: 86%

Section: Resultssupporting

confidence: 86%

Concentrations of Glycolytic Enzymes and Other Cytosolic Proteins in the Diffusible Fraction of a Vertebrate Muscle Proteome

Maughan

Henkin

Vigoreaux

2005

Molecular & Cellular Proteomics

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“…The dissociation rate for Mg 2+ is thought to determine the physiological properties of parvalbumin and determine its contribution to relaxation rate, particularly in sub-maximal tetanic contractions (Hou et al, 1991(Hou et al, , 1993. Dissociation rates of Mg 2+ from parvalbumin might vary between isoforms of parvalbumin.…”

Section: +mentioning

confidence: 99%

Parvalbumin correlates with relaxation rate in the swimming muscle of sheepshead and kingfish

Wilwert

Madhoun

Coughlin

2006

Journal of Experimental Biology

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expression of parvalbumin isoforms will differ between the anterior and posterior red muscle, but little longitudinal variation will be observed in parvalbumin expression in white and pink muscle. We successfully employed protein electrophoresis (SDS-PAGE) with western blots to identify two parvalbumin isoforms in each muscle fiber type. SDS-PAGE and densitometry were used to determine the relative expression levels of the two parvalbumin isoforms and total parvalbumin expression. Red muscle displays a significant shift, from anterior to posterior, in the relative expression of the two isoforms, both in their relative contribution and in total parvalbumin content, but white and pink muscle did not. The red muscle of southern kingfish, Menticirrhus americanus (Pisces, F. Scianidae) showed a pattern similar to the red muscle of sheepshead.

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“…In contrast, parvalbumin has been shown to increase relaxation through an ATP-independent mechanism. Due to its Ca 2+ affinity, parvalbumin acts as a Ca 2+ skeletal muscle [16,17]. The protein is absent in cardiac tissue [18].…”

Section: Introductionmentioning

confidence: 99%

In vivo gene transfer of parvalbumin improves diastolic function in aged rat hearts

Schmidt

Zhu

Lebeche

et al. 2005

Cardiovascular Research

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Role of Parvalbumin in Relaxation of Frog Skeletal Muscle

Cited by 22 publications

References 23 publications

Concentrations of Glycolytic Enzymes and Other Cytosolic Proteins in the Diffusible Fraction of a Vertebrate Muscle Proteome

Concentrations of Glycolytic Enzymes and Other Cytosolic Proteins in the Diffusible Fraction of a Vertebrate Muscle Proteome

Parvalbumin correlates with relaxation rate in the swimming muscle of sheepshead and kingfish

In vivo gene transfer of parvalbumin improves diastolic function in aged rat hearts

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