Desmin Chicken

Desmin Chicken Gizzard
Shipped with Ice Packs
In Stock

Description

Biological Functions in Avian Muscle

Desmin serves dual roles in chickens:

  • Structural Maintenance: Anchors sarcomeres and maintains myofibril alignment, preventing disorganization during muscle contraction .

  • Regeneration Marker: Elevated in fast-growing (FG) broilers during muscle repair cycles. Degeneration-regeneration processes in FG chickens correlate with fluctuating desmin levels (e.g., peak heterodimeric desmin at 21–28 days) .

Comparative Analysis in Broiler Chickens

Studies comparing fast-growing (FG) and medium-growing (MG) broilers reveal genotype-dependent desmin dynamics:

Table 1: Desmin Expression in Pectoralis major Muscles

Age (Days)Native Desmin (FG vs. MG)Heterodimeric Desmin (FG vs. MG)
7No significant differenceNo significant difference
21↑ 2-fold in FG ↑ 3-fold in FG
28↑ 1.5-fold in FG ↑ 2.5-fold in FG
42↓ 30% in FG ↓ 40% in FG

FG = Fast-growing; MG = Medium-growing. Arrows indicate relative changes compared to MG.

In FG chickens, desmin degradation and resynthesis cycles coincide with necrotic fiber replacement, while MG chickens exhibit stable expression . Immunohistochemistry confirms co-localization with vimentin in regenerating fibers .

Genetic and Molecular Insights

  • Amino Acid Sequence: Chicken desmin shares 91% homology with porcine desmin but only 64% with porcine vimentin, highlighting its unique intermediate filament structure .

  • Gene Expression: DES mRNA levels in FG broilers surpass MG by 2.5–3.0-fold during peak regeneration (21–35 days) .

Implications for Poultry Science and Human Medicine

  • Meat Quality: Post-mortem desmin degradation in breast muscle correlates with reduced shear force (102.44 N at slaughter → 34.26 N after 7 days), impacting tenderness .

  • Biomarker Potential: Elevated desmin in FG chickens signals susceptibility to growth-related myopathies, aiding breeder selection .

  • Human Health: Chicken desmin studies inform research on human desminopathies, including mitochondrial mislocalization and impaired myoblast fusion .

Research Gaps and Future Directions

  • Mechanistic Insights: The role of desmin-actin complexes in filament assembly remains unresolved .

  • Longitudinal Studies: Age-dependent desmin fluctuations in FG chickens warrant further proteomic profiling .

Product Specs

Description
Desmin Chicken is a protein with a calculated molecular mass of 53 kDa and an isoelectric point (pI) of 5.4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
Desmin was lyophilized from a solution containing 1 mg/ml Desmin, 10 mM sodium phosphate buffer (pH 7.5), 6M urea, 1mM EDTA, 2mM DTT, and 10mM methylammonium chloride.
Solubility
To reconstitute the lyophilized Desmin, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100 µg/ml. The reconstituted solution can then be further diluted in other aqueous solutions.
Stability
Store the lyophilized Desmin between 2-8°C. Do not freeze. After reconstitution, Desmin should be stored at -20°C. Avoid freeze-thaw cycles.
Purity
The purity of Desmin is greater than 98.0% as determined by SDS-PAGE.
Synonyms

Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

Source

Chicken gizzard.

Q&A

What is desmin and what structural role does it play in chicken muscle tissues?

Desmin is an intermediate filament protein that plays a critical role in maintaining the structural organization of muscle fibers, particularly during regenerative processes. In chicken tissues, desmin has been identified in pericytes of various microvascular beds, including cardiac muscle, exocrine pancreas, and kidney peritubular capillaries . Its presence supports the hypothesis that pericytes may possess contractile apparatus similar to that of vascular smooth muscle cells . The protein provides structural stability to muscle fibers and is involved in muscle fiber regeneration.

How does the distribution of desmin differ across chicken tissue types?

The distribution of desmin varies significantly across different chicken tissues:

  • Pericytes in capillaries of cardiac muscle, exocrine pancreas, and kidney (peritubular capillary) contain both desmin and vimentin

  • In capillaries where pericytes are absent, other cells adjacent to endothelial cells (such as Ito cells in hepatic sinusoids and reticular cells in splenic sinusoids) also contain both desmin and vimentin

  • Podocytes and mesangial cells around renal glomerular capillaries contain only vimentin, lacking desmin expression

  • In Pectoralis major muscles, desmin distribution patterns change during development and differ between fast-growing and medium-growing chicken genotypes

What is the relationship between desmin and vimentin in chicken muscle cells?

Desmin and vimentin are both intermediate filament proteins that often co-exist in muscle cells, forming heterodimers. Immunohistochemistry studies have revealed fibers co-expressing both proteins, particularly during muscle regeneration processes . The VIM-based heterodimer shows 2-3 fold higher levels in fast-growing chickens at days 21 and 28 compared to medium-growing chickens of the same age, which coincides with the beginning and progressive development of regenerative processes . While both proteins are expressed in similar tissue locations, they appear to serve distinct functions, with desmin more directly implicated in muscle regeneration than certain vimentin isoforms .

How does desmin expression change during growth in fast-growing versus medium-growing chickens?

Research comparing desmin expression between fast-growing (FG) and medium-growing (MG) chickens reveals significant differences in expression patterns:

  • Desmin content shows fluctuating trends in FG chickens throughout development (days 7-42), reflecting its role in maintaining structural organization of regenerating fibers

  • Higher expression levels of the DES gene are observed in FG chickens compared to MG chickens, supporting its potential application as a marker of muscle fiber regeneration

  • The protein-level observations generally mirror gene expression patterns, though with a notable time lag between gene expression changes and observable protein-level effects

  • These differences in expression patterns correlate with the growth rate of the chickens, suggesting a relationship between muscle regeneration processes and growth rate in meat-type chickens

How can researchers distinguish between different experimental models when studying desmin in chicken muscle?

When designing experiments to study desmin in chicken muscle:

  • Genotype selection is critical - FG and MG chickens show distinctly different desmin expression patterns and can serve as comparative models

  • Developmental timeline must be carefully planned - collecting samples at specific stages (7, 14, 21, 28, 35, and 42 days) allows tracking of temporal changes

  • Initial classification based on histological features is essential before proceeding to protein and gene analysis

  • Combining multiple analytical approaches (protein analysis, gene expression, and histology) provides more comprehensive understanding

  • Standardized husbandry conditions (feeding program, stocking density, handling) must be maintained to minimize variables

What evidence exists for desmin as a molecular marker of muscle regeneration in chickens?

Several lines of evidence support desmin's potential as a molecular marker for muscle regeneration:

  • Higher expression levels of the DES gene in FG chickens compared to MG chickens correlate with increased regenerative processes

  • Fluctuating trends in desmin protein content and its heterodimer in FG chickens reflect ongoing structural reorganization during regeneration

  • Immunohistochemistry studies show co-expression of desmin and vimentin in regenerating muscle fibers

  • The temporal patterns of desmin expression coincide with periods of intense muscle growth and development in FG chickens

These findings collectively "support the existence of a relationship between the occurrence of muscle regeneration and the growth rate of meat-type chickens and corroborate the potential use of VIM and DES as molecular markers of these cellular processes" .

What techniques are most effective for studying desmin expression in chicken muscle tissues?

A comprehensive approach to studying desmin in chicken muscle requires multiple complementary techniques:

  • Western blot analysis: For quantification of desmin protein levels and heterodimers

  • Immunohistochemistry (IHC): For visualizing desmin distribution in tissue sections and identifying co-expression with other proteins

  • Gene expression analysis: For quantifying DES gene expression using appropriate primers

  • Immunofluorescent labeling: For examining intermediate filament composition in specific cell types

  • Immunoelectron microscopic labeling: For detailed subcellular localization of desmin

When properly combined, these techniques allow researchers to correlate protein expression with gene transcription and histological features, providing comprehensive insights into desmin's role in muscle development and regeneration.

How should samples be collected and preserved for optimal desmin analysis?

Based on established protocols, the following procedures are recommended for sample collection and preservation:

For histology and immunohistochemical analyses:

  • Excise samples from the ventral surface of the Pectoralis major (facing the skin)

  • Quickly freeze in isopentane (cooled with liquid nitrogen)

  • Store at -80°C until analysis

For protein and RNA extraction:

  • Collect samples from the same position of each Pectoralis major

  • Quickly freeze in liquid nitrogen

  • Store in a deep freezer (-80°C) until extraction

Consistent sampling location is critical as desmin expression may vary across different regions of the same muscle.

How should researchers interpret conflicting data in desmin expression studies?

When interpreting seemingly contradictory results in desmin studies:

  • Consider the potential time lag between gene expression and observable protein-level changes

  • Different isoforms may have distinct functions - research indicates that unlike the common VIM sequence, the VIM long isoform may not be directly implicated in muscle regeneration

  • Fluctuations in expression may be functionally significant rather than experimental artifacts

  • Growth rate correlations should be evaluated - desmin expression patterns relate to growth rates of meat-type chickens

  • Evaluate methodological differences between studies, including:

    • Chicken genotypes used

    • Developmental stages examined

    • Tissue preparation methods

    • Antibody specificity

    • Analytical techniques employed

What controls are essential for desmin expression studies in chickens?

Appropriate controls are crucial for accurate interpretation of desmin expression data:

  • Genotype controls: Medium-growing chickens serve as useful comparative controls for fast-growing chickens

  • Age-matched comparisons: Samples from different genotypes should be compared at identical developmental stages

  • Tissue-type controls: Including tissues known to express only vimentin (such as podocytes and mesangial cells)

  • Multiple sampling locations: Collecting samples from standardized locations to account for regional variations

  • Antibody controls: Validating antibody specificity using known positive and negative tissues

How can researchers quantify changes in desmin expression at both protein and gene levels?

For comprehensive quantification of desmin expression:

  • Protein level quantification:

    • Western blot analysis with appropriate loading controls

    • Densitometric analysis of bands corresponding to desmin and its heterodimers

    • Normalization to housekeeping proteins

  • Gene expression quantification:

    • RT-PCR or qPCR targeting the DES gene

    • Comparison between different genotypes and developmental stages

    • Analysis of both common and alternative transcript isoforms

  • Data integration:

    • Correlate protein levels with gene expression data

    • Account for potential time lag between transcription and translation

    • Contextualize with histological observations

What approaches help distinguish normal desmin expression from pathological changes?

To differentiate normal developmental changes from pathological alterations:

  • Compare with age-matched controls from different genotypes (e.g., MG vs. FG chickens)

  • Establish baseline expression patterns across multiple developmental timepoints

  • Correlate desmin expression with histological features indicative of regeneration

  • Examine co-expression patterns with other markers like vimentin

  • Consider the cellular localization of desmin, as abnormal localization may indicate pathology

Product Science Overview

Discovery and Importance

Desmin was first identified as a major component of the intermediate filaments in muscle cells. These filaments are part of the cytoskeleton, which provides mechanical support and helps maintain the shape of the cell. In chicken gizzard, desmin is enriched along with 100-A filaments, which are essential for muscle contraction and stability .

Purification and Properties

The purification of desmin from chicken gizzard involves several steps, including homogenization, centrifugation, and solubilization. The process typically starts with the extraction of desmin using high salt concentrations, such as 1 M potassium iodide (KI). This step removes most of the actin, another protein found in muscle cells, but a small fraction of actin remains insoluble along with desmin .

Desmin can be further purified by repeated cycles of solubilization using 1 M acetic acid and subsequent precipitation by neutralization to pH 4. This method ensures that desmin is obtained in a relatively pure form, free from other contaminating proteins .

Structural and Functional Role

Desmin plays a critical role in the organization and function of muscle cells. It forms a network of filaments that link the contractile apparatus to the cell membrane and other cellular structures. This network is essential for the transmission of mechanical forces generated during muscle contraction.

In chicken gizzard, desmin is localized in dense bodies and longitudinal channels that link consecutive dense bodies. These structures are also occupied by actin, highlighting the close association between desmin and actin in muscle cells . The interaction between desmin and actin is crucial for maintaining the structural integrity and proper functioning of the muscle tissue.

Applications in Research

Desmin from chicken gizzard is widely used in research to study the properties and functions of intermediate filaments. It serves as a protein standard for various biochemical assays, including immunoblotting, immunization, and immunoassays . Researchers use desmin to investigate the molecular mechanisms underlying muscle diseases and to develop potential therapeutic strategies.

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