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Related Concept Videos

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Gastrulation establishes the three primary tissues of an embryo: the ectoderm, mesoderm, and endoderm. This developmental process relies on a series of intricate cellular movements, which in humans transforms a flat, “bilaminar disc” composed of two cell sheets into a three-tiered structure. In the resulting embryo, the endoderm serves as the bottom layer, and stacked directly above it is the intermediate mesoderm, and then the uppermost ectoderm. Respectively, these tissue strata...
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Introduction to Actin01:26

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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Generation of Straight or Branched Actin Filaments01:14

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
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Formation of Higher-order Actin Filaments01:11

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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
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Tissue-specific forms of actin in the developing chick

R V Storti, D M Coen, A Rich

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    Chick brain and muscle actin show distinct differences in primary structure, revealed by urea/SDS gel electrophoresis. Muscle actin type evolves during embryonic development, shifting from brain-type to muscle-type actin.

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    Area of Science:

    • Biochemistry
    • Developmental Biology
    • Molecular Biology

    Background:

    • Actin is a highly conserved protein found in both muscle and non-muscle tissues.
    • Previous studies identified actin as a homogeneous protein across different tissue types.

    Purpose of the Study:

    • To identify and characterize actin from embryonic and adult chick brain and muscle.
    • To compare brain and muscle actin using polyacrylamide gel electrophoresis techniques.
    • To investigate the developmental changes in muscle actin composition during embryogenesis.

    Main Methods:

    • Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis.
    • Urea/SDS gradient polyacrylamide gel electrophoresis.
    • Comparative analysis of actin polypeptide migration patterns.

    Main Results:

    • Under SDS-PAGE, brain and muscle actins co-migrate, appearing homogeneous.
    • Urea/SDS gradient electrophoresis reveals distinct mobility differences between brain and muscle actins.
    • Embryonic chick thigh muscle actin transitions from a 'brain' type to a predominant 'muscle' type during development.

    Conclusions:

    • Actin isoforms in chick brain and muscle possess different primary structures.
    • The developmental shift in muscle actin suggests differential gene expression during muscle formation.
    • These findings contribute to understanding actin heterogeneity and its developmental regulation.