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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
Relaxation of Skeletal Muscles01:29

Relaxation of Skeletal Muscles

The period of muscle contraction primarily influences the duration of stimulation at the neuromuscular junction (NMJ), the presence of free calcium ions in the sarcoplasm, and the availability of energy or ATP to support contractions.
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open.

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Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
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ATPase-coupled release control from polyion complex capsules encapsulating muscle proteins.

Kousuke Sugiura1, Kousaku Ohkawa, Toshihiro Hirai

  • 1Department of Kansei Engineering, Faculty of Textile Science and Technology, Shinshu University, Japan.

Macromolecular Bioscience
|April 13, 2007
PubMed
Summary

This study encapsulated muscle proteins into gellan-chitosan capsules, protecting them from degradation. Actomyosin

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Area of Science:

  • Biomaterials Science
  • Protein Chemistry
  • Polymer Science

Background:

  • Muscle contraction involves the protein complex actomyosin, composed of myosin and actin.
  • Encapsulation technologies are crucial for protecting sensitive biomolecules.
  • Polyion complex (PIC) capsules offer potential for controlled release applications.

Purpose of the Study:

  • To encapsulate actomyosin into gellan-chitosan PIC capsules.
  • To investigate the functional recovery and stability of encapsulated actomyosin.
  • To study the release kinetics of small proteins from these capsules and the influence of actomyosin activity.

Main Methods:

  • Encapsulation of actomyosin (myosin and F-actin) into gellan-chitosan polyion complex (PIC) capsules.
  • Assay of myosin-ATPase activity to confirm actomyosin complex formation and function.
  • Protease protection assays to evaluate the stability of encapsulated proteins.
  • In vitro release studies using myoglobin and cytochrome c under varying ionic strength and pH conditions.
  • Investigation of release modulation by Mg2+-ATP and encapsulated actomyosin.

Main Results:

  • Successful encapsulation of actomyosin with approximately 50% myosin-ATPase activity recovery.
  • Evidence of actomyosin complex formation and Mg2+-ATPase activity stimulation by F-actin.
  • Encapsulation protected myosin, F-actin, and actomyosin from protease hydrolysis.
  • Differential release of myoglobin and cytochrome c influenced by ionic strength and pH.
  • Reduced release of small proteins in the presence of Mg2+-ATP and encapsulated actomyosin, indicating release regulation.

Conclusions:

  • Gellan-chitosan PIC capsules can successfully encapsulate and protect actomyosin.
  • The ATPase-coupled sliding motion of actomyosin filaments appears to regulate the pore size of the PIC capsule membranes.
  • This suggests a novel mechanism for controlled release based on protein activity within the capsule.