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ATP Driven Pumps II: P-type Pumps01:34

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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.
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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.
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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps that are embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction...
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In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would...
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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...
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ATP release through pannexon channels.

Gerhard Dahl1

  • 1School of Medicine, University of Miami, 1600 NW 10th Avenue, Miami, FL 33136, USA gdahl@med.miami.edu.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|May 27, 2015
PubMed
Summary
This summary is machine-generated.

Extracellular adenosine triphosphate (ATP) signals cells, but excessive release via Pannexin1 (Panx1) channels can cause cell death. Panx1 channels regulate ATP release, preventing harmful overstimulation through a feedback mechanism.

Keywords:
ATPPannexinallostericconductancepermeabilitypotassium

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Area of Science:

  • Cellular biology
  • Physiology
  • Molecular biology

Background:

  • Extracellular adenosine triphosphate (ATP) is a crucial signaling molecule involved in various physiological processes.
  • ATP release from cells occurs through multiple mechanisms, with channel-mediated release being a key pathway.
  • Pannexin1 (Panx1) channels are central to this channel-mediated release of extracellular ATP.

Purpose of the Study:

  • To review the role of Pannexin1 (Panx1) channels in extracellular adenosine triphosphate (ATP) release.
  • To elucidate the mechanisms by which Panx1 channels mediate ATP efflux and are modulated by ATP.
  • To explain the regulatory role of Panx1 in preventing excessive purinergic signaling and potential cell death.

Main Methods:

  • Review of existing literature on Pannexin1 (Panx1) channel function and extracellular adenosine triphosphate (ATP) signaling.
  • Analysis of the structural and functional properties of Panx1 channels in different conformations.
  • Examination of the interplay between Panx1 channels, purinergic receptors (P2X and P2Y), and apoptotic pathways.

Main Results:

  • Pannexin1 (Panx1) forms a plasma membrane channel (pannexon) that facilitates adenosine triphosphate (ATP) release.
  • The Panx1 channel exhibits distinct conformations (large, non-selective; small, chloride-selective) depending on stimulation.
  • ATP not only exits through Panx1 but also modulates channel activity, creating a feedback loop involving purinergic receptors and apoptosis.

Conclusions:

  • Pannexin1 (Panx1) channels are critical conduits for extracellular adenosine triphosphate (ATP) release, influencing diverse physiological functions.
  • A negative feedback mechanism exists where ATP binding to Panx1 can inhibit channel activity, preventing excessive signaling.
  • Understanding the dual role of Panx1 in ATP release and regulation is vital for comprehending cellular communication and preventing pathological conditions.