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Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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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.
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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.
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...
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ATP Driven Pumps I: An Overview01:27

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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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ATP Synthase: Structure01:18

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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 Synthase: Mechanism01:48

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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...
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Overview of Secretory Vesicles01:33

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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V-type ATPase proton pump expression during enamel formation.

Juni Sarkar1, Xin Wen1, Emil J Simanian1

  • 1Center for Craniofacial Molecular Biology, Herman Ostrow School of Dentistry of USC, University of Southern California, Los Angeles 90033, USA.

Matrix Biology : Journal of the International Society for Matrix Biology
|November 21, 2015
PubMed
Summary

The V-type ATPase proton pump is upregulated in enamel-forming cells during tooth development. This finding is crucial for understanding dental health and enamel formation, particularly during the maturation stage.

Keywords:
ATP6 subunitsAmelogenesisV-type ATPasepH regulation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Developmental Biology

Background:

  • Intracellular pH regulation is vital for cellular functions, with V-type ATPase (a proton pump) playing a critical role.
  • Dysregulation of pH, often due to ion channel mutations, is linked to diseases like renal tubular acidosis and osteoporosis.
  • The V-type ATPase's role in amelogenesis (enamel formation), particularly its connection to endocytosis and lysosomal acidification in ameloblasts, requires further elucidation.

Purpose of the Study:

  • To investigate the expression patterns of V-type ATPase subunits in ameloblasts during different stages of enamel development.
  • To understand the functional significance of V-type ATPase-mediated pH regulation in amelogenesis.
  • To identify specific V-type ATPase subunits upregulated during the maturation stage of amelogenesis.

Main Methods:

  • Quantitative RT-PCR was used to assess V-type ATPase subunit gene expression in secretory and maturation-stage enamel organs.
  • Western blot analysis validated qPCR findings for specific V-type ATPase subunits (Atp6v0d2, Atp6v1b2, Atp6v1c1, Atp6v1e1).
  • Immunohistochemistry was employed to determine the spatiotemporal localization of V-type ATPase subunits within the enamel organ.

Main Results:

  • Cytoplasmic V-type ATPase expression was significantly higher in maturation-stage ameloblasts compared to secretory-stage ameloblasts.
  • Increased V-type ATPase expression correlates with heightened endocytotic activity and lysosomal acidification needs during enamel maturation.
  • Immunolocalization revealed significant expression of V-type ATPase subunits (Atp6v1c1, Atp6v1e1) at the apical membrane of maturation-stage ameloblasts.

Conclusions:

  • V-type ATPase is significantly upregulated in enamel organ cells during the maturation stage of amelogenesis.
  • The apical membrane localization of V-type ATPase in maturation-stage ameloblasts suggests a role in regulating the extracellular environment or specific transport processes.
  • These findings enhance our understanding of the V-type ATPase's critical role in pH homeostasis during enamel development and its potential implications for dental health.