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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
Intracellular Signaling Cascades01:24

Intracellular Signaling Cascades

Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

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Related Experiment Video

Updated: May 17, 2026

Spectral Karyotyping to Study Chromosome Abnormalities in Humans and Mice with Polycystic Kidney Disease
12:47

Spectral Karyotyping to Study Chromosome Abnormalities in Humans and Mice with Polycystic Kidney Disease

Published on: February 3, 2012

Polycystins and cellular Ca2+ signaling.

D Mekahli1, Jan B Parys, G Bultynck

  • 1Laboratory of Molecular and Cellular Signaling, Department of Cellular and Molecular Medicine, KU Leuven, Campus Gasthuisberg O/N-I, B-802, Herestraat 49, 3000, Leuven, Belgium.

Cellular and Molecular Life Sciences : CMLS
|October 19, 2012
PubMed
Summary
This summary is machine-generated.

Autosomal dominant polycystic kidney disease (ADPKD) involves cell signaling dysfunction, particularly calcium (Ca2+) signaling. This review explores polycystin interactions with Ca2+ signaling, impacting cell proliferation and apoptosis in cystic kidney diseases.

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Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium
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Published on: September 1, 2015

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Published on: February 3, 2012

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Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium
08:46

Implementing Patch Clamp and Live Fluorescence Microscopy to Monitor Functional Properties of Freshly Isolated PKD Epithelium

Published on: September 1, 2015

Area of Science:

  • Nephrology
  • Cell Biology
  • Molecular Medicine

Background:

  • Autosomal dominant polycystic kidney disease (ADPKD) exhibits a cystic phenotype driven by cellular signaling dysregulation.
  • Key cellular processes affected include increased cell proliferation and apoptotic cell death.
  • Disruption of cellular calcium (Ca2+) signaling is implicated as a primary event in ADPKD pathogenesis.

Purpose of the Study:

  • To review current knowledge on the molecular and functional interactions between polycystins and cellular Ca2+ signaling components.
  • To discuss how altered Ca2+ signaling contributes to increased proliferation and apoptosis in ADPKD cystic cells.

Main Methods:

  • Literature review synthesizing existing research on polycystins and calcium signaling in ADPKD.
  • Analysis of molecular interactions and functional consequences of disrupted Ca2+ pathways.

Main Results:

  • Polycystins interact with multiple components of the cellular Ca2+ signaling machinery.
  • These interactions lead to significant alterations in intracellular Ca2+ dynamics.
  • Altered Ca2+ signaling pathways are directly linked to the observed increases in cell proliferation and apoptosis in cystic kidney epithelia.

Conclusions:

  • Dysfunctional Ca2+ signaling, mediated by polycystin interactions, is central to ADPKD cystogenesis.
  • Targeting polycystin-Ca2+ signaling pathways may offer therapeutic strategies for ADPKD.
  • Understanding these molecular mechanisms is crucial for developing treatments for cystic kidney diseases.