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Related Concept Videos

Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
What are Second Messengers?01:12

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
What are Second Messengers?01:12

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

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Related Experiment Video

Updated: Jul 5, 2026

Measurement of Cyclic Guanosine Monophosphate (cGMP) in Solid Tissues using Competitive Enzyme-Linked Immunosorbent Assay (ELISA)
07:15

Measurement of Cyclic Guanosine Monophosphate (cGMP) in Solid Tissues using Competitive Enzyme-Linked Immunosorbent Assay (ELISA)

Published on: July 3, 2025

Cyclic GMP and the second messenger hypothesis.

D L Garbers1

  • 1David L. Garbers is at the Howard Hughes Medical Institute, Departments of Pharmacology and Molecular Physiology and Biophysics, Vanderbilt Medical Center, Nashville, TN 37232, USA.

Trends in Endocrinology and Metabolism: TEM
|November 1, 1989
PubMed
Summary
This summary is machine-generated.

Guanylate cyclase, an enzyme in the plasma membrane, has distinct intracellular and extracellular regions. Binding of extracellular peptides to this enzyme boosts the production of cyclic GMP, a key cellular messenger.

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Area of Science:

  • Molecular Biology
  • Cell Signaling

Background:

  • Guanylate cyclase is a crucial enzyme involved in cellular signaling pathways.
  • The enzyme's structure includes transmembrane domains that dictate its localization and function.

Purpose of the Study:

  • To elucidate the structural organization of plasma membrane-bound guanylate cyclase.
  • To understand the mechanism by which extracellular peptides modulate guanylate cyclase activity.

Main Methods:

  • The study likely involved protein structural analysis and biochemical assays to investigate guanylate cyclase.
  • Experiments focused on identifying the transmembrane domain and its role in protein structure.

Main Results:

  • A single transmembrane domain was identified, separating conserved intracellular and variable extracellular domains of guanylate cyclase.
  • Direct binding of extracellular peptides to the enzyme was observed to enhance its activity.

Conclusions:

  • The plasma membrane form of guanylate cyclase possesses a unique transmembrane domain structure.
  • Extracellular peptide binding is a key regulatory mechanism for guanylate cyclase, leading to increased cyclic GMP production.