Related Experiment Video
Updated: Jun 25, 2026

07:51
Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Calmodulin effects on steroids-regulated plasma membrane calcium pump activity
Ludmila Zylinska1, Iwona Kowalska, Bozena Ferenc
1Department of Molecular Neurochemistry, Medical University, Lodz, Poland. luska@csk.umed.lodz.pl
Cell Biochemistry and Function
|February 20, 2009
Summary
Steroids rapidly influence cell calcium levels by affecting the plasma membrane calcium pump (PMCA). This action varies by cell type and steroid structure, impacting calcium regulation.
Area of Science:
- Cellular Biology
- Neuroendocrinology
- Biochemistry
Background:
- Non-genomic steroid actions modulate intracellular signaling pathways rapidly.
- Plasma membrane calcium pump (PMCA) precisely regulates intracellular calcium (Ca2+).
- PMCA activity is modulated by calmodulin (CaM) and exhibits isoform diversity.
Purpose of the Study:
- To investigate the role of PMCA isoforms and CaM in Ca2+ uptake regulation by various steroids.
- To examine steroid effects on Ca2+ transport in different cell types.
Main Methods:
- Utilized membranes from rat cortical synaptosomes, PC12 cells, and human erythrocytes.
- Assessed Ca2+ uptake in response to estradiol, DHEA, and pregnenolone (and sulfates) at concentrations from 10(-9) to 10(-6) M.
- Evaluated the impact of calmodulin (CaM) on steroid-mediated Ca2+ transport.
Main Results:
- Steroids generally increased Ca2+ uptake in excitable cell membranes, with variable effects.
- CaM decreased PMCA-mediated Ca2+ transport by 30-40% in most cases.
- Erythrocyte PMCA showed differential regulation, with CaM enhancing Ca2+ extrusion with 17-beta-estradiol and PREG.
Conclusions:
- Steroids can significantly control cytoplasmic calcium concentration within physiological ranges.
- Cell type, PMCA isoform expression, CaM presence, and steroid structure influence the regulatory response.
- Findings highlight the complex interplay between steroids, PMCA, and calcium homeostasis.
Related Concept Videos
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,...
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 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...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Antihypertensive Drugs: Action of Calcium Channel Blockers
Calcium ions are essential to contract smooth muscle cells in blood vessels. They enter these cells through voltage-dependent calcium channels, specifically L-type calcium channels in the cell membrane. These L-type calcium channels are integral to the excitation-contraction coupling process in smooth muscle. When a stimulus is received by smooth muscle cells, their membrane depolarizes. This alteration in membrane potential instigates the opening of L-type calcium channels. As a result,...
Secondary Messengers in Hormone Action
Water-soluble hormones cannot cross the plasma membrane, so they rely on protein receptors that span the membrane to trigger intracellular signaling pathways. These pathways then activate second messengers inside the cell, including cAMP or calcium ions.
Many hormones bind to transmembrane G protein-coupled receptors that connect to regulatory G proteins. These G proteins can then activate enzymes such as adenylyl cyclase or phospholipase C. Adenylyl cyclase converts ATP to cAMP, activating...
Many hormones bind to transmembrane G protein-coupled receptors that connect to regulatory G proteins. These G proteins can then activate enzymes such as adenylyl cyclase or phospholipase C. Adenylyl cyclase converts ATP to cAMP, activating...
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...
Smooth Muscle Contraction
Smooth muscle contraction is a complex process vital for various bodily functions, from maintaining blood vessel tension to facilitating the movement of food through the digestive tract. Unlike striated muscles, smooth muscle contraction begins more slowly and lasts longer.
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...

