Related Experiment Video
Updated: Jun 24, 2026
09:30
Phosphopeptide Analysis of Rodent Epididymal Spermatozoa
Published on: December 30, 2014
Dynamics of heparin-binding proteins on boar sperm
Dora G Dapino1, Juan M Teijeiro, Marcelo O Cabada
1Cátedra de Fisiología. Facultad de Ciencias Veterinarias, Universidad Nacional de Rosario, Argentina.
Animal Reproduction Science
|March 31, 2009
Summary
Heparin-binding proteins (HBP) on boar sperm change location during capacitation, indicating membrane remodelling. This HBP pattern shift offers a new method to assess sperm physiological state in vitro.
Area of Science:
- Reproductive biology
- Cell biology
- Biochemistry
Background:
- Heparin-binding proteins (HBP) play roles in sperm function.
- Understanding HBP dynamics is crucial for evaluating sperm capacitation.
Purpose of the Study:
- To investigate the presence, topology, and dynamics of HBP on boar sperm.
- To correlate HBP distribution patterns with sperm capacitation status.
Main Methods:
- Subcellular fractionation and biotinylated heparin for HBP detection.
- Indirect fluorescence microscopy to visualize HBP binding patterns.
- Assessment of acrosome reaction and protein phosphorylation for capacitation validation.
Main Results:
- HBP were identified as peripheral and integral periacrosomal membrane proteins.
- Two distinct HBP fluorescent patterns (A and B) were observed, correlating with non-capacitated and capacitated states.
- Capacitation significantly increased the proportion of sperm exhibiting pattern B.
- Heparin decreased p32 phosphorylation, suggesting an alternative capacitation pathway.
Conclusions:
- HBP distribution on boar sperm changes during capacitation, reflecting membrane surface remodelling.
- HBP patterns provide a novel, simple method for evaluating in vitro boar sperm capacitation.
Related Concept Videos
01:30Anticoagulant Drugs: Low-Molecular-Weight Heparins
Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
01:30Drug Binding to Blood Components
When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...
01:16Protein-Drug Binding: Mechanism and Kinetics
Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
01:29Drug Distribution: Plasma Protein Binding
Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...