Lysozyme activity in the initially formed in situ pellicle
Christian Hannig1, Jörg Hoch, Klaus Becker
1Department of Operative Dentistry, Preventive Dentistry and Periodontology, University of Göttingen, Robert-Koch-Street 40, D-37075 Göttingen, Germany. christian.hannig@med.uni-goettingen.de
Archives of Oral Biology
|June 23, 2005
Summary
Salivary pellicle, rich in lysozyme, exhibits enzymatic activity even after short formation times. This activity is consistent across different oral sites and formation durations, though individual variations exist.
Area of Science:
- Biochemistry
- Oral Biology
- Enzymology
Background:
- Lysozyme is a key enzyme found in salivary pellicles.
- Understanding its activity within the pellicle is crucial for oral health research.
Purpose of the Study:
- To investigate the enzymatic activity of lysozyme immobilized in salivary pellicles.
- To assess the influence of pellicle formation time and oral site on lysozyme activity.
Main Methods:
- An in situ study using bovine enamel slabs on dental trays worn by human subjects.
- Pellicle formation for 3 and 30 minutes at buccal and oral sites.
- Photometric determination of both desorbed and immobilized lysozyme activity using Micrococcus lysodeicticus.
Main Results:
- All investigated pellicles demonstrated lysozyme activity.
- No significant difference in activity was found based on pellicle formation time (3 vs. 30 min) or oral site (buccal vs. oral).
- Significant intra- and inter-individual variations in lysozyme activity were observed.
Conclusions:
- In situ salivary pellicles expose lysozyme activity rapidly, within 3 minutes of formation.
- Pellicle formation time and location do not impact exposed lysozyme activity.
- Substantial individual variability in salivary lysozyme activity is a key characteristic.
More Related Videos
Related Concept Videos
01:06Lipid Digestion
Lipids are large molecules that are generally not water-soluble. Since most of the digestive enzymes in the human body are water-based, there are specific steps the body must take to break down lipids and make them available for use.
01:31Lysosomes
Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
01:22Lysosomal Hydrolases
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
01:39Mechanism of Filopodia Formation
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
01:31Mechanism of Lamellipodia Formation
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
01:19Formation of Lipopolysaccharides
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...