8 Glycoproteins Study Guide
Glycoproteins
Definition: Glycoproteins are proteins that have a small amount of carbohydrates attached to them.
Contrast with Proteoglycans: Proteoglycans are predominantly carbohydrates with only a small protein component.
Functionality: Glycoproteins typically have defined functions, and they are predominantly found outside the cell or in the bloodstream.
Types of Glycoproteins
O-linked Glycoproteins
Attachment: O-linked carbohydrates are attached to serine or threonine residues through a free hydroxyl group.
Variety: O-linked glycans exhibit a greater variety in structure.
N-linked Glycoproteins
Attachment: N-linked carbohydrates are attached to asparagine residues through the amide nitrogen in the R group of asparagine.
Predictability: N-linked glycans are generally more predictable in structure compared to O-linked.
Core Structure: Commonly starts with two N-acetylglucosamine (GlcNAc) residues followed by mannose.
**Classification: **N-linked glycans can further be categorized into the following:
High Mannose Type: Composed primarily of mannose along with N-acetylglucosamine.
Hybrid Type: Begins with N-acetylglucosamine, has mannose, and then features additional structures such as N-acetylglucosamine and galactose.
Complex Type: Contains N-acetylglucosamine, mannose, galactose, and includes a sialic acid residue at the terminal end.
ABO Blood Type System and Glycoproteins
Overview: The ABO blood type system includes antigens that are glycoproteins or glycolipids with specific carbohydrate structures.
Common Structures:
All blood types have a common structure consisting of:
Galactose residue
N-acetylglucosamine residue (GlcNAc)
N-acetylgalactosamine residue (GalNAc)
Fucose
Differentiation of Blood Types:
Type O: No additional attachment on the galactose.
Type B: Contains an additional galactose residue attached to the initial galactose.
Type A: Contains an N-acetylgalactosamine attached to the initial galactose.
Antibody Interaction with Antigen
Antibody in Type B Blood: The antibody that recognizes the type A antigen is the anti-A antibody.
Interactions: The interaction involves several key amino acid residues:
Histidine Residue: Interacts with the oxygen atom of the acetyl group of the type A antigen.
Tyrosine Residue (Tyrosine L32): Forms a hydrogen bond with the hydroxyl group of the fucose residue.
Tryptophan Residue: Forms hydrophobic interactions with the nonpolar side of N-acetylgalactosamine (GalNAc).
Carbohydrate-Protein Interactions
Hydrophobic and Hydrogen Bonding: Normal interactions between carbohydrates and proteins include specific hydrogen bonding and non-specific hydrophobic interactions.
Examples of Non-Solubility: Cellulose and amylose, which are generally insoluble in water.
Hexose Structures: Hexoses with the C3 hydroxyl group pointed upward (mannose, galactose, glucose) tend to exhibit hydrophobic interactions with amino acids.
Selectins and Cellular Interactions
Definition of Selectins: Selectins are a specific type of lectin that facilitate cell-to-cell interactions by binding carbohydrates.
Function in Leukocyte Movement:
Interaction with Endothelial Cells: Selectins on endothelial cells (E and P selectins) interact with L-selectin on leukocytes, promoting rolling and migration.
Inflammatory Response: Under inflammation, endothelial cells increase E-selectin expression.
Rolling to Binding: Leukocyte rolls through the bloodstream and binds tightly to sites of inflammation due to the presence of selectins.
Glycoproteins and Inflammation
Evolutionary Perspective: Inflammation was historically vital for healing; however, advancements in medicine have made it less essential, leading to potential overreactions in modern contexts.
Examples of Receptor Structures:
Oligosaccharide Composition: Consists of N-acetylglucose, fucose, galactose, and sialic acid.
Calcium’s Role: Calcium aids in mediating interactions between carbohydrates on receptors and selectins, enhancing leukocyte adhesion effectiveness.
Fish Antifreeze Proteins
Description: A unique protein that enables fish in polar regions to survive freezing conditions.
Mechanism: The protein contains a repeat sequence of alanine, alanine, and threonine, and features a disaccharide (galactose attached to N-acetylgalactosamine).
Function: The hydroxyl groups on the antifreeze protein interact with water molecules, preventing ice crystal formation, allowing fish to thrive in frigid oceans.
Biomass Consideration: Notably, these antifreeze proteins are crucial to the ecology of regions such as Antarctica where species relying on these adaptations constitute a significant portion of local fish biomass (approximately 90%).