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Glycoprotein

INTRODUCTION
Glycoprotein is proteins that contain covalently attached sugar residues. The hydrophilic and
polar characteristics of sugars may dramatically change the chemical characteristics of the
protein to which they are attached. The addition of sugars is often required for a
glycoprotein to function properly and reach its ultimate destination in the cell or organism.
Glycoproteins are frequently present at the surface of cells where they function as
membrane proteins or as part of the extracellular matrix. These cell surface glycoproteins
play a critical role in cell–cell interactions and the mechanisms of infection by bacteria and
viruses.

The plasma membrane surrounds the eukaryotic cell. Glycoproteins—proteins bonded to


carbohydrates—allow for the detection of foreign cells, such as invading bacteria.

GLYCOSYLATION
Glycosylation is the process or result of addition of saccharides to proteins and lipids.

CLASSIFICATION
There are two major types of glycoproteins based on their structure and the mechanism of
synthesis: N-linked glycoproteins and O-linked glycoproteins.
Glycoprotein

N-linked Glycoprotein

• synthesized and modified within two membrane-bound organelles in the cell, the
rough endoplasmic reticulum and the Golgi apparatus.
• important for the folding of some eukaryotic proteins. The N-linked glycosylation
process occurs in eukaryotes and widely in Achaea, but very rarely in bacteria.
• protein component of the glycoprotein is assembled on the surface of the rough
endoplasmic reticulum by the sequential addition of amino acids, creating a linear
polymer of amino acids called a polypeptide.
• the specific order of the amino acids in the polypeptide is critical to its function and
is referred to as the amino acid sequence

The twenty different amino acids can be used for the synthesis of polypeptides. One of the
twenty amino acids used for the synthesis of polypeptides, asparagine (C4H8N2O3), is
essential for the synthesis of N-linked glycoproteins.

N-linked glycoproteins have carbohydrates attached to the R side chain of asparagine


residues within a polypeptide. The carbohydrate is always located in amino acid sequences,
where some other amino acid and then a serine or threonine residue follows the asparagine
(-Asn-Xaa-Ser/Thr). Carbohydrate is not attached to the polypeptide one sugar at a time.
Rather, a large preformed carbohydrate containing fourteen or more sugar residues is
attached to the asparagine as the protein is being translated in the rough endoplasmic
reticulum. The carbohydrate on the glycoprotein is then modified by enzymes that remove
some sugars; and attach others as the newly formed glycoprotein moves from the rough
endoplasmic reticulum to the Golgi apparatus and other locations in the cell. Many N-linked
glycoproteins eventually become part of the cell membrane or are secreted by the cell.
Glycoprotein

O-linked Glycoproteins

O-linked glycoproteins are usually synthesized by the addition of sugar residues to the
hydroxyl side chain of serine or threonine residues in polypeptides in the Golgi apparatus.
Unlike N-linked glycoproteins, O-linked glycoproteins are synthesized by the addition of a
single sugar residue at a time. Many O-linked glycoproteins are secreted by the cell to
become a part of the extracellular matrix that surrounds it.

Nonenzymatic Glycosylation

Nonenzymatic glycosylation or glycation creates glycoproteins by the chemical addition of


sugars to polypeptides. Since this type of glycosylation is nonenzymatic, the factors that
control glycosylation are simply time and the concentration of sugar. Older proteins are
more glycosylated, and people with higher circulating levels of glucose experience higher
levels of nonenzymatic glycosylation. This is the basis of the glycosylated hemoglobin A1c
diagnostic test used for the monitoring and long-term maintenance of blood sugar levels in
diabetics.
Glycoprotein

THE EIGHT SUGARS CONTAINED IN GLYCOPROTEINS


Glycoprotein

BIOFUNCTION

Function Description
Structural molecule Collagen

Many of the viruses with helical internal


structure have outer coverings (also known
as envelopes) composed of lipoprotein or
glycoprotein, or both.

Lubricant and protective agent Mucin

Transport molecule Transferrin (for iron ion delivery),


ceruloplasmin (carries 90% of the copper in
our plasma)

Immunologic molecule Immunoglobins, histocompatibility antigens

Hormone Chorionoic gonadotropin (to prevent the


disintegration of the corpus luteum of the
ovary and thereby maintain progesterone
production that is critical for a pregnancy in
humans).

thyroid-stimulating hormone (TSH)

Enzyme Various, e.g. alkaline phosphatase

Cell attachment-recognition site Various proteins involved in cell-cell (e.g.


sperm-oocyte), virus-cell, bacterium-cell, and
hormone cell interactions

Prion, an infectious agent that does not


contain any nucleic acid but rather an
abnormal form of a glycoprotein.

HIV infects certain human cells by binding its


envelope glycoproteins gp120 and gp41 to
specific molecules on the surface of the cells.
Only cells that carry the appropriate
molecules are susceptible to infection by
HIV.

Antifreeze Certain plasma proteins of coldwater fish

Interact with specific carbohydrates Lectins, selectins (cell adhesion lectins),


antibodies

Receptor Various proteins involved in hormone and


drug action
Glycoprotein

Affect folding of certain proteins Calnexin, calreticulin

Creutzfeldt-Jakob Disease; The gene for the


normal glycoprotein is on the short arm of
chromosome 20, and mutations of this gene
have been shown to have a dominant
inheritance, that is, are likely to be inherited.
About 15 per cent of cases of CJD are
inherited.

Regulation of development Notch (highly conserved cell signalling


system present in most multicellular
organisms) and its analogs, key proteins in
development.

Glycoprotein laminin controls the growth of


axons within the central nervous system.

Homeostasis (and thrombosis) Specific glycoproteins on the surface


membranes of platelets.

Cobalamin, or vitamin B12, one of the most


recently isolated vitamins, is necessary in
minute amounts for the formation of
nucleoproteins, proteins, and red blood cells,
and for the functioning of the nervous
system. Cobalamin deficiency is often due to
the inability of the stomach to produce a
glycoprotein (intrinsic factor), which aids in
the absorption of this vitamin.