BIOCHEMISTRY

Course code: PBT2531M

GLYCOCONJUGATES

Submitted by,
A.Annapoorani.
18PBTE05.
I PG Biotechnology.
 INTRODUCTION:
Glycoconjugates is the general classification for
carbohydrates covalently linked with other type of molecules
such as proteins, peptides, lipids and saccharides. The
biosynthesis of glycoconjugates occurs in two specialized,
membranous biosynthetic compartments within the cell: the
endoplasmic reticulum and the Golgi apparatus. Degradation
of glycoconjugates occurs in another specialized
membranous digestive compartment: the lysosome.

BIOLOGICAL ROLE:
Glycoconjugates are play an important roles as stored
fuels such as starch, glycogen, dextran and as structural
materials like cellulose, chitin, peptidoglycans,
polysaccharides and oligosaccharides are information
carriers. It is used as destination labels for some proteins and
as mediators of specific cell-cell interactions and interactions
between cells and the extracellular matrix.
Specific carbohydrate containing molecules act in cell-
cell recognition and adhesion, cell migration during
development, blood clotting, the immune response, and
wound healing, to name but a few of their many roles. So the
glycoconjugates states that which is the biologically active
molecule.
TYPES:
Glycoconjugates are very important compounds in
biology and consist of many different categories such as,
 Glycoproteins,
 Proteoglycans,
 Glycolipids,
 Glycopeptides,
 Glycosides.
They are involved in cell-cell interactions, recognition,
in cell-matrix interactions: in detoxification processes.

PROTEOGLYCANS:
Proteoglycans are macromolecules of the cell
surface or extracellular matrix in which one or more
glycosaminoglycan chains are joined covalently to a
membrane protein or a secreted protein. The
glycosaminoglycan forms the greater fraction of the
proteoglycan molecule, and it is the main site of biological
activity. The biological activity is the provision of multiple
binding sites, rich in opportunities for hydrogen bonding and
electrostatic interactions with other proteins of the cell
surface or the extracellular matrix. Proteoglycans are major
components of connective tissue such as cartilage, in which
their many noncovalent interactions with other
proteoglycans, proteins, and glycosaminoglycans provide
strength.

THE SPECIFIC GAGs OF PHYSIOLOGICAL

SIGNIFICANCE ARE:

Hyaluronic acid (D-glucuronate + GlcNAc)

Occurence:
Synovial fluid, ECM of loose connective tissue.

Hyaluronic acid is unique among the GAGs because it

does not contain any sulfate and is not found covalently
attached to proteins. It forms non-covalently linked
complexes with proteoglycans in the ECM.
Hyaluronic acid polymers are very large (100-10,000
kD) and can displace a large volume of water.

Dermatan sulfate (L-iduronate + GlcNAc sulfate)

Occurence: Skin, Blood vessels, Heart valves.

Chondroitin sulfate (D-glucuronate + GalNAc sulfate)

Occurence: Cartilage, Bone, Heart valves.

It is the most abundant GAG.

Heparin and heparan sulfate (D-glucuronate sulfate + N-

sulfo-D-glucosamine)

Heparans have less sulfate groups than heparins

Occurence:
Heparin: component of intracellular granules of mast cells
lining the arteries of the lungs, liver and skin
Heparan sulfate: basement membranes, component of cell
surfaces

Keratan sulfate (Gal + GlcNAc sulfate)

Occurence: Cornea, Bone, Cartilage.

Keratan sulfates are often aggregated with chondroitin
sulfates.

GLYCOPROTEINS:
Glycoproteins have one or several oligosaccharides of
varying complexity joined covalently to a protein. They are
found on the outer face of the plasma membrane, in the
extracellular matrix, and in the blood. Inside cells they are
found in specific organelles such as Golgi complexes,
secretory granules, and lysosomes. The oligosaccharide
portions of glycoproteins are less monotonous than the
glycosaminoglycan chains of proteoglycans; they are rich in
information, forming highly specific sites for recognition
and high-affinity binding by other proteins.

O-LINKED AND N-LINKED GLYCOPROTEINS:

Glycoproteins are categorized according to the attachment
site of the carbohydrate to an amino acid in the protein.
O-linked glycoproteins:
The carbohydrate bonds to the oxygen atom (O) of the
hydroxyl group (-OH) of the R group of either the amino
acid threonine or serine. O-linked carbohydrates may also
bond to hydroxylysine or hydroxyproline. The process is
termed O-glycosylation. O-linked glycoproteins are bound to
sugar within the Golgi complex.
N-linked glycoproteins:
Carbohydrate bonded to the nitrogen (N) of the amino
group (-NH2) of the R group of the amino acid asparagine.
The R group is usually the amide side chain of asparagine.
The bonding process is called N-glycosylation. N-linked
glycoproteins gain their sugar from the endoplasmic
reticulum membrane and then are transported to the Golgi
complex for modification.
While O-linked and N-linked glycoproteins are the most
common forms, other connections are also possible:
 P-glycosylation occurs when the sugar attaches to the
phosphorus of phosphoserine.
C-glycosylation is when the sugar attaches to the carbon
atom of an amino acid. An example is when the sugar
mannose bonds to the carbon in tryptophan.
Glypiation is when a glycophosphatidylinositol (GPI)
glycolipid attaches to the carbon terminus of a polypeptide.

EXAMPLES AND FUNCTIONS:

Glycoproteins function in the structure, reproduction,
immune system, hormones, and protection of cells and
organisms.
Glycoproteins are found on the surface of the lipid
bilayer of cell membranes. Their hydrophilic nature allows
them to function in the aqueous environment, where they act
in cell-cell recognition and binding of other molecules. Cell
surface glycoproteins are also important for cross-linking
cells and proteins (e.g., collagen) to add strength and
stability to a tissue. Glycoproteins in plant cells are what
allow plants to stand upright against the force of gravity.
Glycosylated proteins are not just critical for intercellular
communication. They also help organ systems communicate
with each other. Glycoproteins are found in brain gray
matter, where they work together with axons and
synaptosomes.
EXAMPLES: Hormones may be glycoproteins,
including human chorionic gonadotropin (HCG) and
erythropoietin (EPO).
Blood clotting depends on the glycoproteins
prothrombin, thrombin and fibrinogen.
Cell markers may be glycoproteins. The MN blood
groups are due to two polymorphic forms of the glycoprotein
glycophorin A.
Glycophorin A is also important because it's the
attachment site for Plasmodium falciparum, a human blood
parasite.
Glycoproteins are important for reproduction because
they allow for the binding of the sperm cell to the surface of
the egg.
Mucins are glycoproteins found in mucus. The
molecules protect sensitive epithelial surfaces including the
respiratory, urinary, digestive and reproductive tracts.
The immune response relies on glycoproteins. The
carbohydrate of antibodies (which are glycoproteins)
determines the specific antigen it can bind. B cells and T
cells have surface glycoproteins which bind antigens, as
well.
GLYCOLIPIDS:
Glycolipids are membrane lipids in which the
hydrophilic head groups are oligosaccharides, which, as in
glycoproteins, act as specific sites for recognition by
carbohydrate-binding proteins. The four types of human
RBC have different oligosaccharides or antigens in their cell
membranes. Blood groups depends on the gangliosides in the
surface of the RBC.

CONCLUSION:
Glycoconjugates are biologically important molecules
with diverse functions. They consist of carbohydrates of
varying size and complexity, attached to a non-sugar moiety
as a lipid or a protein. Glycoconjugates are often very
complex and intricrate biosynthetic pathways makes
overexpression difficult.
Generally the carbohydrate part(s) play an integral role
in the function of a glycoconjugate; prominent examples of
this are NCAM and blood proteins where fine details in the
carbohydrate structure determine cell binding or not or
lifetime in circulation.
 Although the important molecular species DNA,
RNA, ATP, cAMP, cGMP, NADH, NADPH, and coenzyme
A all contain a carbohydrate part, generally they are not
considered as glycoconjugates. Glycocojugates is covalent
linking of carbohydrates antigens to protein scaffolds with
goal of achieving a long term immunological response in
body. Immunization with glycoconjugates successfully
induced long term immune memory against carbohydrates
antigens.

REFERENCES:
 Glycoconjugates by Fredrik Wallner, Department of
chemistry, Umea University. PDF
 Devlin, M.T, (1997), Textbook of Biochemistry with
clinical correlations, New York: Wiley-Liss.
 Nelson, D.L and cox, M.M (2008). Lehinger-
Principles of Biochemistry (5th edition). New York:
W.H.Freeman and company. Print.
 Rawn, J.D, (2009), Biochemistry. (4th edition).
Burlington: Neil Patterson Publisher. Print.
 https://www.diva-portal.org
 www.springer.com>glycoconjugates>pdf
 www.encyclopedia.org>glycoconjugates