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BLOOD INCOMPATIBILITY

GROUP 4
Red Blood Cell
The main function Hemoglobin- about
are relatively simple, 95% of its intracellular
it delivers oxygen to protein
the tissue and of There are no
helping in the intracellular organelles
disposal of carbon such as mitochondria,
dioxide and protons lysosomes or Golgi
formed by tissue apparatus.
metabolism. It is nonnucleated
 ATP used is synthesized
from Glycolysis and is
important in processes
that help the red cell
maintain its biconcave
shape and also in the
regulation of the
transport of ions.
THE COMPOSITION OF RBC
MEMBRANE
• about 50% lipid and 50% protein
• The major phospholipids are phosphatidyl
choline, phosphatidyl ethanolamine, and
phosphatidyl serine along with sphingomyelin.
• The Major Integral Proteins: Anion Exchange
Protein & the Glycophorins
• Spectrin, Ankyrin, & Other Peripheral
Membrane Proteins Help Determine the
Shape & Flexibility of the Red Blood Cell
THE COMPOSITION OF RBC
MEMBRANE
The anion exchange protein (band 3)
• a transmembrane glycoprotein
• multipass membrane protein
• forms a tunnel, permitting the exchange of
chloride for bicarbonate
• The amino terminal end binds many proteins,
including hemoglobin, proteins 4.1 and 4.2,
ankyrin, and several glycolytic enzymes.
Glycophorins A, B, and C
• transmembrane glycoproteins but of the
single-pass type
• A is the major glycophorin
• Glycophorin A contains binding sites for
influenza virus and for Plasmodium falciparum
Spectrin
• major protein of the cytoskeleton. It is
composed of two polypeptides: spectrin 1 (α
chain) and spectrin 2 (β chain).
• four binding sites can be defined in spectrin:
(1) for self-association, (2) for ankyrin (bands
2.1, etc), (3) for actin (band 5), and (4) for
protein 4.1.
Ankyrin
• Pyramid-shaped protein that binds spectrin.
• It binds tightly to band 3, securing attachment
of spectrin to the membrane.
• Ankyrin is sensitive to proteolysis
Actin (band 5)
• short, double-helical filaments of F-actin.
• The tail end of spectrin dimers binds to actin.
• Actin also binds to protein 4.1.
 Protein 4.1
• a globular protein, binds tightly to the tail end
of spectrin
• also binds to the integral proteins,
glycophorins A and C, thereby attaching the
ternary complex to the membrane
• may interact with certain membrane
phospholipids, thus connecting the lipid
bilayer to the cytoskeleton
THE COMPOSITION OF RBC MEMBRANE
Biochemical basis of blood typing and of
blood type determination.
Antibody Immune Response
H Substance Is the Biosynthetic Precursor
of Both the A & B Substances

Formed by Fucosyltransferase- that catalyses


the addition of terminal fucose in alpha 1-> 2
linkage onto the terminal Gal residue of its
precursor
• The A Gene Encodes a GalNAc Transferase

• The B Gene a Gal Transferase

• The O Gene an Inactive Product


Importance of the oligosaccharide
sequence in the RBC membrane in blood
type determination
Roles of Genetics in determining the Blood
type
Roles of Genetics in determining the Blood
type
Predicting human blood types
What are the possible blood types of the offspring of a
cross between individuals that are type AB and type
O?
Cases on Blood Incompatibility
Hemolytic Disease of the Newborn
Hemolytic Disease of the Newborn

• Erythroblastosis Fetalis
• Rh INCOMPATIBILITY- a condition which
develops when a pregnant woman has an Rh-
negative blood type and the fetus she carries
has Rh-positive blood type.
Hemolytic Transfusion Reaction
• blood transfused into an individual is an
incompatible blood type
• may result to:
– minor rise in the plasma bilirubin to severe
jaundice
– renal tubular damage leading to death
Hemolytic Transfusion Reaction
Thank you for listening….

Bustos, Precious
Cabantac, Katherine Rhea
Cabungcal, Kristine
Cada, Kristel Joy
Cada, Kristian
Caeg, Anne Clarisse
Calupig, Tiffany

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