The Physiology of Blood: 128

1
The Physiology of Blood 1/28

• Chemical composition of plasma
• Lipoproteins Good, Bad and Ugly
• Types of leukocytes
• LAST MATERIAL FOR LECTURE TEST 1 CH 17 and 18
  (up to what we cover in lecture today- hemoglobin
  cooperativity not on test)
• What does hemoglobin look like?
• How does cooperativity ensure that hemoglobin
  is either 100 saturated with oxygen or 0
  saturated?
• WHY is it important for a fetus to have Hb that
  are different from adult Hb?
• How does oxygen binding by hemoglobin change
  during exercise? Why is this so beneficial?
• What particles do we find in blood besides the
  formed elements?
• Why are lipoproteins needed to move lipids in the
  blood?
• Which lipoproteins are termed Good and Bad?
• How are red blood cells typed with the ABO and Rh
  Systems?
• What are the primary leukocytes and what is a
  differential blood count?
• What is the specialized function of each type of
  WBC?

2
Lab Exam Next Thursday sign-up Friday

• Practice Quiz for Monday notes
• 1) Which type of anemia would be associated with
  deficient EPO production?
• a) Hemolytic b) Hemorhhagic c)
  Erythropoietic d) Polycythemic
• 2) The hormone _______reduces sodium reabsorption
  I nthe kidney and blood pressure.
• a)Thymopoietin b)Aldosterone c)Angiotensin
  d)Nitric oxide e)None of above
• 3) A normal hematocrit value for a healthy woman
  would be ______.
• a) 32 b) 37 c) 42 d) 47 e) 52
  
• 4) Which paracrine hormones would be most likely
  to be associated with causing your allergy
  symptoms?
• Arachidonic acids b) Prostacyclin s c)
  Prostaglandins d) Leukotrienes
• 5) True/False Your pineal gland secreted more
  melatonin this morning when you woke up before
  your alarm clock to come to class.

3
What is the relative size of the materials in
blood?
Each erythrocytes contains about 380 million
molecules of oxygen carrying hemoglobin (4 O2/Hb).
4
PLASMA PROTEINS HAVE VARIED SIZE, WEIGHTS AND
FUNCTIONS. WHILE THEY MAY NOT BE PRESENT IN
LARGE AMOUNTS, THEY ARE CRITICAL FOR OUR HEALTH.

• Liver produces about 4 grams plasma protein/hour.
• ..But not the gamma globulins
• Albumin 60- Pickup truck of the human body
• Plasma Globulin Types 36 ?-, ?-, and ?-
• Fibrinogen 4gt Fibringt Cross-linked FibringtFirm
  Clot Serum is plasma that has had the fibrinogen
  removed!
• Plasma proteins influence drug availability-
• What would happen to blood viscosity in a person
  who has chronic blood loss and anemia from a
  stomach ulcer and liver failure?

5
WHAT HEALTH CONSEQUENCES COULD CHANGES IN PLASMA
AND/OR BLOOD VISCOSITY HAVE TO A PERSON?

• Plasma and blood viscosity relative to water-
• PCV, disease and cardiac workload- Do blood
  thinners really change viscosity? What
  happens to plasma viscosity after a diuretic?
• Osmotic pressure of the protein in the plasma
  creates an effect that pulls fluid from the
  interstitium into the plasma- -Kwashiorkor,
  Ascites, and dietary protein deficiency -What
  causes the pot-bellied appearance as child nears
  death?
• Viscosity and clotting during severe dehydration
  
• Why does gangrene often occur in the limbs of a
  diabetic?
• What happens to blood viscosity during severe
  frostbite? Why does gangrene often result?

6
Lipoproteins and the similar Chylomicrons have an
outer phospholipid layer with special proteins
facing the water and variable lipid contents on
the inside. These small particles help you move
lipids between locations in the body.
7
What particles carry fats in our bodies?

• Chylomicrons largest and synthesized in the
  intestine.
• Carry_____________from the _______to the
  ________
• Very Low Density Lipoproteins VLDL Big and
  synthesized by liver . Carry_______from the
  _______to the _________
• Low Density Lipoproteins LDL VLDL-left over!
  Carry__________from the _______to the
  ______________
• High Density Lipoproteins HDL smallest and
  synthesized by liver. Carry________from the
  _______to the ____________
• WHY is HDL called Good Cholesterol and LDL
  Bad Cholesterol
• Plasma cholesterol and coronary heart
  disease/stroke risk
• Dietary influence and Genetic Influence
• Why do we often die of a heart attack a few hours
  after a fatty Christmas dinner? Look and see
  next Wednesday!

8
What to know about the five white blood cell
(leukocyte) types? 1) ID by appearance, 2) ID by
function, 3) Relative frequency

• Granulocytes grainy cytoplasm
• Neutraphil most common
• Nucleus sausages on a string!
• Count increased in presence to fight bacterial
  infections
• Eosinophil uncommon
• Red/pink cytosol color
• Phagocytose Ab-Ag, makes defensive enzymes,
  allergies and inflammation
• Indicator of gut parasites
• Basophil purple and rare
• Secrete histamine-dilator
• Secrete heparin-block clotting
• Intensify allergic response

• Agranulocytes clear cytosol
• Lypmphocytes common
• Small cell with big round nucleus
• B-cellmakeAbs against Antigens
• T-cell and Nat. Killer CellHandle Ags
• Monocytes slightly common
• Clear cytosol/bean-like nucleus
• Become macrophages when mature
• Migrate in response to signals
• Dont Forget RBC no nucleus for gas transport
• Platelet Hemostasis

9
Leukopenia low WBC numbers under 5K/ul
Leukocytosis high WBC numbers
10K/ulDifferential Counts of each WBC as
of total WBC count

• Leukemia WBC Cancer
• Myeloid Cancer granulocytes
• Lymphoid Cancer agranulocytes
• Chemotherapy often results in a fatal opportunist
  infection in patient! Because no replacement
  WBCs are available when infection is encountered.

10
Content for Lecture Test 1 Stops here50 points
45 multiple choice questions 5 written pts 2
pt extra credit The rest of this material will
be on test 2Let the notes be your guide to
what is most important and most likely to appear
on the exam?Look at questions in back of
chapter?Look at practice quiz questions?Create
your own study guide an exam questions from your
notes?Practice test in ONLY to help you
understand test format.DO NOT study it as a
study guide.Bring a CLEAN scantron (50 que/
half sheet).Write written questions anywhere you
want ON BACK OF SCANTONDouble check your bubble
answers for smears, mistakes, etc. What you hand
in is what is graded, instructor will not correct
for poorly erased, partially filled bubbles, or
other errors.
11
Hemoglobin consists of 4 protein subunits
(globins) and each globin has a heme at its
center. Each heme holds a single Fe and can
hold a single O2 molecule (4 O2
/hemoglobin).There are about 380,000,000
hemoglobins in each erythrocyte!Each erythrocyte
can carry up to about 4X380,000,000 oxygens!
12
Hemoglobin has 4 globins, 4 hemes, 4 Fe, and
binds up to a maximum of 4 O2 (or No O2 at all)

• The protein subunits are called globins
• Two can be alpha in adult or fetus
• Two can be beta in adult-appear just before
  birth
• Two can be gamma in fetus-lost right around
  birth
• The HEME is a ring like structure that has Fe
  in the center. Oxygen is attracted to the Fe
  that binds it temporarily and releases it later
  where needed.
• Attachment and release is determined by
  concentration gradients (What are gradients in
  LUNG or HEART?)
• Oxygen tends to fall of the heme if there is
  little oxygen around the heme.so oxygen is then
  supplied to tissues.
• Oxygen binds to the heme when there is plenty of
  oxygen available and none is attached to the
  hemethis condition occurs when erythrocytes are
  in the capillaries that line the alveoli of the
  lung.

13
Cooperativity describes how the four globins of
hemoglobin interact with each other and oxygen.

• When all 4 hemes are without oxygen (empty)
  affinity is low, but gradient is high.
• The binding of oxygen to any one heme affects the
  remaining three and makes them more likely to
  bind oxygen.
• When another oxygen binds, it makes the remaining
  two even more likely to bind oxygen.
• Binding of a third oxygen tremendously increases
  the affinity of the last empty heme to find and
  oxygen.
• Assuming an oxygen can bind the heme, the
  hemoglobin is now filled (100 saturated) with
  oxygen.
• INVERSE When any single heme in the hemoglobin
  looses an oxygen, the other three are more likely
  to lose an oxygen, etc
• Net Result? Hemes want to be completely filled
  with oxygen or completely empty! This gives the
  binding curve a sigmoid shape. This is HUGELY
  important physiologically!

14
Myoglobin in muscle has one heme and globin (No
Cooperativity).Hemoglobin in a erythrocyte has
four hemes and globins.Why do the oxygen binding
characteristics of these two proteins look so
different? Hyperbolic vs. Sigmoid Curve
Oxygen is bound to almost 100 of available
Hb-hemes in the lung.
1) Oxygen is removed from the hemoglobin 2)
Percent saturation reduced (oxygen used).
Hb has Cooperativity--------- Mb has NO
Cooperativity!
15
Why would you want fetal hemoglobin (2 gamma
subunits) to bind oxygen much more tightly than
adult hemoglobin? Is there more oxygen in the
blood of the fetus or the mother? Like all
molecules oxygen can only diffuse down
concentration gradients in the body.
DANGER! When carbon monoxide has an extremely
high affinity for Hb (Hb-CO), so oxygen cannot
bind Hb in the lung!
16
The Bohr Effect is amazing!

• Acids accumulate ( ?pH) in metabolically active
  tissues!
• This is a signal that oxygen needs have increased
  in the tissue!
• If oxygen needs increase, oxygen delivery needs
  to increase! HOW IS THIS DONE?
• Protons (H or acids) are a signal that cause the
  hemoglobins to DUMP their oxygen in acidic
  tissues that should also be hypoxic!
• The Bohr Effect says that as conditions become
  more acidic (even slightly) the hemoglobin is
  more likely to release its oxygen.
• The reverse can also occur..remember
  hyperventilating as a kid?
• This causes your blood pH to become alkaline and
  you pass out because you have plent of oxygen in
  the blood, you cannot remove the oxygen from your
  hemoglobin properly in your brain!

17
The shift in the oxygen binding curve to the
right means less oxygen will be attached to the
hemoglobins in an acidic region! So oxygen leaves
the hemoglobin and can be delivered to where it
is needed most! ?Carbon dioxide and ?Temperature
have similar effects.
18
If the Hb is not bound by oxygen you will appear
cyanotic (bluish)! Remember that only a tiny
amount of oxygen can dissolve directly in blood!
(see bottom yellow line) The more hemoglobin you
have in your blood, the more oxygen your blood
can deliver (that simple)! If the tissues are
warmer or more acidic, the oxygen is more likely
to leave the hemoglobin so it can be used in this
tissue (that simple).
Shift occurs if pH? or Temp. ?