BIOCHEMICAL ASPECTS OF

DROWNING IMPACTS

Rondang Soegianto
2015
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Definition by World Health Organization:

Drowning is the process of experiencing
respiratory impairment from
submersion/immersion in liquid
Pathophysyology:
Oxygen deprivation
Water inhalation
Cold water immersion
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Oxygen Deprivation
Breathing reflex in human body is
- Weakly related to amount of O2 in blood
- Strongly related to amount of CO 2

During apnea, O2 is used up by cells and

excreted as CO2 breathing reflex
Continued lack of O2 (hypoxia) in brain
unconsciousness brain damage
Immediate artificial respiration (resuscitation)
very important for recovery.

Lack of O2 chemical changes in the blood

(disturbed acid-base balance)
May cause heart to stop beating (cardiac arrest).
Transport of O2 to brain stops brain death
after ~ 6 minutes without O2 and special
treatment.

Water Inhalation
Fresh water taken into lungs enters pulmonary
circulation by osmosis blood dilution
hemolysis. Electrical activity of heart disturbed,
plasma K+ >> and Na+ <<. ventricular fibrilation cardiac arrest. Acute renal failure can
result because of Hb accumulation in kidneys.

Salt water is hypertonic. Osmosis will pull

water from blood stream into lungs.
Thickening of blood cardiac arreast
Autopsies on human drowning fatalities do
not
show these effects.

Cold Water Immersion

Cause of death in cold and very cold water
usually due to lethal body reactions as
protective response to change of external
temperature, rather than any loss of core body
temperature, such as
- Uncontrolled rapid breathing
- Gasping, causing water inhalation
- Massive increase in blood pressure
- Cardiac strain cardiac arrest
- Panic

Biochemical Aspects
Risks and consequences:
Rescued person may be found
Already dead
Saved and recovering
Consequences of drowning experience

What makes a person able to survive

oxygen deprivation which could lead to death?
Humans are aerobic and need O2 to obtain
energy for the functioning of organs.
ATP biosynthesis occurs via Respiratory Chain
in mitochondria

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Globins
Globins are metalloproteins that bind O 2
reversibly thru Fe.
Four types of globins are found in humans
and vertebrae with different structure,
location and function. These are:
- Hemoglobin
- Myoglobin
- Neuroglobin
- Cytoglobin
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Hemoglobin (Hb)
Heterotetramer found in erythrocytes.
Functions in transport of O2.
Four protein subunits with heme attached.
A molecule of Hb binds 4 molecules O 2
Body produces ~ 160 million/min RBC
Lifespan ~ 110 days
Produced in bone marrow
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RBC production is stimulated by

erythropoietin
formed in kidney medulla
When O2 is low hormone >>
more erythrocytes p0roduced
No mitochondria in RBC.
Energy produced via glycolysis lactate

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Myoglobin (Mb)
Mb is an intracellular monomeric hemoprotein
Expressed in heart and oxidative skeletal
myofibres
Reversibly binds molecular O2 by its haem.
Functions as O2 storage protein in muscle that
is capable of releasing and delivering O 2 during
periods of Hypoxia or Anoxia to mitochondria.
High concentrations of Mb in muscle cells allow
people hold their breath for longer period of time
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Additional function of Mb:

Scavenging NO and ROS in the heart
Saturation curve of Hb is sigmoid
Saturation curve of Mb is hyperbolic
Explains why Mb is still capable of binding
O2 at low oxygen pressure
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Neuroglobin (Ngb)
Neuroglobin is a myoglobin-like
haemprotein
Expressed in vertebrate brain and retina
Involved in neuroprotection from damage
due to hypoxia or ischemia.

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Cytoglobin (Cygb)
Cygb is a globin molecule very much
expressed in all tissues, most utilized in
marine mammals.
Is thought to protect against hypoxia.
Functions to transfer O2 from arterial blood
to the brain.

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Cygb is a hexacoordinate hemoglobin that

facilitates diffusion of oxygen thru tissues..
scavenge nitric oxide or reactive oxygen
species protective function during oxidative
stress.

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