SAVED BY ROOMMATE

SCHOOL OF MEDICAL SCIENCES. PBL SCENARIO: SAVED BY ROOMMATE. : 

SCHOOL OF MEDICAL SCIENCES. PBL SCENARIO: SAVED BY ROOMMATE. UNIVERSITY OF CAPE COAST

GROUP MEMBERS: 

GROUP MEMBERS Nkansah Betty Priscilla Baafi Mohammed Don Kudus Moro Safori Oparebia Yaa Edward Kyei-Achampong Kojo Arhin Jeffrey Johnny Arthur Komey Addaquay Frank Jemima Owusua Yeboah George Aidoo FACILITATOR: Mr. Michael Anim.

PROBLEM STATEMENT : 

PROBLEM STATEMENT Kofi experienced difficulty in breathing and a mild headache which followed with progressively blurred vision, in an airtight room. He collapsed in an attempt to pick a book from his book shelf after a feel of lightheadedness and unsteadiness.

OBJECTIVES: 

OBJECTIVES Transport of gases in the blood. Exchange of gases; in the Lungs And in the tissues. Structure and functions of hemoglobin ( Hb ). Kinetics of O 2 -Hb binding. Carbon monoxide poisoning and its management. Pulse oximetry and its interpretations.

GAS TRANSPORT IN THE BLOOD.: 

GAS TRANSPORT IN THE BLOOD. Major gases; O 2 & CO 2 . GAS METHOD OF TRANSPORT IN BLOOD PERCENTAGE CARRIED OXYGEN PHYSICALLY DISSOLVES IN THE BLOOD PLASMA. BOUND TO HEMOGLOBIN. 1.5 98.5 CARBON DIOXIDE PHYSICALLY DISSOLVES IN BLOOD PLASMA. BOUND TO HEMOGLOBIN AS BICARBONATE IONS(HCO 3 - ) 10 30 60

EXCHANGE OF GASES: 

EXCHANGE OF GASES Achieved by simple diffusion. And largely depends on partial pressure gradient. In the lungs. In the tissues.

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EXCHANGE OF GASES In the lungs In the tissues

Haemoglobin (Hb): 

Haemoglobin ( Hb ) Two parts Haem Globin Haem & globin produced at two different sites in the cells Haem in mitochondria Globin in polyribosomes

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Synthesis of Haem Protoporphyrin ring with an iron atom in centre The main site is mitochondria as it contains ALAS

Synthesis of globin: 

Synthesis of globin

Synthesis of Haemoglobin: 

Synthesis of Haemoglobin

Synthesis of Haemoglobin: 

Synthesis of Haemoglobin Various types of globin combines with haem to form different haemoglobin . Eight functional globin chains, arranged in two clusters the b - cluster ( b , g , d and e globin genes) on the short arm of chromosome 11 a - cluster ( a and z globin genes) on the short arm of chromosome 16

Functions of Haemoglobin: 

Functions of Haemoglobin Reaction of Hb & oxygen Oxygen delivery to the tissues One Hb can bind to four O 2 molecules b chain move closer when oxygenated When oxygenated 2,3-DPG is pushed out b chains are pulled apart when O 2 is unloaded, permitting entry of 2,3-DPG resulting in lower affinity of O 2

Kinetics of oxygen binding.: 

Kinetics of oxygen binding. Four subunits, so four O 2 -binding sites. Hemoglobin exhibits cooperative binding kinetics. Oxygenation of hemoglobin is accompanied by conformational changes Apoprotein Near the heme group 14

REGULATORS OF HEMAGLOBIN.: 

REGULATORS OF HEMAGLOBIN. In the context of the affinity of hemoglobin for oxygen there are four primary regulators. These are CO 2 , hydrogen ion (H + ), chloride ion ( Cl - ), and 2,3-bisphosphoglycerate (2,3BPG). 15

Oxygen-haemoglobin dissociation curve: 

Oxygen- haemoglobin dissociation curve O 2 carrying capacity of Hb at different Po 2 Sigmoid shape Binding of one molecule facilitate the second molecule binding P 50 (partial pressure of O 2 at which Hb is half saturated with O 2 ) 26.6mmHg

Oxygen-haemoglobin dissociation curve: 

Oxygen- haemoglobin dissociation curve O 2 carrying capacity of Hb at different Po 2 Sigmoid shape Binding of one molecule facilitate the second molecule binding P 50 (partial pressure of O 2 at which Hb is half saturated with O 2 ) 26.6mmHg

Hb-oxygen dissociation curve: 

Hb -oxygen dissociation curve

Hb-oxygen dissociation curve: 

The normal position of curve depends on Concentration of 2,3-DPG H + ion concentration (pH) CO 2 in red blood cells Structure of Hb Hb-oxygen dissociation curve

Hb-oxygen dissociation curve: 

Right shift (easy oxygen delivery) High 2,3-DPG High H + High CO 2 HbS Left shift (give up oxygen less readily) Low 2,3-DPG HbF Hb-oxygen dissociation curve

CARBON MONOXIDE (CO) POISONING.: 

CARBON MONOXIDE (CO) POISONING. Properties of CO. Produces from incomplete combustion of substances containing carbon. Early symptoms of carbon monoxide poisoning such as headaches, nausea, and fatigue. Prolonged exposure can lead to brain damage and even death.

CARBON MONOXIDE MANAGEMENT.: 

CARBON MONOXIDE MANAGEMENT. Immediate treatment. Hospital; oxygen therapy. Hyperbaric oxygen therapy in SEVERE CASES.

PULSE OXIMETRY: 

PULSE OXIMETRY How does an oximeter works? What does pulse oximeter measures? The types of oximeters . The interpretations as in Kofi’s case.

REFERENCES: 

REFERENCES Maton , Anthea ; Jean Hopkins, Charles William McLaughlin, Susan Johnson, Maryanna Quon Warner, David LaHart , Jill D. Wright (1993). Human Biology and Health . Englewood Cliffs, New Jersey, USA: Prentice Hall. Dominguez de Villota ED, Ruiz Carmona MT, Rubio JJ, de Andrés S (December 1981). "Equality of the in vivo and in vitro oxygen-binding capacity of haemoglobin in patients with severe respiratory disease". Uthman , MD, Ed. " Hemoglobinopathies and Thalassemias " . http://web2.airmail.net/uthman/hemoglobinopathy/hemoglobinopathy.html . Retrieved 2007-12-26. Reed, Leslie. "Adaptation found in mouse genes." Omaha World-Herald 11 Aug. 2009: EBSCO. Web. 30 Oct. 2009. "Hemoglobin Synthesis" . April 14, 2002. http://sickle.bwh.harvard.edu/hbsynthesis.html . Retrieved 2007-12-26. van Kessel et al. "2.4 Proteins - Natural Polyamides." Chemistry 12. Toronto: Nelson, 2003. 122. Print. "Hemoglobin Tutorial." University of Massachusetts Amherst. N.p ., n.d . Web. 23 Oct. 2009. < http://www.umass.edu/molvis/tutorials/hemoglobin/index.htm >.

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THANK YOU