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NCE Year 2 · 2 Credits · Compulsory · Rain Semester

BIO 222 — Vertebrate
Anatomy & Physiology

Structure meets function — 15 weeks of interactive anatomy, biochemistry, and physiology for Nigerian biology teachers

12Body Systems
15Weeks
15Quizzes
12Diagrams

Welcome to BIO 222

Select a week to begin. Progress saves automatically.

🎯 Course Objectives
  • Outline and explain the various organ systems of the vertebrate body
  • Describe the structure and functions of the digestive, circulatory, respiratory, excretory, nervous, skeletal, endocrine, and reproductive systems
  • Explain enzyme biochemistry, nutrition, and metabolic processes
  • Describe the reproductive systems and processes of fertilisation, gestation, and birth
WEEK 01

Introduction — Scope of Vertebrate Anatomy & Physiology

Definitions · Levels of organisation · Tissue types · Overview of systems

Learning Outcomes

  • Define anatomy, physiology, and their relationship
  • List the levels of biological organisation from chemical to organism
  • Describe the four tissue types in vertebrates
  • Name the major organ systems and their primary functions

1.1 Definitions

Anatomy is the scientific study of the structure of organisms and their component parts. It asks: "What is this?" and "Where is it?"

Physiology is the study of the normal functions of living organisms and their parts. It asks: "What does it do?" and "How does it work?"

Together they form the foundation of all biomedical and biological science. Structure and function are inseparable — the shape of the heart's valves determines their pumping function; the shape of alveoli determines their gas exchange efficiency.

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This course focuses primarily on mammals (human as the model) with comparative reference to amphibians (frog) — two vertebrate classes with contrasting physiological adaptations.

1.2 Levels of Organisation

Levels of Biological Organisation — hover each level
Chemical Atoms, molecules Cellular Individual cells Tissue Groups of similar cells + matrix Organ Two+ tissue types with specific function e.g. heart, liver Organ System Organs working together e.g. digestive Organism All systems integrated complete body
Organisation increases upward in complexity. Each level depends on the levels below it. BIO 222 focuses mainly on the organ and organ-system levels.

1.3 Four Tissue Types

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Epithelial Tissue
Lines surfaces; forms glands; covers body
Functions: protection, secretion, absorption, sensory reception. Types: simple (one layer) or stratified (multilayer); squamous, cuboidal, or columnar. Examples: skin epidermis, intestinal lining, lung alveolar lining, kidney tubules.
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Connective Tissue
Supports, binds, connects, transports
Most diverse tissue type. Functions: structural support, binding organs, transport (blood). Types: loose connective tissue, dense connective tissue, cartilage (hyaline, fibrous, elastic), bone, blood, adipose (fat) tissue.
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Muscular Tissue
Contracts to produce movement
Three types: (1) Skeletal muscle — striated, voluntary, multinucleate; attached to bones by tendons. (2) Smooth muscle — non-striated, involuntary; walls of hollow organs (gut, blood vessels). (3) Cardiac muscle — striated, involuntary, intercalated discs; heart wall only.
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Nervous Tissue
Detects stimuli; transmits signals
Two cell types: (1) Neurons — excitable cells that generate and conduct electrical impulses. (2) Glial cells (neuroglia) — support, nourish, and protect neurons; Schwann cells (PNS), oligodendrocytes, astrocytes, microglia (CNS). Form brain, spinal cord, and all nerves.
📝 Self-Check Quiz — Week 1
What is the correct hierarchical order of biological organisation from simplest to most complex?
WEEK 02

Nutrition, Balanced Diet & Liver Function

Components of food · Mineral requirements · Deamination · Urea synthesis

Learning Outcomes

  • State the six classes of food and the function of each
  • Define balanced diet and explain its importance
  • State the mineral requirements of animals with their sources and functions
  • Explain the function of the liver with emphasis on deamination and urea synthesis

2.1 Components of Food

Nutrient ClassChemical NaturePrimary FunctionFood Sources
CarbohydratesSugars, starch, glycogen (C, H, O — H:O = 2:1)Main energy source (4 kcal/g); glucose for cellular respirationYam, cassava, rice, plantain, maize
ProteinsPolypeptide chains of amino acids (C, H, O, N, S)Growth and repair; enzymes and hormones; antibodies; transport (haemoglobin)Beans, groundnut, fish, meat, eggs
Lipids (Fats & Oils)Glycerol + fatty acids; phospholipids, steroidsEnergy store (9 kcal/g); cell membranes; fat-soluble vitamins; insulationPalm oil, groundnut oil, butter, avocado
VitaminsOrganic compounds (varied structure); fat-soluble (A,D,E,K) or water-soluble (B complex, C)Coenzymes in metabolic reactions; antioxidants; regulationVegetables, fruits, animal organs
MineralsInorganic ionsStructural (bones, teeth); regulatory (nerve impulse, pH)See table below
WaterH₂OUniversal solvent; transport medium; reactant in hydrolysis; thermoregulationDrinking water; fruits; all foods
Dietary FibreNon-digestible polysaccharides (cellulose, pectin)Promotes gut motility; prevents constipation; feeds gut microbiomeVegetables, whole grains, legumes

2.2 Mineral Requirements

MineralFunctionDeficiency
Calcium (Ca²⁺)Bone and teeth mineralisation; muscle contraction; nerve impulse; blood clottingRickets (children), osteomalacia (adults), tetany
Phosphorus (PO₄³⁻)Bone and teeth; ATP synthesis; DNA/RNA backbone; cell membranesBone weakness, impaired energy metabolism
Iron (Fe²⁺/Fe³⁺)Haemoglobin (O₂ transport); myoglobin; cytochromes in electron transport chainIron-deficiency anaemia (very common in Nigeria)
Iodine (I⁻)Essential component of thyroxine (thyroid hormone)Goitre; cretinism in children (iodine deficiency common in inland Nigeria)
Sodium (Na⁺)Resting membrane potential; action potential; osmotic balance; pH regulationHyponatraemia: cramps, weakness, seizures
Potassium (K⁺)Resting membrane potential; inside cells; heart rhythm regulationHypokalaemia: muscle weakness, cardiac arrhythmia
Magnesium (Mg²⁺)Cofactor for 300+ enzymes including ATP-dependent reactions; nerve and muscle functionMuscle cramps, anxiety, cardiac issues

2.3 Function of the Liver — Emphasis on Deamination

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Deamination & Urea Synthesis
Removal of amino groups from excess amino acids
Deamination: R–NH₂ + O₂ → R=O (keto acid) + NH₃. The keto acid enters the Krebs cycle for energy. The NH₃ (ammonia) is toxic. Urea cycle (ornithine cycle): NH₃ + CO₂ → carbamoyl phosphate → (via ornithine cycle) → urea → excreted in urine. This is the primary nitrogenous excretory product of mammals.
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Glycogen Storage
Regulates blood glucose homeostasis
After a meal: excess glucose → glycogen (glycogenesis; stimulated by insulin). During fasting: glycogen → glucose (glycogenolysis; stimulated by glucagon). Also: gluconeogenesis — synthesis of new glucose from non-carbohydrate sources (amino acids, lactate, glycerol).
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Bile Production
Emulsifies dietary fats for digestion
Bile is produced in liver cells (hepatocytes) → stored in gall bladder → released into duodenum via bile duct. Contains: bile salts (emulsification), bile pigments (bilirubin, biliverdin — breakdown products of haemoglobin), cholesterol, water. Bile pigments colour faeces and urine.
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Detoxification
Breaks down alcohol, drugs, and hormones
Liver Kupffer cells and hepatic enzymes (cytochrome P450 family) detoxify: alcohol (→ acetaldehyde → acetic acid → acetyl-CoA); drugs (paracetamol, antibiotics); hormones (oestrogen, cortisol). Excessive alcohol overwhelms this system → liver cirrhosis.
Deamination → Urea Cycle — Animated Flow
Amino Acid
R–NH₂ (dietary excess)
Deamination
NH₂ removed in liver
LIVER HEPATOCYTES
Keto Acid
Enters Krebs cycle → energy
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Ammonia (NH₃)
TOXIC — must be converted
Urea Cycle
NH₃ + CO₂ → Urea
ORNITHINE CYCLE
Urea in Blood
→ Kidney → Excreted in urine
📝 Self-Check Quiz — Week 2
Deamination of an amino acid produces two major products. Which are they?
WEEK 03

Enzymes I — Nature, Classification & Naming

Definition · Properties · IUB classes · Systematic naming

Learning Outcomes

  • Define enzyme and list five properties of enzymes
  • Name the six IUB classes of enzymes with one example each
  • Apply the systematic naming convention to given enzyme reactions
  • Distinguish enzyme from inorganic catalyst

3.1 Definition and Properties of Enzymes

An enzyme is a biological catalyst — a protein molecule that speeds up a biochemical reaction without itself being consumed or permanently changed. Enzymes are essential for virtually every metabolic reaction; without them, life chemistry would proceed too slowly to sustain life.

✦ Key Properties of Enzymes
  • Proteinaceous: All enzymes are proteins (with the exception of ribozymes — RNA enzymes). Their 3D shape is essential for function.
  • Specific: Each enzyme catalyses one type of reaction on one type of substrate (or closely related substrates). This is due to the complementary shape of the active site and the substrate.
  • Thermolabile: Sensitive to heat. High temperatures (above ~45°C in most mammalian enzymes) disrupt hydrogen bonds and ionic bonds → protein denaturation → permanent loss of activity.
  • pH-sensitive: Each enzyme has an optimum pH. Extreme pH values disrupt the ionic charges that maintain the active site shape → denaturation.
  • Reusable: Enzymes are not consumed in reactions — they can be used repeatedly. Present in tiny quantities.
  • Reducible activation energy: Enzymes work by lowering the activation energy of a reaction — the minimum energy needed to start the reaction.

3.2 IUB Classification — Six Main Classes

Class (EC number)Reaction TypeExampleLocation
1. OxidoreductasesOxidation-reduction (electron/hydrogen transfer)Lactate dehydrogenase; cytochrome oxidaseMitochondria; cytoplasm
2. TransferasesTransfer of a chemical group from one molecule to anotherTransaminase (aminotransferase); kinases (ATP phosphate transfer)Liver; cytoplasm
3. HydrolasesHydrolysis — cleavage by addition of waterAmylase, lipase, protease, sucrase, lactaseDigestive system; lysosomes
4. LyasesBond cleavage (other than hydrolysis); addition to double bondsCarbonic anhydrase; aldolase (glycolysis)RBCs; cytoplasm
5. IsomerasesIntramolecular rearrangement (isomerisation)Phosphoglucose isomerase; triosephosphate isomeraseCytoplasm (glycolysis)
6. Ligases (Synthetases)Bond formation using ATP energyDNA ligase; pyruvate carboxylase; aminoacyl-tRNA synthetaseNucleus; mitochondria

3.3 Systematic Naming of Enzymes

Enzymes are named by the substrate they act on + the reaction type + the suffix -ase. This gives a systematic name that immediately tells you what the enzyme does:

Systematic NameSubstrateReactionCommon Name
Lactate dehydrogenaseLactateRemoves hydrogen (oxidation)LDH
Sucrose hydrolaseSucroseHydrolysisSucrase / invertase
Glucose oxidaseGlucoseOxidationGOx (used in glucose test strips)
DNA polymerasedNTPs (DNA building blocks)Polymerisation (ligase activity)DNA pol I, II, III
UreaseUreaHydrolysis → NH₃ + CO₂Urease
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Mnemonic: "Oh To Have Lovely Iced Lemon" = Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, Ligases.

📝 Self-Check Quiz — Week 3
The enzyme amylase breaks down starch by adding water to the glycosidic bonds. Which IUB class does amylase belong to?
WEEK 04

Enzymes II — Mechanism, Factors & Coenzymes

Lock-and-key · Induced fit · Temperature · pH · Inhibition · Coenzymes · Prosthetic groups

Learning Outcomes

  • Explain the lock-and-key and induced-fit models of enzyme action
  • Explain how temperature, pH, substrate concentration, and inhibitors affect enzyme activity
  • Distinguish competitive from non-competitive inhibition
  • Define coenzyme and prosthetic group with examples

4.1 Mechanism of Enzyme Action

Proposed by Emil Fischer (1894). The active site of the enzyme has a rigid, fixed shape that is exactly complementary to the shape of the substrate — like a lock and its key. Only the correct substrate can fit.

Mechanism: Substrate (S) → binds to active site → enzyme-substrate complex (ES) → bonds in substrate broken/formed → products (P) released → enzyme (E) available again. E + S → ES → E + P.

  • Strength: Simple; explains specificity well
  • Weakness: Oversimplistic — active sites are not completely rigid

Proposed by Daniel Koshland (1958). The active site is flexible and changes shape when the substrate approaches — moulding around the substrate like a glove fitting a hand. Explains a wider range of enzyme behaviours.

Key difference: In induced fit, binding of the substrate induces a conformational change in the enzyme that precisely positions catalytic residues around the substrate, improving catalytic efficiency.

  • Strength: Explains allosteric regulation, cooperativity, and why some substrates are "competitive"
  • Now the accepted model in biochemistry

4.2 Factors Affecting Enzyme Activity

Temperature and pH Effects on Enzyme Activity Rate
Effect of Temperature Rate of reaction Temperature (°C) 37°C ↑ rate with temperature Denaturation ↓ rate Optimum Effect of pH Rate of reaction pH Pepsin (pH 2) Salivary amylase (pH 7) 1 4 7 10 13
Left: Enzyme activity peaks at the optimum temperature (~37°C in mammals) then falls sharply due to denaturation. Right: Different enzymes have different optimal pH values — pepsin in the acidic stomach, salivary amylase at neutral pH.
FactorEffect on RateExplanation
↑ Temperature (up to optimum)Rate increasesMore kinetic energy → more enzyme-substrate collisions per second
Temperature above optimumRate falls sharply → zeroHeat breaks H-bonds and ionic bonds → protein denaturation → active site loses shape
pH at optimumMaximum rateIonic interactions in active site optimal; substrate binds perfectly
pH away from optimumRate decreasesH⁺/OH⁻ ions disrupt ionic/hydrogen bonds in active site → denaturation
↑ Substrate concentrationRate increases → plateau (Vmax)More substrate fills available active sites; at Vmax all active sites occupied → no further increase
Competitive inhibitorRate decreases; reversible by ↑[S]Inhibitor has similar shape to substrate; competes for active site; can be overcome by increasing substrate
Non-competitive inhibitorRate decreases; NOT reversible by ↑[S]Inhibitor binds allosteric site (not active site); changes enzyme shape → reduces activity regardless of substrate level

4.3 Coenzymes and Prosthetic Groups

TermDefinitionExampleRole
CoenzymeNon-protein organic molecule that loosely associates with an enzyme to assist catalysis; can be removedNAD⁺ (from niacin/Vit B₃); FAD (from riboflavin/Vit B₂); Coenzyme A (from pantothenic acid)NAD⁺/NADH carry hydrogen atoms in cellular respiration; CoA carries acyl groups
Prosthetic groupNon-protein component TIGHTLY (covalently) bound to the enzyme; cannot be removed without destroying enzyme functionHaem group in catalase and peroxidase; FAD in succinate dehydrogenase; biotin in carboxylasesHaem group participates directly in the catalytic reaction (e.g. iron in haem accepts/donates electrons)
ApoenzymeThe protein portion of the enzyme alone (without the cofactor); catalytically inactiveApoenzyme of catalase (without haem)Provides the specific substrate-binding structure
HoloenzymeComplete, catalytically active enzyme = apoenzyme + cofactorCatalase = apoenzyme + haem prosthetic groupFull enzymatic activity
📝 Self-Check Quiz — Week 4
A student adds a competitive inhibitor to an enzyme reaction. Increasing the substrate concentration will:
WEEK 05

Digestive System

Organs · Secretions · Enzymes · Absorption · Role of liver and pancreas

Learning Outcomes

  • Trace the path of food from mouth to anus, naming each organ
  • Name the digestive enzymes secreted at each site and their substrates/products
  • Explain the roles of bile and pancreatic juice in the duodenum
  • Describe absorption in the small intestine

5.1 Gross Anatomy of the Digestive Tract

Mouth
Mechanical digestion + amylase
Pharynx
Swallowing reflex
Oesophagus
Peristalsis; no digestion
Stomach
HCl + pepsin; chyme formed
Duodenum
Bile + pancreatic juice; major digestion
Jejunum/Ileum
Intestinal enzymes; absorption
Large Intestine
Water absorption; faeces formed
Rectum/Anus
Defaecation

5.2 Digestive Enzymes — Complete Summary

SiteSecretion/EnzymeSubstrateProduct
MouthSalivary amylase (ptyalin)Starch (amylose/amylopectin)Maltose + dextrins
StomachPepsin (from pepsinogen, activated by HCl)ProteinsPeptides (polypeptides)
StomachHCl (from parietal cells)Denatures proteins; kills bacteria; activates pepsinogen → pepsinAcidic environment (pH ~2)
StomachGastric lipaseTriglycerides (minor contribution)Fatty acids + glycerol
DuodenumBile salts (from liver/gall bladder)Lipid droplets (emulsification)Lipid micelles (↑ surface area for lipase)
DuodenumPancreatic amylaseStarch (remaining)Maltose
DuodenumPancreatic lipaseTriglyceridesFatty acids + monoglycerides
DuodenumTrypsin + chymotrypsin (from trypsinogen)Proteins and peptidesShorter peptides
DuodenumPancreatic nucleasesDNA, RNANucleotides
Small intestineMaltase, sucrase, lactaseMaltose, sucrose, lactoseGlucose, fructose, galactose (monosaccharides)
Small intestinePeptidases (dipeptidases, aminopeptidases)Dipeptides, oligopeptidesAmino acids

5.3 Absorption in the Small Intestine

The small intestine (ileum) is the primary site of nutrient absorption. Three structural adaptations maximise surface area: circular folds (plicae circulares), villi (finger-like projections), and microvilli (brush border on each villus cell) — together increasing area ~600× compared to a smooth tube.

📥 Absorption Routes
  • Monosaccharides and amino acids: Active transport into villus epithelial cells → capillaries in villus → hepatic portal vein → liver
  • Fatty acids and glycerol: Diffuse into epithelial cells → re-synthesised into triglycerides → packaged into chylomicrons → enter lacteals (lymph capillaries) → lymphatic system → thoracic duct → bloodstream (bypasses liver initially)
  • Fat-soluble vitamins (A, D, E, K): Absorbed with fats via lacteals
  • Water and minerals: Absorbed throughout small and large intestine
📝 Self-Check Quiz — Week 5
Bile does NOT contain digestive enzymes, yet it is essential for fat digestion. What is bile's precise role?
WEEK 06

Circulatory System I — Heart & Blood Vessels

Heart chambers · Cardiac cycle · SA node · Autonomic control · Blood pressure

Learning Outcomes

  • Describe the four chambers of the mammalian heart and their functions
  • Explain the cardiac cycle including systole and diastole
  • Describe the conduction system of the heart (SA node to Purkinje fibres)
  • Explain nervous and hormonal control of heart rate

6.1 Mammalian Heart — Structure and Double Circulation

Mammalian Heart — Four Chambers and Blood Flow
RIGHT SIDE (receives deoxygenated blood) Right Atrium Receives blood from superior + inferior vena cava ▼ TRICUSPID VALVE ▼ Right Ventricle Pumps blood to LUNGS (pulmonary artery) Pulmonary artery → LEFT SIDE (receives oxygenated blood) Left Atrium Receives blood from 4 pulmonary veins (from lungs) ▼ BICUSPID (MITRAL) VALVE ▼ Left Ventricle Thickest wall; pumps blood to BODY (aorta) → Aorta → Body SEPTUM Via lungs
The heart has two separate pumps separated by the interventricular septum. Right side handles pulmonary circulation (deoxygenated blood to lungs). Left side handles systemic circulation (oxygenated blood to body). Left ventricle wall is ~3× thicker than right — pumps blood much further.

6.2 Cardiac Conduction System

StructureLocationRole
SA Node (Sinoatrial)Right atrium wall"Pacemaker" — generates electrical impulse spontaneously (~70/min at rest); initiates each heartbeat
AV Node (Atrioventricular)Base of right atriumReceives impulse from SA node; delays it (~0.1 sec) allowing atria to finish contracting before ventricles
Bundle of HisInterventricular septumTransmits impulse from AV node down the septum to ventricular walls
Purkinje FibresVentricular wallsRapidly spread impulse through ventricular muscle → simultaneous ventricular contraction from apex upward
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Control of heart rate: Sympathetic nerves + adrenaline → INCREASE rate (in exercise, fear, fever). Vagus nerve (parasympathetic) → DECREASE rate (at rest, during relaxation). Blood O₂/CO₂ levels detected by chemoreceptors also modulate rate.

📝 Self-Check Quiz — Week 6
Why is the wall of the left ventricle approximately three times thicker than the wall of the right ventricle?
WEEK 07

Circulatory System II — Blood, Clotting & Transfusion

Blood components · Clotting cascade · ABO groups · AIDS · Blood screening

Learning Outcomes

  • Describe the structure and function of each blood component
  • Explain the blood clotting mechanism step by step
  • Explain ABO and Rh blood groups and their clinical importance
  • Describe HIV/AIDS and the importance of blood screening in Nigeria

7.1 Blood Components and Functions

Component% of BloodStructureFunctions
Red Blood Cells (Erythrocytes)~45%Biconcave disc; no nucleus; diameter ~8 μm; contains ~280 million haemoglobin moleculesO₂ transport (oxyhaemoglobin); CO₂ transport; buffering blood pH
White Blood Cells (Leukocytes)~1%Nucleated; 5 types: neutrophils (most common), lymphocytes (T and B cells), monocytes, eosinophils, basophilsImmunity: phagocytosis (neutrophils, monocytes); antibody production (B lymphocytes); cell-mediated immunity (T lymphocytes)
Platelets (Thrombocytes)~1%Cell fragments; no nucleus; formed from megakaryocytes; 150–400 × 10⁹/LBlood clotting (haemostasis); release clotting factors; plug small wounds
Plasma~55%Liquid matrix: 90% water + plasma proteins (albumin, globulins, fibrinogen) + ions + glucose + hormones + wastesTransport of all blood components; osmotic balance; immune proteins; clotting proteins; hormone transport

7.2 Blood Clotting Cascade

Injury
Blood vessel damaged
Platelet Plug
Platelets aggregate; release thromboplastin
Prothrombin Activator
Thromboplastin + Ca²⁺ + clotting factors
Thrombin
Prothrombin → Thrombin (active serine protease)
Fibrin Net
Fibrinogen (soluble) → Fibrin (insoluble threads)
Blood Clot
Fibrin traps RBCs + platelets → wound sealed
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Clotting disorders in Nigeria: Haemophilia A (factor VIII deficiency) — X-linked; males affected. Sickle-cell disease — altered Hb leads to RBC sickling, haemolytic anaemia, vaso-occlusive crises. Vitamin K deficiency impairs synthesis of clotting factors II, VII, IX, X.

7.3 Blood Groups, AIDS, and Screening

Blood GroupAntigen on RBCAntibody in PlasmaCan Donate ToCan Receive From
AA antigenAnti-B antibodyA, ABA, O
BB antigenAnti-A antibodyB, ABB, O
ABA and B antigensNo antibodiesAB onlyA, B, AB, O (Universal recipient)
ONo A or B antigenAnti-A and Anti-BA, B, AB, O (Universal donor — Rh−)O only
🩸 Blood Screening Importance in Nigeria
  • HIV: Mandatory; window period of 3 months where ELISA may give false negative — modern NAT (nucleic acid test) reduces window to 10–14 days
  • Hepatitis B and C: Very high prevalence in Nigeria (~10–15% HBV); major cause of liver cirrhosis and hepatocellular carcinoma
  • Malaria: Plasmodium can be transmitted by blood transfusion; screening by thick blood film or RDT
  • Sickle-cell trait: Screening prevents transfusion of sickle-cell trait blood
  • Leukaemia detection: Differential WBC count reveals abnormal proportions of blast cells
  • Cancer markers: PSA (prostate), CA-125 (ovarian), AFP (liver) detected in blood
📝 Self-Check Quiz — Week 7
A patient with blood group B receives group A blood in error. What will happen and why?
WEEK 08

Mid-Semester Review

Synthesis of Weeks 1–7 · Comparative summary · Practice questions

Review Focus

  • Integrate all content from introduction through circulatory system
  • Practise examination-style questions across all topics

8.1 Synthesis Summary

TopicKey Point 1Key Point 2
OrganisationChemical → Cellular → Tissue → Organ → System → OrganismFour tissue types: epithelial, connective, muscular, nervous
Nutrition6 food classes: carbohydrates, proteins, lipids, vitamins, minerals, waterDeamination in liver: R–NH₂ → keto acid + NH₃ → urea (ornithine cycle)
Enzymes6 IUB classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligasesLock-and-key vs. induced-fit; competitive vs. non-competitive inhibition
DigestionAmylase → starch; pepsin → protein; lipase → fats; specific enzyme at each siteBile emulsifies fat; absorption via villi/microvilli; fats via lacteals
CirculationSA node → AV node → Bundle of His → Purkinje fibres; double circulationBlood components; clotting cascade; ABO groups; blood screening

8.2 Practice Questions

📝 Attempt Before Continuing
  • Distinguish anatomy from physiology. Why are they studied together?
  • Name the six classes of food with their functions. Which class provides the most energy per gram?
  • Explain why increasing temperature above 40°C destroys enzyme activity.
  • Trace a molecule of starch from the mouth to absorption in the ileum, naming every enzyme involved.
  • Why does the left ventricle have a thicker wall than the right ventricle?
  • Explain the blood clotting cascade in five steps.
  • Why is blood screening especially important in Nigeria?
📝 Review Quiz — Week 8
Which of the following correctly describes a NON-competitive enzyme inhibitor?
WEEK 09

Respiratory System

Breathing mechanism · Aerobic/Anaerobic respiration · Glycolysis · Krebs cycle · Significance

Learning Outcomes

  • Describe the structure of the respiratory system and alveoli
  • Explain the mechanics of inhalation and exhalation
  • Trace glucose through glycolysis, the link reaction, the Krebs cycle, and oxidative phosphorylation
  • Compare aerobic and anaerobic respiration; state the significance of respiration

9.1 Respiratory Anatomy

StructureFunction
Nostrils and nasal cavityFilters (nasal hairs, mucus), warms, and humidifies air; olfaction
PharynxCommon passage for air and food; contains tonsils
LarynxVoice box; contains vocal cords; epiglottis closes during swallowing
TracheaC-shaped cartilage rings maintain patency; ciliated epithelium moves mucus upward
Bronchi (primary)Two main airways to left and right lungs
BronchiolesSmall airways without cartilage; smooth muscle allows vasoconstriction in asthma
AlveoliGas exchange; ~300 million per lung; ~70 m² total surface area; one cell thick; rich capillary network; moist surface

9.2 Mechanism of Breathing

Active process. Diaphragm contracts → flattens (moves inferiorly). External intercostal muscles contract → ribs move up and outward. Result: thoracic cavity volume increases → intrathoracic pressure drops below atmospheric pressure (approx. −2 to −3 mmHg) → pressure gradient drives air into lungs.

Passive process at rest (active during exercise). Diaphragm relaxes → domes upward. Internal intercostal muscles and gravity pull ribs downward and inward. Result: thoracic cavity volume decreases → intrathoracic pressure rises above atmospheric → air pushed out of lungs. During forced expiration: abdominal muscles assist.

9.3 Aerobic Respiration — Stage by Stage

Glucose (C₆H₁₂O₆)
Starting material
Glycolysis
Glucose → 2 Pyruvate + 2 ATP + 2 NADH
CYTOPLASM
Link Reaction
Pyruvate → Acetyl-CoA + CO₂ + NADH
MITOCHONDRIAL MATRIX
Krebs Cycle
Acetyl-CoA → 2CO₂ + 3NADH + FADH₂ + ATP (×2 turns)
MITOCHONDRIAL MATRIX
Oxidative Phosphorylation
NADH/FADH₂ → Electron transport → 34 ATP; O₂ → H₂O
INNER MITOCHONDRIAL MEMBRANE
Total: 38 ATP
+ 6CO₂ + 6H₂O
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Anaerobic respiration: In muscle (no O₂): Glucose → 2 Lactic acid + 2 ATP. Lactic acid accumulates → muscle fatigue; repaid during recovery (oxygen debt). In yeast: Glucose → 2 Ethanol + 2 CO₂ + 2 ATP. Anaerobic yields only 2 ATP vs. 38 ATP in aerobic — 19× less efficient.

📝 Self-Check Quiz — Week 9
Which part of aerobic respiration produces the MOST ATP per glucose molecule?
WEEK 10

Excretory System

Organs of excretion · Kidney nephron · Ultrafiltration · Nitrogenous wastes

Learning Outcomes

  • State the need for excretion and name the major metabolic wastes
  • Describe the structure and function of each excretory organ
  • Trace filtrate through a kidney nephron (ultrafiltration → selective reabsorption → secretion)
  • Distinguish nitrogenous excretion from gaseous excretion

10.1 Why Excretion is Necessary

Excretion is the removal of metabolic waste products from the body. Unlike egestion (removal of undigested food in faeces — these are not metabolic waste), excretion involves the elimination of substances produced by the body's own metabolic reactions. Failure to excrete these wastes causes metabolic poisoning: ammonia causes liver encephalopathy; CO₂ excess causes respiratory acidosis; urea excess causes uraemia.

Waste ProductOriginExcretory Organ
Carbon dioxide (CO₂)Aerobic respiration in all cellsLungs (gaseous excretion)
Water (H₂O)Aerobic respiration; metabolic reactionsLungs, skin, kidneys
Urea (NH₂–CO–NH₂)Deamination of amino acids in liverKidneys (primary nitrogenous excretion in mammals)
Salts (NaCl, KCl, etc.)Excess dietary saltsKidneys, skin (sweat)
Bile pigments (bilirubin)Breakdown of haemoglobin in liverLiver → bile → faeces; some via kidneys → urine (urobilinogen)
CreatinineBreakdown of creatine phosphate in muscleKidneys

10.2 The Kidney Nephron

🔬 Three Processes in the Nephron
  • Ultrafiltration (Bowman's capsule/glomerulus): High blood pressure in glomerular capillaries forces small molecules (water, glucose, amino acids, urea, salts, creatinine) through the filtration membrane into Bowman's space. Large molecules (proteins, blood cells) remain in blood. ~180 litres of filtrate formed per day.
  • Selective reabsorption (PCT, loop of Henle, DCT): Useful molecules reabsorbed back into blood. PCT: glucose, amino acids, most water, Na⁺ actively reabsorbed (all glucose reabsorbed normally). Loop of Henle: creates osmotic gradient in medulla; descending limb permeable to water; ascending limb pumps out NaCl. DCT: fine-tuning of Na⁺/K⁺ and water under aldosterone/ADH control.
  • Tubular secretion (DCT and collecting duct): H⁺ ions, NH₄⁺, K⁺, some drugs (penicillin, creatinine) secreted from blood into tubular fluid — actively pumped across tubular wall against concentration gradient.
🇳🇬

Kidney disease in Nigeria: Hypertension (very prevalent) and diabetes mellitus (rising) are the two leading causes of chronic kidney disease in Nigeria. Early detection by urine protein (dipstick) and serum creatinine testing is essential.

📝 Self-Check Quiz — Week 10
A healthy person produces 180 litres of glomerular filtrate per day but only ~1.5 litres of urine. This means approximately how much water is reabsorbed by the kidney tubules?
WEEK 11

Nervous System I — Neuron, Impulse & Synapse

Neuron structure · Resting potential · Action potential · Synaptic transmission · Reflex arc

Learning Outcomes

  • Describe the structure and types of neurons
  • Explain the resting membrane potential and how an action potential is generated
  • Describe synaptic transmission including the role of neurotransmitters
  • Trace the pathway of a reflex arc and give an example

11.1 Neuron Structure

Motor Neuron — Annotated Structure
Dendrites Receive signals Nucleus Cell Body (Soma) Axon hillock (action potential initiated here) Node of Ranvier Myelin sheath (Schwann cells) insulates axon; speeds saltatory conduction Axon terminals (synaptic knobs) → synapse
The myelin sheath (made by Schwann cells in PNS) insulates the axon and allows saltatory conduction — impulse "jumps" from node to node reaching speeds of 70–120 m/s. Unmyelinated fibres conduct at only ~1 m/s.

11.2 Action Potential

PhaseIon MovementMembrane Potential
Resting potentialK⁺ inside; Na⁺ outside (maintained by Na⁺/K⁺ ATPase pump)−70 mV (inside negative)
DepolarisationVoltage-gated Na⁺ channels open; Na⁺ rushes INTO cellRises rapidly to +40 mV
RepolarisationNa⁺ channels close; voltage-gated K⁺ channels open; K⁺ rushes OUTFalls back toward −70 mV
HyperpolarisationK⁺ channels slow to close; brief overshootDrops slightly below −70 mV
Refractory periodNa⁺/K⁺ pump restores ion distribution; Na⁺ channels in absolute refractory stateReturns to −70 mV; no new AP possible briefly

11.3 Synaptic Transmission & Reflex Arc

⚡ Synaptic Transmission Steps
  • Action potential arrives at pre-synaptic axon terminal
  • Voltage-gated Ca²⁺ channels open → Ca²⁺ flows into terminal
  • Ca²⁺ triggers synaptic vesicles to fuse with pre-synaptic membrane → exocytosis of neurotransmitter (e.g. acetylcholine)
  • Neurotransmitter diffuses across synaptic cleft (~20 nm)
  • Binds to receptors on post-synaptic membrane → ion channels open → new action potential (excitatory) or hyperpolarisation (inhibitory)
  • Neurotransmitter removed: by enzyme breakdown (acetylcholinesterase breaks ACh) or reuptake into pre-synaptic terminal
🔄 Reflex Arc Pathway
  • Receptor detects stimulus (e.g. skin pain receptor)
  • Sensory (afferent) neuron transmits impulse to spinal cord
  • Relay (interneuron) in posterior horn of spinal cord processes and relays
  • Motor (efferent) neuron transmits impulse from spinal cord to effector
  • Effector (muscle contracts / gland secretes) → response
  • Signal also travels up spinal cord to brain — consciousness is aware AFTER the reflex occurs
📝 Self-Check Quiz — Week 11
During an action potential, what causes the membrane potential to rise from −70 mV to +40 mV (depolarisation)?
WEEK 12

Nervous System II — CNS, PNS & Sense Organs

Brain regions · Autonomic NS · Eye · Ear · Skin · Taste · Smell

Learning Outcomes

  • Name the major brain regions and their functions
  • Distinguish sympathetic from parasympathetic nervous systems
  • Describe the structure and function of the eye, ear, skin, tongue, and nose as sense organs

12.1 Brain Regions and Functions

Brain RegionLocationFunctions
Cerebrum (cerebral cortex)Largest; two hemispheres; anteriorVoluntary movement, thought, memory, language, consciousness, sensory interpretation, personality
CerebellumPosterior, inferiorBalance, coordination, fine motor control, muscle tone; damage → ataxia
Medulla oblongataInferior brainstemVital centres: respiratory rhythm, heart rate, blood pressure, swallowing, vomiting, coughing; cranial nerves IX–XII
HypothalamusFloor of diencephalonThermoregulation (body temperature set point), hunger/satiety, thirst, sleep-wake cycle, controls pituitary gland (master of endocrine system)
ThalamusCentral diencephalonSensory relay station — all sensory input (except olfaction) passes through thalamus before reaching cortex
PonsBrainstem, between medulla and midbrainRelay between cerebrum and cerebellum; breathing centres; cranial nerves V–VIII

12.2 Sympathetic vs. Parasympathetic

FeatureSympatheticParasympathetic
Activation stateFight-or-flight; exercise; stress; emergencyRest-and-digest; sleep; recovery
Heart rate↑ Increases↓ Decreases (vagus nerve)
PupilsDilated (mydriasis)Constricted (miosis)
BronchiolesDilated (bronchodilation) — more O₂Constricted (bronchoconstriction)
Digestive systemInhibited (peristalsis slows, sphincters close)Stimulated (peristalsis increases, digestive glands active)
NeurotransmitterNoradrenaline at target organsAcetylcholine at target organs

12.3 Sense Organs Summary

Sense OrganStimulusReceptor CellsKey Structures / Pathway
EyeLight (photons 380–750 nm)Rods (dim light, b&w, rhodopsin); Cones (colour, iodopsin — 3 types)Cornea (refraction) → aqueous humour → iris/pupil → lens (accommodation by ciliary muscles) → vitreous humour → retina → fovea (highest acuity) → optic nerve → visual cortex
EarSound waves; gravity/rotation (vestibular)Hair cells in Organ of Corti (hearing); hair cells in semicircular canals/utricle/saccule (balance)Pinna → ear canal → tympanum → 3 ossicles (malleus, incus, stapes) → oval window → cochlea (perilymph → endolymph waves → hair cell bending → impulse) → auditory nerve → auditory cortex
SkinTouch, pressure, temperature, pain, vibrationMeissner's (light touch); Pacinian (deep pressure/vibration); Merkel's (sustained touch); Ruffini (skin stretch); free nerve endings (pain/temperature)Stimulation → sensory neuron → spinal cord → thalamus → somatosensory cortex
TongueChemical (taste = gustation)Taste receptor cells in taste buds (on papillae)5 basic tastes: sweet (sugars), sour (H⁺), salty (Na⁺), bitter (alkaloids), umami (glutamate/protein). 3 cranial nerves carry taste: VII (anterior 2/3), IX (posterior 1/3), X (epiglottis)
NoseChemical (smell = olfaction)Olfactory receptor neurons (bipolar neurons) in olfactory epithelium (roof of nasal cavity)Volatile chemicals → olfactory receptor proteins → olfactory nerve (CN I) → olfactory bulb → olfactory cortex + limbic system (explains strong emotion-smell link)
📝 Self-Check Quiz — Week 12
During an emergency, a student hears a gunshot. Their heart races, pupils dilate, and digestion slows. Which division of the autonomic nervous system is active?
WEEK 13

Skeletal System & Muscular Contraction

Skeleton functions · Axial/Appendicular · Joints · Sliding filament theory

Learning Outcomes

  • State five functions of the mammalian skeleton
  • Distinguish axial from appendicular skeleton
  • Classify joints and give examples
  • Explain the sliding filament theory of muscular contraction step by step

13.1 Functions of the Skeleton

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Support
Maintains body shape against gravity
The skeleton is the body's scaffold. Without it, soft tissues would collapse. Upright posture requires the vertebral column (spine) as a central pillar, while limb bones bear body weight during standing and locomotion.
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Protection
Shields vital organs from damage
Skull protects the brain. Rib cage and sternum protect the heart and lungs. Vertebrae protect the spinal cord. Pelvic girdle protects bladder, rectum, and reproductive organs.
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Movement
Bones as levers for muscles
Muscles attach to bones via tendons. Bones act as levers; joints as fulcrums. When muscles contract, they pull on bones, producing movement. Without bone, muscles would contract without producing useful movement.
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Blood Cell Production
Red bone marrow generates all blood cells
Red bone marrow in flat bones (sternum, ribs, vertebrae, pelvis) and epiphyses of long bones produces: red blood cells (erythropoiesis), white blood cells (leukopoiesis), and platelets (thrombopoiesis) — all from pluripotent stem cells.

13.2 Sliding Filament Theory of Muscular Contraction

The sliding filament theory (Hanson and Huxley, 1954) explains how sarcomeres shorten during muscle contraction. Actin (thin) filaments slide over myosin (thick) filaments — the filaments themselves do not shorten, but the sarcomere (and thus the muscle) shortens.

Nerve impulse arrives
ACh released at neuromuscular junction
Action potential across sarcolemma
Spreads into T-tubules
Ca²⁺ released
From sarcoplasmic reticulum into cytoplasm
Ca²⁺ binds Troponin
Tropomyosin moves → actin binding sites exposed
Myosin heads bind actin
Cross-bridge formation
Power stroke
Myosin head pivots → actin slides → sarcomere shortens
ATP binds myosin
Cross-bridge detaches; cycle repeats
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Rigor mortis occurs because after death, ATP is depleted — myosin heads remain bound to actin (no ATP to detach cross-bridges) → muscles stiffen. This resolves after ~24–48 hours as muscle proteins degrade.

📝 Self-Check Quiz — Week 13
In the sliding filament theory, what is the role of calcium ions (Ca²⁺) released from the sarcoplasmic reticulum?
WEEK 14

Endocrine System & Hormones

Pituitary tropic hormones · Thyroxine · Adrenaline · Reproductive hormones · Insulin

Learning Outcomes

  • Define hormone and state five properties of hormones
  • Name the pituitary hormones, their targets, and effects
  • Describe the effects of thyroxine, adrenaline, and insulin/glucagon
  • Name the reproductive hormones and their effects

14.1 Properties and Definition of Hormones

A hormone is a chemical messenger secreted by an endocrine gland directly into the bloodstream, transported to a target organ, where it produces a specific physiological effect. The endocrine system and nervous system together maintain homeostasis — the nervous system acts quickly (milliseconds) but briefly; the endocrine system acts slowly (minutes to hours) but with prolonged effects.

✦ Properties of Hormones
  • Secreted by specialised endocrine (ductless) glands directly into blood
  • Transported in blood to target organs — may travel long distances
  • Effective in very small (nanomolar) concentrations
  • Specific — act only on cells bearing complementary receptors for that hormone
  • Slow-acting but long-lasting compared to nerve impulses
  • Chemical nature: protein/peptide (water-soluble, bind surface receptors) OR steroid (lipid-soluble, enter cell and bind nuclear receptors → gene regulation)

14.2 Pituitary Gland — The Master Gland

HormoneTargetEffect / Deficiency / Excess
GH (Growth Hormone)Liver, bone, muscle↑ Protein synthesis, bone growth; deficiency: pituitary dwarfism; excess in childhood: gigantism; excess in adult: acromegaly
TSH (Thyroid-Stimulating H.)Thyroid glandStimulates thyroxine synthesis and secretion
ACTH (Adrenocorticotropic H.)Adrenal cortexStimulates cortisol secretion; stress response
FSH (Follicle-Stimulating H.)Ovary / TestisFemale: stimulates follicle development and oestrogen secretion. Male: stimulates spermatogenesis
LH (Luteinising H.)Ovary / TestisFemale: triggers ovulation (LH surge), forms corpus luteum. Male: stimulates testosterone secretion from Leydig cells
ADH (Antidiuretic H.)Kidney collecting ducts↑ Water reabsorption → concentrated urine; deficiency: diabetes insipidus (large volumes of dilute urine)
OxytocinUterus, mammary glandsUterine contractions during labour; milk ejection reflex (positive feedback)
ProlactinMammary glandsStimulates milk production (lactation) after childbirth

14.3 Key Hormones — Thyroxine, Adrenaline, Insulin, Reproductive

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Thyroxine (T₄)
Thyroid gland; requires dietary iodine
Effects: increases basal metabolic rate (BMR); essential for normal brain development in foetus and young child; stimulates protein synthesis and bone growth. Deficiency: goitre (enlarged thyroid — iodine deficiency, common in non-coastal Nigeria); cretinism in children (severe mental retardation, stunted growth); myxoedema in adults. Excess: hyperthyroidism (Graves' disease) — weight loss, rapid heart rate, exophthalmos.
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Adrenaline (Epinephrine)
Adrenal medulla; fight-or-flight
Released in seconds during stress or exercise. Effects: ↑ heart rate and cardiac output; ↑ blood glucose (glycogenolysis in liver); bronchodilation; pupil dilation; vasoconstriction in skin/gut; vasodilation in muscle. Clinical use: anaphylaxis treatment (EpiPen); cardiac arrest; bronchospasm (asthma).
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Insulin & Glucagon
Pancreatic islets of Langerhans
Insulin (β cells): released when blood glucose ↑ after a meal; stimulates glucose uptake by cells (especially muscle/fat); promotes glycogenesis (glucose → glycogen); inhibits gluconeogenesis. Deficiency: Type 1 diabetes. Resistance: Type 2 diabetes (very common in Nigeria). Glucagon (α cells): released when blood glucose ↓ (fasting); stimulates glycogenolysis (glycogen → glucose) and gluconeogenesis in liver.
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Reproductive Hormones
Testosterone · Oestrogen · Progesterone
Testosterone (testes/Leydig cells): male secondary sex characteristics (deepened voice, body hair, muscle mass); drives spermatogenesis; anabolic steroid. Oestrogen (ovary/follicle cells): female secondary sex characteristics; thickens endometrium; regulates menstrual cycle. Progesterone (corpus luteum/placenta): maintains endometrial lining; inhibits further ovulation during pregnancy; prepares mammary glands for lactation.
📝 Self-Check Quiz — Week 14
Iodine deficiency causes goitre in Nigeria. Which hormone requires iodine for its synthesis, and what would be the effect of insufficient iodine on TSH levels?
WEEK 15

Reproductive System, Fertilisation & Course Synthesis

Male/female anatomy · Fertilisation · Gestation · Birth · Menstrual cycle

Learning Outcomes

  • Describe the structure and function of the male and female reproductive systems in mammals
  • Trace the process of fertilisation, implantation, and gestation
  • Explain the events of childbirth (parturition)
  • Describe the hormonal control of the menstrual cycle

15.1 Male Reproductive System

StructureFunction
Testes (in scrotum, ~2°C below body temperature)Produce spermatozoa (spermatogenesis) and testosterone
EpididymisSite of sperm maturation and storage (~3 weeks)
Vas deferensTransports sperm from epididymis to ejaculatory duct
Seminal vesiclesSecrete fructose (sperm energy), prostaglandins, and alkaline fluid (~60% of semen volume)
Prostate glandSecretes alkaline fluid that neutralises vaginal acidity; contains enzymes that liquefy semen
Bulbourethral (Cowper's) glandsPre-ejaculatory lubricating fluid; neutralises residual urine acidity in urethra
Urethra / PenisCommon passage for urine and semen; sexual intercourse and ejaculation

15.2 Female Reproductive System

StructureFunction
Ovaries (two, in pelvic cavity)Produce ova (oogenesis) and sex hormones (oestrogen, progesterone)
Fallopian tubes (oviducts)Transport ovum from ovary to uterus; site of fertilisation (usually at ampulla)
UterusSite of implantation and foetal development; muscular wall (myometrium) contracts during birth; inner lining = endometrium (shed during menstruation)
CervixLower narrow part of uterus; normally closed; dilates during birth; secretes mucus (thick mid-cycle, watery at ovulation)
VaginaBirth canal; receives penis during intercourse; acidic environment (pH 3.5–4.5) prevents infection

15.3 Fertilisation, Gestation, and Birth

Ovulation
LH surge releases secondary oocyte
DAY 14 of cycle
Fertilisation
Sperm penetrates oocyte in fallopian tube; acrosome reaction; cortical reaction prevents polyspermy
FALLOPIAN TUBE (AMPULLA)
Cleavage
Zygote → 2-cell → 4-cell → morula (16-cell)
DAYS 1–4
Blastocyst
Hollow ball; inner cell mass (embryo) + trophoblast (placenta)
DAYS 4–6
Implantation
Blastocyst embeds in endometrium; placenta begins forming
DAYS 6–10
Gestation (~38 wks)
Embryo → foetus; placenta exchanges O₂/nutrients/wastes; progesterone maintains pregnancy
Parturition (Birth)
Oxytocin → uterine contractions (positive feedback) → cervix dilates → delivery → placenta expelled

15.4 The Menstrual Cycle (~28 days)

📅 Four Phases of the Menstrual Cycle
  • Days 1–5 — Menstruation: Corpus luteum degenerates → progesterone and oestrogen fall → endometrium sheds → menstrual flow. FSH begins to rise.
  • Days 6–13 — Follicular Phase: FSH stimulates follicle growth in ovary → follicle secretes increasing oestrogen → endometrium rebuilds (proliferative phase). Oestrogen rises sharply by Day 12–13.
  • Day 14 — Ovulation: High oestrogen triggers LH surge from anterior pituitary → mature Graafian follicle ruptures → secondary oocyte released into fallopian tube.
  • Days 15–28 — Luteal Phase: Ruptured follicle → corpus luteum → secretes progesterone (and oestrogen) → endometrium thickens further (secretory phase, preparing for implantation). If no fertilisation: corpus luteum degenerates Day 24–26 → hormone levels fall → menstruation begins (Day 1 of next cycle).

15.5 Course Synthesis — All 12 Systems Integrated

SystemKey ConceptClinical Importance (Nigeria)
DigestiveHydrolytic enzymes at each site; bile emulsifies fats; absorption via villiMalnutrition; diarrhoeal disease; food contamination
CirculatoryDouble circulation; cardiac conduction; ABO groups; clotting cascadeHypertension; sickle-cell disease; HIV transmission via blood
RespiratoryAlveolar exchange; aerobic respiration; 38 ATP per glucoseAsthma; TB; COVID-19 respiratory complications
ExcretoryUltrafiltration → selective reabsorption → secretion; deamination → ureaKidney disease (hypertension + diabetes driven); malaria-related nephrotic syndrome
NervousAction potential; synaptic transmission; reflex arc; brain regionsEpilepsy (neurocysticercosis); stroke; meningitis
Skeletal/MuscularSliding filament; levers; red bone marrow; joint typesRickets (Vit D/Ca deficiency); fractures; sickle-cell bone pain
EndocrinePituitary tropic hormones; thyroxine; adrenaline; insulinGoitre (iodine deficiency); Type 2 diabetes (rising epidemic)
ReproductiveMale/female anatomy; fertilisation; gestation; menstrual cycleMaternal mortality; antenatal care; family planning
📝 Final Review Quiz — Week 15
A pregnant woman is told she has severe pre-eclampsia. Her blood pressure is very high, her kidneys are leaking protein into urine, and she develops seizures. Which endocrine connection explains why oxytocin is used to induce labour in her management?
COURSE COMPLETE
Congratulations!

You have completed BIO 222 — from enzyme kinetics to childbirth, from the action potential to the Krebs cycle. Structure and function are inseparable. Use this knowledge well in your teaching.