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Physiology - NEETMDS- courses
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Physiology

The Parathyroid Glands

The parathyroid glands are 4 tiny structures embedded in the rear surface of the thyroid gland. They secrete parathyroid hormone (PTH) a polypeptide of 84 amino acids. PTH increases the concentration of Ca2+ in the blood in three ways. PTH promotes

  • release of Ca2+ from the huge reservoir in the bones. (99% of the calcium in the body is incorporated in our bones.)
  • reabsorption of Ca2+ from the fluid in the tubules in the kidneys
  • absorption of Ca2+ from the contents of the intestine (this action is mediated by calcitriol, the active form of vitamin D.)

PTH also regulates the level of phosphate in the blood. Secretion of PTH reduces the efficiency with which phosphate is reclaimed in the proximal tubules of the kidney causing a drop in the phosphate concentration of the blood.

Hyperparathyroidism

Elevate the level of PTH causing a rise in the level of blood Ca2+ .Calcium may be withdrawn from the bones that they become brittle and break.

 Patients with this disorder have high levels of Ca2+ in their blood and excrete small amounts of Ca2+ in their urine. This causes hyperparathyroidism.

Hypoparathyroidism

This disorder have low levels of Ca2+ in their blood and excrete large amounts of Ca2+ in their urine.

HEART DISORDERS

  1. Pump failure => Alters pressure (flow) =>alters oxygen carrying capacity.
    1. Renin release (Juxtaglomerular cells) Kidney
    2. Converts Angiotensinogen => Angiotensin I
    3. In lungs Angiotensin I Converted => Angiotensin II
    4. Angiotensin II = powerful vasoconstrictor (raises pressure, increases afterload)
      1. stimulates thirst
      2. stimulates adrenal cortex to release Aldosterone
        (Sodium retention, potassium loss)
      3. stimulates kidney directly to reabsorb Sodium
      4. releases ADH from Posterior Pituitary
  2. Myocardial Infarction

     

    1. Myocardial Cells die from lack of Oxygen
    2. Adjacent vessels (collateral) dilate to compensate
    3. Intracellular Enzymes leak from dying cells (Necrosis)
      1. Creatine Kinase CK (Creatine Phosphokinase) 3 forms
        1. One isoenzyme = exclusively Heart (MB)
        2. CK-MB blood levels found 2-5 hrs, peak in 24 hrs
        3. Lactic Dehydrogenase found 6-10 hours after. points less clearly to infarction
      2. Serum glutamic oxaloacetic transaminase (SGOT)
        1. Found 6 hrs after infarction, peaks 24-48 hrs at 2 to 15 times normal,
        2. SGOT returns to normal after 3-4 days
    4. Myocardium weakens = Decreased CO & SV (severe - death)
    5. Infarct heal by fibrous repair
    6. Hypertrophy of undamaged myocardial cells
      1. Increased contractility to restore normal CO
      2. Improved by exercise program
    7. Prognosis
      1. 10% uncomplicated recovery
      2. 20% Suddenly fatal
      3. Rest MI not fatal immediately, 15% will die from related causes
  3. Congenital heart disease (Affect oxygenation of blood)
    1. Septal defects
    2. Ductus arteriosus
    3. Valvular heart disease
      1. Stenosis = cusps, fibrotic & thickened, Sometimes fused, can not open
      2. Regurgitation = cusps, retracted, Do not close, blood moves backwards

Membrane Structure & Function

Cell Membranes

  • Cell membranes are phospholipid bilayers (2 layers)
  • Bilayer forms a barrier to passage of molecules in an out of cell
  • Phospholipids = glycerol + 2 fatty acids + polar molecule (i.e., choline) + phosphate
  • Cholesterol (another lipid) stabilizes cell membranes
  • the hydrophobic tails of the phospholipids (fatty acids) are together in the center of the bilayer. This keeps them out of the water

Membranes Also Contain Proteins

  • Proteins that penetrate the membrane have hydrophobic sections ~25 amino acids long
  • Hydrophobic = doesn't like water = likes lipids
  • Membrane proteins have many functions:
    • receptors for hormones
    • pumps for transporting materials across the membrane
    • ion channels
    • adhesion molecules for holding cells to extracellular matrix

cell recognition antigens

Structure and function of skeletal muscle.

Skeletal muscles have a belly which contains the cells and which attaches by means of tendons or aponeuroses to a bone or other tissue. An aponeurosis is a broad, flat, tendinous attachment, usually along the edge of a muscle. A muscle attaches to an origin and an insertion. The origin is the more fixed attachment, the insertion is the more movable attachment. A muscle acts to shorten, pulling the insertion toward the origin. A muscle can only pull, it cannot push.

Muscles usually come in pairs of antagonistic muscles. The muscle performing the prime movement is the agonist, the opposite acting muscle is the antagonist. When the movement reverses, the names reverse. For example, in flexing the elbow the biceps brachii is the agonist, the triceps brachii is the antagonist. When the movement changes to extension of the elbow, the triceps becomes the agonist and the biceps the antagonist. An antagonist is never totally relaxed. Its function is to provide control and damping of movement by maintaining tone against the agonist. This is called eccentric movement.

Muscles can also act as synergists, working together to perform a movement. This movement can be different from that performed when the muscles work independently. For example, the sternocleidomastoid muscles each rotate the head in a different direction. But as synergists they flex the neck.

Fixators act to keep a part from moving. For example fixators act as postural muscles to keep the spine erect and the leg and vertebral column extended when standing. Fixators such as the rhomboids and levator scapulae keep the scapula from moving during actions such as lifting with the arms.

Urine is a waste byproduct formed from excess water and metabolic waste molecules during the process of renal system filtration. The primary function of the renal system is to regulate blood volume and plasma osmolarity, and waste removal via urine is essentially a convenient way that the body performs many functions using one process. Urine formation occurs during three processes:

Filtration

Reabsorption

Secretion

Filtration

During filtration, blood enters the afferent arteriole and flows into the glomerulus where filterable blood components, such as water and nitrogenous waste, will move towards the inside of the glomerulus, and nonfilterable components, such as cells and serum albumins, will exit via the efferent arteriole. These filterable components accumulate in the glomerulus to form the glomerular filtrate.

Normally, about 20% of the total blood pumped by the heart each minute will enter the kidneys to undergo filtration; this is called the filtration fraction. The remaining 80% of the blood flows through the rest of the body to facilitate tissue perfusion and gas exchange.

Reabsorption

 

The next step is reabsorption, during which molecules and ions will be reabsorbed into the circulatory system. The fluid passes through the components of the nephron (the proximal/distal convoluted tubules, loop of Henle, the collecting duct) as water and ions are removed as the fluid osmolarity (ion concentration) changes. In the collecting duct, secretion will occur before the fluid leaves the ureter in the form of urine.

Secretion

During secretion some substances±such as hydrogen ions, creatinine, and drugs—will be removed from the blood through the peritubular capillary network into the collecting duct. The end product of all these processes is urine, which is essentially a collection of substances that has not been reabsorbed during glomerular filtration or tubular reabsorbtion.

The pancreas

The pancreas consists of clusters if endocrine cells (the islets of Langerhans) and exocrine cells whose secretions drain into the duodenum.

Pancreatic fluid contains:

  • sodium bicarbonate (NaHCO3). This neutralizes the acidity of the fluid arriving from the stomach raising its pH to about 8.
  • pancreatic amylase. This enzyme hydrolyzes starch into a mixture of maltose and glucose.
  • pancreatic lipase. The enzyme hydrolyzes ingested fats into a mixture of fatty acids and monoglycerides. Its action is enhanced by the detergent effect of bile.
  • 4 zymogens— proteins that are precursors to active proteases. These are immediately converted into the active proteolytic enzymes:
    • trypsin. Trypsin cleaves peptide bonds on the C-terminal side of arginines and lysines.
    • chymotrypsin. Chymotrypsin cuts on the C-terminal side of tyrosine, phenylalanine, and tryptophan residues (the same bonds as pepsin, whose action ceases when the NaHCO3 raises the pH of the intestinal contents).
    • elastase. Elastase cuts peptide bonds next to small, uncharged side chains such as those of alanine and serine.
    • carboxypeptidase. This enzyme removes, one by one, the amino acids at the C-terminal of peptides.
  • nucleases. These hydrolyze ingested nucleic acids (RNA and DNA) into their component nucleotides.

The secretion of pancreatic fluid is controlled by two hormones:

  • secretin, which mainly affects the release of sodium bicarbonate, and
  • cholecystokinin (CCK), which stimulates the release of the digestive enzymes.

Bronchitis = Irreversible Bronchioconstriction
 .    Causes - Infection, Air polution, cigarette smoke

a.    Primary Defect = Enlargement & Over Activity of Mucous Glands, Secretions very viscous
b.    Hypertrophy & hyperplasia, Narrows & Blocks bronchi, Lumen of airway, significantly narrow
c.    Impaired Clearance by mucocillary elevator
d.    Microorganism retension in lower airways,Prone to Infectious Bronchitis, Pneumonia
e.    Permanent Inflamatory Changes IN epithelium, Narrows walls, Symptoms, Excessive sputum, coughing
f.    CAN CAUSE EMPHYSEMA

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