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Physiology - NEETMDS- courses
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Physiology

The Cardiac Cycle: the sequence of events in one heartbeat.

systole - the contraction phase; unless otherwise specified refers to left ventricle, but each chamber has its own systole.

diastole - the relaxation phase; unless otherwise specified refers to left ventricle, but each chamber has its own diastole.

1) quiescent period - period when all chambers are at rest and filling. 70% of ventricular filling occurs during this period. The AV valves are open, the semilunar valves are closed.

2) atrial systole - pushes the last 30% of blood into the ventricle.

3) atrial diastole - atria begin filling.

4) ventricular systole - First the AV valves close causing the first heart sound, then after the isovolumetric contraction phase the semilunar valves open permitting ventricular ejection of blood into the arteries.

5) ventricular diastole - As the ventricles relax the semilunar valves close first producing the second heart sound, then after the isovolumetric relaxation phase the AV valves open allowing ventricular filling.

The Stomach :

The wall of the stomach is lined with millions of gastric glands, which together secrete 400–800 ml of gastric juice at each meal. Three kinds of cells are found in the gastric glands

  • parietal cells
  • chief cells
  • mucus-secreting cells

Parietal cells : secrete

Hydrochloric acid : Parietal cells contain a H+ ATPase. This transmembrane protein secretes H+ ions (protons) by active transport, using the energy of ATP.

Intrinsic factor: Intrinsic factor is a protein that binds ingested vitamin B12 and enables it to be absorbed by the intestine. A deficiency of intrinsic factor  as a result of an autoimmune attack against parietal cells  causes pernicious anemia.

Chief Cells : The chief cells synthesize and secrete pepsinogen, the precursor to the proteolytic enzyme pepsin.

Secretion by the gastric glands is stimulated by the hormone gastrin. Gastrin is released by endocrine cells in the stomach in response to the arrival of food.

Carbon Dioxide Transport

Carbon dioxide (CO2) combines with water forming carbonic acid, which dissociates into a hydrogen ion (H+) and a bicarbonate ions:

CO2 + H2O ↔ H2CO3 ↔ H+ + HCO3

95% of the CO2 generated in the tissues is carried in the red blood cells:

  • It probably enters (and leaves) the cell by diffusing through transmembrane channels in the plasma membrane. (One of the proteins that forms the channel is the D antigen that is the most important factor in the Rh system of blood groups.)
  • Once inside, about one-half of the CO2 is directly bound to hemoglobin (at a site different from the one that binds oxygen).
  • The rest is converted — following the equation above — by the enzyme carbonic anhydrase into
    • bicarbonate ions that diffuse back out into the plasma and
    • hydrogen ions (H+) that bind to the protein portion of the hemoglobin (thus having no effect on pH).

Only about 5% of the CO2 generated in the tissues dissolves directly in the plasma. (A good thing, too: if all the CO2 we make were carried this way, the pH of the blood would drop from its normal 7.4 to an instantly-fatal 4.5!)

When the red cells reach the lungs, these reactions are reversed and CO2 is released to the air of the alveoli.

Serum Proteins

Proteins make up 6–8% of the blood. They are about equally divided between serum albumin and a great variety of serum globulins.

After blood is withdrawn from a vein and allowed to clot, the clot slowly shrinks. As it does so, a clear fluid called serum is squeezed out. Thus:

Serum is blood plasma without fibrinogen and other clotting factors.

The serum proteins can be separated by electrophoresis.

  • The most prominent of these and the one that moves closest to the positive electrode is serum albumin.
  • Serum albumin
    • is made in the liver
    • binds many small molecules for transport through the blood
    • helps maintain the osmotic pressure of the blood
  • The other proteins are the various serum globulins.
    • alpha globulins (e.g., the proteins that transport thyroxine and retinol [vitamin A])
    • beta globulins (e.g., the iron-transporting protein transferrin)
    • gamma globulins.
      • Gamma globulins are the least negatively-charged serum proteins. (They are so weakly charged, in fact, that some are swept in the flow of buffer back toward the negative electrode.)
      • Most antibodies are gamma globulins.
      • Therefore gamma globulins become more abundant following infections or immunizations. 

The Types of muscle cells. There are three types, red, white, and intermediate.

White Fibers

Fast twitch

Large diameter, used for speed and strength.

Depends on the phosphagen system and on glycolysis-lactic acid.

Stores glycogen for conversion to glucose.

Fewer blood vessels.

Little or no myoglobin.

Red Fibers

Slow twitch

Small diameter, used for endurance.

Depends on aerobic metabolism.

Utilize fats as well as glucose.

Little glycogen storage.

Many blood vessels and much myoglobin give this muscle its reddish appearance.

 

Intermediate Fibers: sometimes called "fast twitch red", these fibers have faster action but rely more on aerobic metabolism and have more endurance. Most muscles are mixtures of the different types. Muscle fiber types and their relative abundance cannot be varied by training, although there is some evidence that prior to maturation of the muscular system the emphasis on certain activities can influence their development

Bleeding Disorders

A deficiency of a clotting factor can lead to uncontrolled bleeding.

The deficiency may arise because

  • not enough of the factor is produced or
  • a mutant version of the factor fails to perform properly.

Examples:

  • von Willebrand disease (the most common)
  • hemophilia A for factor 8 deficiency
  • hemophilia B for factor 9 deficiency.
  • hemophilia C for factor 11 deficiency

In some cases of von Willebrand disease, either a deficient level or a mutant version of the factor eliminates its protective effect on factor 8. The resulting low level of factor 8 mimics hemophilia A.

The thyroid gland is a double-lobed structure located in the neck. Embedded in its rear surface are the four parathyroid glands.

The Thyroid Gland

The thyroid gland synthesizes and secretes:

  • thyroxine (T4) and
  • calcitonin

T4 and T3

Thyroxine (T4 ) is a derivative of the amino acid tyrosine with four atoms of iodine. In the liver, one atom of iodine is removed from T4 converting it into triiodothyronine (T3). T3 is the active hormone. It has many effects on the body. Among the most prominent of these are:

  • an increase in metabolic rate
  • an increase in the rate and strength of the heart beat.

The thyroid cells responsible for the synthesis of T4 take up circulating iodine from the blood. This action, as well as the synthesis of the hormones, is stimulated by the binding of TSH to transmembrane receptors at the cell surface.

Diseases of the thyroid

1. hypothyroid diseases; caused by inadequate production of T3

  • cretinism: hypothyroidism in infancy and childhood leads to stunted growth and intelligence. Can be corrected by giving thyroxine if started early enough.
  • myxedema: hypothyroidism in adults leads to lowered metabolic rate and vigor. Corrected by giving thyroxine.
  • goiter: enlargement of the thyroid gland. Can be caused by:
    • inadequate iodine in the diet with resulting low levels of T4 and T3;
    • an autoimmune attack against components of the thyroid gland (called Hashimoto's thyroiditis).

2. hyperthyroid diseases; caused by excessive secretion of thyroid hormones

Graves´ disease. Autoantibodies against the TSH receptor bind to the receptor mimicking the effect of TSH binding. Result: excessive production of thyroid hormones. Graves´ disease is an example of an autoimmune disease.

Osteoporosis. High levels of thyroid hormones suppress the production of TSH through the negative-feedback mechanism mentioned above. The resulting low level of TSH causes an increase in the numbers of bone-reabsorbing osteoclasts resulting in osteoporosis.

Calcitonin

Calcitonin is a polypeptide of 32 amino acids. The thyroid cells in which it is synthesized have receptors that bind calcium ions (Ca2+) circulating in the blood. These cells monitor the level of circulating Ca2+. A rise in its level stimulates the cells to release calcitonin.

  • bone cells respond by removing Ca2+ from the blood and storing it in the bone
  • kidney cells respond by increasing the excretion of Ca2+

Both types of cells have surface receptors for calcitonin.

Because it promotes the transfer of Ca2+ to bones, calcitonin has been examined as a possible treatment for osteoporosis

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