Jaundice and haemoglobinopathies
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This document defines jaundice and discusses its causes and types. Jaundice is the yellow discoloration of skin and eyes due to high bilirubin levels in blood. Bilirubin is produced from breakdown of hemoglobin and normally eliminated by the liver. Jaundice can be pre-hepatic from increased hemoglobin breakdown, hepatic from liver issues, or post-hepatic from biliary obstruction. Liver enzymes and bilirubin levels help determine the type of jaundice. The document also discusses physiological jaundice in newborns and provides examples of hemoglobinopathies like sickle cell anemia.
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RBC Indices- MCV, MCH, MCHC II Blood Physiology
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The slide will cover the following:
1. Introduction to RBC indices
2. Mean Corpuscular volume (MCV)
3. Mean Corpuscular hemoglobin (MCH)
4. Mean Corpuscular hemoglobin concentration (MCHC)
5. Color index (CI)
You can also watch the same topic on HM Learnings Youtube channel.
You can also follow HM Learnings on facebook, instagram and twitter for daily updates
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Plasma proteins have important functions including transport, osmotic regulation, catalytic functions, and protective functions. The major plasma proteins are albumin, globulins, and fibrinogen. Albumin is the most abundant plasma protein and serves important roles such as transporting metabolites, maintaining colloid osmotic pressure, and buffering. Electrophoresis is used to separate plasma proteins into fractions including albumin, alpha-1-globulin, alpha-2-globulin, beta-globulin, and gamma-globulin. Abnormal protein levels can provide clues for various clinical diseases.
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The slide will cover the following:
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2. Mean Corpuscular volume (MCV)
3. Mean Corpuscular hemoglobin (MCH)
4. Mean Corpuscular hemoglobin concentration (MCHC)
5. Color index (CI)
You can also watch the same topic on HM Learnings Youtube channel.
You can also follow HM Learnings on facebook, instagram and twitter for daily updates
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2. The screening markers and recommended tests used to detect these infectious agents, such as ELISA, chemiluminescence, and nucleic acid amplification technologies.
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Serum proteins
Serum proteins are the most abundant compounds in blood after removing cells. They serve many important functions including acting as building blocks, enzymes, hormones, antibodies, and helping maintain acid-base balance and osmotic pressure. The major serum proteins measured are albumin and globulins, with albumin primarily made in the liver and globulins including antibodies and transport proteins. Abnormal levels can provide clues about conditions affecting the liver, kidneys, nutrition, infections, and more.
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2) The structure of haemoglobin includes a heme group which is an iron-porphyrin complex, and a globin protein composed of two alpha and two beta polypeptide chains. Haemoglobin's role is to transport oxygen to tissues and carbon dioxide to the lungs.
3) Variations discussed include fetal haemoglobin, sickle cell haemoglobin caused by an amino acid substitution, and thalassemias which are defects in globin chain synthesis. The document provides details on the
Blood screening, quarantine and release
The document discusses procedures for screening donated blood for infectious diseases at a regional laboratory and blood bank. It provides details on:
1. The viruses, bacteria, parasites, and prions that are screened for, including HIV, HCV, HBV, HTLV, syphilis, malaria, and vCJD.
2. The screening markers and recommended tests used to detect these infectious agents, such as ELISA, chemiluminescence, and nucleic acid amplification technologies.
3. Protocols for quarantining and properly disposing of reactive blood units based on screening results, as well as archiving donor samples and blood components for further testing and research.
Coagulation tests
The bleeding time test measures the time it takes for a small puncture wound to stop bleeding. It evaluates platelet function and vascular integrity. The preferred method is the Surgicutt/Simplate method, which uses a spring-loaded device to make a standardized 1mm deep incision. The procedure involves inflating a blood pressure cuff to 40mmHg, making the incision, and blotting the wound every 30 seconds with filter paper to see when bleeding stops. The normal bleeding time range is 1-9 minutes. Sources of error include aspirin use, improper puncture technique, not timing correctly, or allowing the filter paper to touch the wound.
Bombay blood group
- The Bombay blood group is an extremely rare blood type where red blood cells lack the H, A, and B antigens and plasma contains antibodies against these antigens.
- It was first discovered in Bombay, India in 1952 in about 1 in 10,000 people in Mumbai. Worldwide prevalence is about 1 in 1 million.
- People with this blood group can only receive blood from other Bombay blood group donors, as their blood will hemolyze if receiving blood from other blood groups.
- It is important for those with the Bombay blood group to register with blood banks so their rare blood can be available in emergencies.
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Hemoglobin is an oxygen-binding protein in red blood cells. It is composed of four polypeptide subunits - two alpha chains and two beta chains - as well as a heme group containing iron. The heme group gives hemoglobin its red color and allows it to carry oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Mutations in hemoglobin genes can lead to hemoglobinopathies like thalassemias, sickle cell anemia, and hemoglobin M disease. These disorders disrupt hemoglobin's ability to carry oxygen and can cause anemia.
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Hemoglobinopathies are genetic disorders that result in abnormalities in the structure or synthesis of hemoglobin. There are two main types: qualitative abnormalities that change the structure of the globin chains, and quantitative abnormalities that reduce globin chain production (thalassemias). Thalassemias are caused by mutations that decrease or eliminate alpha or beta globin chain synthesis. This leads to imbalanced globin chain production and severe anemia. The most severe form is beta thalassemia major, which requires lifelong blood transfusions if untreated. Beta thalassemia trait is a milder form with microcytic anemia and elevated hemoglobin A2 levels.
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Bilirubin is formed from the breakdown of heme in hemoglobin. It is transported to the liver bound to albumin, where it enters hepatocytes. The liver conjugates bilirubin with glucuronic acid via the enzyme bilirubin UDP-glucuronosyltransferase to increase its solubility. The conjugated bilirubin is excreted in the bile or undergoes enterohepatic circulation and is eventually excreted in the urine. Certain drugs can displace bilirubin from albumin, allowing it to enter the brain and cause neural damage in infants due to their immature bilirubin metabolism.
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Glucosuria
Glucosuria, or glucose in the urine, can occur due to diabetes mellitus resulting in hyperglycemia that exceeds the renal threshold, or due to renal tubular disorders resulting in glycosuria without hyperglycemia. Renal glycosuria is caused by defects in glucose transporters like SGLT2 that normally reabsorb glucose from the glomerular filtrate in the proximal tubule. This leads to glucose appearing in the urine despite normal blood glucose levels. Renal glycosuria is usually benign and inherited in an autosomal recessive pattern, though it can also be caused by advanced chronic kidney disease.
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Glomerular function tests include clearance tests such as creatinine clearance test which measures glomerular filtration rate (GFR). Tubular function tests assess kidney's concentrating and diluting abilities through urine concentration and dilution tests. Urine analysis examines physical properties, chemical components, and microscopic contents of urine to detect abnormalities.
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The document discusses abnormal hemoglobin metabolism and hemoglobinopathies. It provides information on hemoglobin structure, definitions of thalassemias and hemoglobinopathies, specifics on sickle cell anemia and thalassemia, Bart's hydrops fetalis, and diagnosis of hemoglobinopathies. Sickle cell anemia results from a single amino acid substitution causing hemoglobin S, which polymerizes and makes red blood cells rigid and sickle-shaped. Thalassemias involve absent or reduced alpha or beta globin chains. Diagnosis involves family history, symptoms, lab tests, and analyzing hemoglobin structure.
Hemoglobin structure
Haemoglobin is an iron-containing protein in red blood cells that transports oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. It is a tetramer composed of two alpha and two non-alpha subunits. In adults, normal haemoglobin is 96-98% HbA which contains two alpha and two beta subunits. Fetal haemoglobin contains two alpha and two gamma subunits and makes up a smaller percentage. Mutations in the beta globin gene can result in haemoglobinopathies like sickle cell anemia.
Structure and function of hemoglobin
Hemoglubin is are carrier protein for oxygen and CO2. it a pigmented and globular protein present within the red blood cell, its structure, synthesis, and how it function in the transportation of oxygen and CO2 are given in this presentation
MECHANISM OF CONCENTRATION OF URINE
The document discusses the mechanism of urine concentration in the kidney through countercurrent flow. It explains how the loop of Henle acts as a countercurrent multiplier and the vasa recta acts as a countercurrent exchanger to generate and maintain an osmotic gradient in the renal medulla. This gradient allows water to be reabsorbed in the collecting ducts under the influence of ADH, resulting in concentrated urine when water intake is low. The kidney thus regulates urine concentration through countercurrent mechanisms to maintain water homeostasis.
Hemoglobin estimation
This document provides information on hemoglobin estimation methods. It discusses the structure and function of hemoglobin, normal hemoglobin concentration ranges, and various laboratory methods for estimating hemoglobin levels. The key methods described are the Sahli acid hematin method, cyanmethemoglobin method, and automated blood count method. Advantages and disadvantages of each method are outlined.
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The major sites of heme biosynthesis are the liver, which synthesizes a number of heme proteins (particularly the CYP proteins), and the erythrocyte-producing cells of the bone marrow, which are active in hemoglobin synthesis. [Note: Over 85% of all heme synthesis occurs in erythroid tissue.] In the liver, the rate of heme synthesis is highly variable, responding to alterations in the cellular heme pool caused by fluctuating demands for heme proteins. In contrast, heme synthesis in erythroid cells is relatively constant and is matched to the rate of globin synthesis. The initial reaction and the last three steps in the formation of porphyrins occur in mitochondria, whereas the intermediate steps of the biosynthetic pathway occur in the cytosol. [Note: Mature red blood cells (RBCs) lack mitochondria and are unable to synthesize heme.]
Postoperative jaundice
Jaundice is a condition where the skin and eyes take on a yellowish color due to high bilirubin levels. It can be caused by excessive breakdown of red blood cells, liver problems impairing bilirubin processing or excretion, or blockages obstructing bile flow. Diagnosis involves blood tests to measure bilirubin levels and other liver enzymes. Treatment depends on the underlying cause but may include medications, surgery, or phototherapy for newborns. Preventive measures include moderating alcohol intake and getting vaccinated against hepatitis if traveling to endemic regions.
Heme metabolism
1. Heme synthesis occurs in mitochondria and involves two starting molecules, succinyl CoA and glycine. The reaction produces aminolevulonic acid and needs the enzyme ALA synthase.
2. There are several types of hemoglobin in humans including HbA, HbA2, fetal Hb, and HbA1c. HbA1c levels are used to monitor diabetes by indicating average blood glucose levels over several weeks.
3. Abnormal hemoglobins include methemoglobin, carboxyhemoglobin, sulfhemoglobin, and hematin. Porphyrias are diseases caused by deficiencies in heme synthesis enzymes that can cause anemia, pain, and photosensitivity.
JAUNDICE PRESENTATION FOR MEDICAL STUDENTS AROUND THE WORLD
This document discusses bilirubin metabolism and jaundice. It begins by defining bilirubin and jaundice, and outlines the normal concentration of bilirubin in the blood. It then describes the three main types of jaundice: pre-hepatic (hemolytic) jaundice caused by excessive bilirubin production; hepatic (hepatocellular) jaundice caused by impaired liver function; and post-hepatic (obstructive) jaundice caused by obstruction of the biliary tract. For each type, the document discusses causes, clinical features, and pathophysiology. It also covers neonatal jaundice, risk factors, evaluation, and management.
Jaundice
The document discusses jaundice, which is caused by increased bilirubin in the blood. Bilirubin is produced during the natural breakdown of red blood cells. Normally the liver metabolizes and excretes bilirubin, but jaundice can occur if this process is disrupted. Jaundice has pre-hepatic, hepatic, and post-hepatic causes that relate to where in the process the disruption occurs. The types of jaundice include neonatal, obstructive, hemolytic, and cholestatic varieties. Symptoms of jaundice include yellow skin and eyes, light stool, dark urine, and potentially abdominal pain or itching.
Neonatal hyperbilirubinemia management
This document discusses the management of hyperbilirubinemia in newborns. It begins by covering bilirubin metabolism, sources of bilirubin, and inherited disorders that can cause jaundice. It then addresses physiological and non-physiological hyperbilirubinemia in newborns. The management section covers evaluation, treatment options like phototherapy and exchange transfusion, and measures to prevent bilirubin toxicity and kernicterus. Key points include the various causes of neonatal jaundice, methods for estimating bilirubin levels, and the mechanisms by which phototherapy works to reduce serum bilirubin.
Jaundice (new).ppt
Jaundice, or yellowish discoloration of the skin and eyes, occurs when bilirubin levels are elevated above normal in the bloodstream. Bilirubin is produced from the breakdown of hemoglobin in red blood cells. There are three main types of jaundice based on where the blockage in bilirubin metabolism occurs: hemolytic, cholestatic, and hepatocellular. Hemolytic jaundice results from excessive red blood cell breakdown that overloads the liver's bilirubin processing. Cholestatic jaundice occurs when bile flow from the liver is obstructed. Hepatocellular jaundice reflects impaired bilirubin processing in the liver itself due
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JAUNDICE PRESENTATION FOR MEDICAL STUDENTS AROUND THE WORLD
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Jaundice and haemoglobinopathies
- 1. By Dr. Abdul Majid Siddiqui
- 2. Definition: yellow discolouration of skin and sclera as a result of hyperbilirubinaemia Bilirubin >35mmol/L for jaundice to be visible on examination Sclera first place to become jaundiced
- 3. Bilirubin is a product of metabolism of haemoglobin (80%) and other haem containing proteins (e.g. Myoglboin, cytochrome P450: 20%) Degredation of haemoglobin into bilirubin takes place in macrophages. Bilirubin is then excreted into plasma and binds with albumin Haemoglobin Globin Haem (iron + porphyrin) Amino Acids Biliverdin Bilirubin (unconjugated) Bilirubin binds to albumin in the plasma RBC breakdown
- 5. Pre-hepatic: pathology occuring prior to the liver Any cause of increased haemolysis (e.g. Spherocytosis, thalassaemia, sickle cell disease, transfusion reaction, auto- immune, malaria etc.) and some drugs Causes unconjugated hyperbilirubinaemia Intra-Hepatic: pathology occuring within the liver All the causes of hepatitis/cirrhosis (e.g. Alcohol, viral, auto- immune, primray biliary cirrhosis etc) Can result in hepatocyte destruction and therefore unconjugated hyperbilirubinaemia or in bile cannaliculi destruction and therefore conjugated hyperbilirubinaemia or both
- 6. Post-hepatic: Pathology occuring after conjugation of bilirubin within the liver (also known as obstructive jaundice) •Any cause of biliary obstruction (e.g. Gallstones) •Causes conjugatedhyperbilirubinaemia
- 7. PHYSIOLOGICAL JAUNDICE Usually mild form of jaundice appears in some newborn children on the second or third day of life,called jaundice of newborn or Neonatal jaundice. CAUSE--- Excessive destruction of R B Cs after birth causing increase in serum bilirubin. Due to hepatic immaturity-- During intrauterine life bilirubin formed is mainly eliminated via the placenta and to lesser extent by liver. Immediately after birth the liver has to eliminate all the bilirubin formed, therefore, liver is unable to deal adequately with this increase amount of bilirubin during the first 10 days of life causing development of jaundice When S. Bilirubin risebeyond 5mg/dL clinical jaundice apperars Treatment----Phototherapy
- 8. Test Pre-hepatic Hepatic Post-hepatic Total bilirubin + ++ +++ Conjugated bilirubin Normal Increased Increased Unconjugated bilirubin Increased Increased Normal Total bilirubin and its conjugated and unconjugated levels help to determine nature of jaundice
- 9. Liver Enzymes ALT/AST mainly present in hepatocytes ALP/GGT mainly present in bile cannaliculi biliary tree Derrangement of particular liver enzymes in association with jaundice can determine nature of the jaundice Test Pre-hepatic Hepatic Post-hepatic ALT/AST Normal +++ + ALP/GGT Normal + +++
- 10. Hemoglobinopathy is a genetic disorder caused by abnormal polypeptide chains of hemoglobin. Some of the hemoglobinopathies are: i. Hemoglobin S: It is found in sickle cell anemia. In this, the α-chains are normal and β-chains are abnormal. ii. Hemoglobin C: The β-chains are abnormal. It is found in people with hemoglobin C disease, which is characterized by mild hemolytic anemia and splenomegaly. Hemoglobinopathies
- 11. iii. Hemoglobin E: Here also the β-chains are abnormal. It is present in people with hemoglobin E disease which is also characterized by mild hemolytic anemia and splenomegaly. iv. Hemoglobin M: It is the abnormal hemoglobin present in the form of methemoglobin. It occurs due to mutation of genes of both in α and β chains, resulting in abnormal replacement of amino acids. It is present in babies affected by hemoglobin M disease or blue baby syndrome. It is an inherited disease, characterized by methemoglobinemia