Amyloidosis
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Amyloidosis occurs when misfolded proteins aggregate and deposit in extracellular tissues, causing damage. The deposits take up Congo Red stain and show apple-green birefringence under polarized light. Amyloidosis can be systemic, involving multiple organs, or localized to one organ. The main types are primary amyloidosis, caused by immunoglobulin light chain deposition; secondary, caused by serum amyloid A protein in chronic inflammatory states; and familial Mediterranean fever. Treatment involves chemotherapy, blood thinners, dialysis, organ transplantation or stem cell transplant depending on the severity and organs involved.
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AMYLODIOSIS
Amyloidosis is the term used for a group of diseases characterized by extracellular deposition of insoluble protienaceous substance called “Amyloid”.Amyloidosis was first described by Rokintansy in 1842.
Virchow named it as amyloid under the mistaken belief that the material was starch like.
Amyloidosis
Dr. Sadaf Khan discusses amyloidosis, a disorder caused by the deposition of abnormal protein fibrils in tissues and organs. Amyloidosis can be localized to a single organ or systemic. The type of amyloid protein deposited determines the classification, with the most common types being AL amyloidosis associated with plasma cell dyscrasias and AA amyloidosis associated with inflammatory conditions. Diagnosis involves staining biopsy samples with dyes like Congo red and examining under polarized light. Treatment depends on the type and organ involvement but may include targeting the underlying condition, chemotherapy, dialysis, or organ transplantation.
Amyloidosis
Amyloidosis is a condition characterized by the deposition of abnormal protein fibrils called amyloid in tissues and organs. It results from misfolded proteins aggregating into insoluble deposits. Amyloidosis can be classified based on cause, extent of deposition, histological features, clinical location, tissue affected, and precursor protein involved. Common symptoms vary by the organs affected but may include weakness, weight loss, hepatomegaly, cardiac issues, and neuropathy. Diagnosis involves tests to evaluate organ involvement, biopsy with Congo red staining to identify amyloid deposits, and immunohistochemistry to determine the type of amyloid protein. Alzheimer's disease involves amyloid plaques and neurofibrillary tangles in the brain that can be detected by molecular PET
Amyloidosis
This document discusses amyloidosis, which is the extracellular deposition of abnormal protein fibrils called amyloid in tissues and organs. Amyloidosis can be primary, meaning the deposition is in the disease itself, or secondary, as a complication of another underlying disease. Diagnosis involves biopsy and staining of tissues with Congo red dye to detect amyloid deposits. The kidney is a commonly affected organ where amyloid deposits are seen in the glomerular capillary tuft and surrounding tissues, which can lead to atrophy and impaired function.
Amyloidosis
Amyloidosis is a condition caused by abnormal protein deposits forming fibrils that damage tissues. These fibrils result from improperly folded proteins aggregating. There are different types depending on the precursor protein, including AL amyloidosis associated with plasma cell disorders and AA amyloidosis linked to chronic inflammation. Amyloid fibrils have a characteristic beta-pleated sheet structure and stain apple-green under polarized light when bound to Congo red dye. The deposits can affect many organs and cause tissue destruction and organ dysfunction. The kidneys, liver, spleen, heart and nervous system are commonly involved.
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The document discusses the benefits of exercise for mental health. Regular physical activity can help reduce anxiety and depression and improve mood and cognitive function. Exercise causes chemical changes in the brain that may help protect against mental illness and improve symptoms for those who already suffer from conditions like anxiety and depression.
Amyloidosis 1
Amyloidosis refers to abnormal deposits of insoluble fibrillar proteins in tissues. It is associated with conditions like multiple myeloma. The deposits have similar staining properties but different biochemical structures. On microscopy, amyloid deposits appear as non-branching fibrils composed of beta-pleated sheets. Major forms are AL, AA, and A-beta. Clinical manifestations depend on organ involvement and include weakness, renal failure, and heart failure. Definitive diagnosis requires biopsy and Congo red staining showing apple-green birefringence. Prognosis varies by type from median 2 years for AL to over 10 years for ATTR.
Amyloidosis
1. Amyloidosis occurs when misfolded proteins aggregate into insoluble fibrils that deposit in tissues, damaging organ structure and function.
2. There are different types of amyloidosis depending on the type of protein that aggregates, including light chain (AL), amyloid A (AA), and variants associated with specific proteins like transthyretin.
3. Amyloidosis can be localized to single organs or systemic, and systemic forms include primary amyloidosis associated with plasma cell disorders, secondary amyloidosis linked to chronic inflammation, and rare hereditary types.
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AMYLODIOSIS
Amyloidosis is the term used for a group of diseases characterized by extracellular deposition of insoluble protienaceous substance called “Amyloid”.Amyloidosis was first described by Rokintansy in 1842.
Virchow named it as amyloid under the mistaken belief that the material was starch like.
Amyloidosis
Dr. Sadaf Khan discusses amyloidosis, a disorder caused by the deposition of abnormal protein fibrils in tissues and organs. Amyloidosis can be localized to a single organ or systemic. The type of amyloid protein deposited determines the classification, with the most common types being AL amyloidosis associated with plasma cell dyscrasias and AA amyloidosis associated with inflammatory conditions. Diagnosis involves staining biopsy samples with dyes like Congo red and examining under polarized light. Treatment depends on the type and organ involvement but may include targeting the underlying condition, chemotherapy, dialysis, or organ transplantation.
Amyloidosis
Amyloidosis is a condition characterized by the deposition of abnormal protein fibrils called amyloid in tissues and organs. It results from misfolded proteins aggregating into insoluble deposits. Amyloidosis can be classified based on cause, extent of deposition, histological features, clinical location, tissue affected, and precursor protein involved. Common symptoms vary by the organs affected but may include weakness, weight loss, hepatomegaly, cardiac issues, and neuropathy. Diagnosis involves tests to evaluate organ involvement, biopsy with Congo red staining to identify amyloid deposits, and immunohistochemistry to determine the type of amyloid protein. Alzheimer's disease involves amyloid plaques and neurofibrillary tangles in the brain that can be detected by molecular PET
Amyloidosis
This document discusses amyloidosis, which is the extracellular deposition of abnormal protein fibrils called amyloid in tissues and organs. Amyloidosis can be primary, meaning the deposition is in the disease itself, or secondary, as a complication of another underlying disease. Diagnosis involves biopsy and staining of tissues with Congo red dye to detect amyloid deposits. The kidney is a commonly affected organ where amyloid deposits are seen in the glomerular capillary tuft and surrounding tissues, which can lead to atrophy and impaired function.
Amyloidosis
Amyloidosis is a condition caused by abnormal protein deposits forming fibrils that damage tissues. These fibrils result from improperly folded proteins aggregating. There are different types depending on the precursor protein, including AL amyloidosis associated with plasma cell disorders and AA amyloidosis linked to chronic inflammation. Amyloid fibrils have a characteristic beta-pleated sheet structure and stain apple-green under polarized light when bound to Congo red dye. The deposits can affect many organs and cause tissue destruction and organ dysfunction. The kidneys, liver, spleen, heart and nervous system are commonly involved.
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The document discusses the benefits of exercise for mental health. Regular physical activity can help reduce anxiety and depression and improve mood and cognitive function. Exercise causes chemical changes in the brain that may help protect against mental illness and improve symptoms for those who already suffer from conditions like anxiety and depression.
Amyloidosis 1
Amyloidosis refers to abnormal deposits of insoluble fibrillar proteins in tissues. It is associated with conditions like multiple myeloma. The deposits have similar staining properties but different biochemical structures. On microscopy, amyloid deposits appear as non-branching fibrils composed of beta-pleated sheets. Major forms are AL, AA, and A-beta. Clinical manifestations depend on organ involvement and include weakness, renal failure, and heart failure. Definitive diagnosis requires biopsy and Congo red staining showing apple-green birefringence. Prognosis varies by type from median 2 years for AL to over 10 years for ATTR.
Amyloidosis
1. Amyloidosis occurs when misfolded proteins aggregate into insoluble fibrils that deposit in tissues, damaging organ structure and function.
2. There are different types of amyloidosis depending on the type of protein that aggregates, including light chain (AL), amyloid A (AA), and variants associated with specific proteins like transthyretin.
3. Amyloidosis can be localized to single organs or systemic, and systemic forms include primary amyloidosis associated with plasma cell disorders, secondary amyloidosis linked to chronic inflammation, and rare hereditary types.
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This document discusses pathology related to the extracellular matrix and connective tissue. It describes abnormalities that can occur in the extracellular matrix, including abnormal accumulations of proteins like fibrinoid, hyaline, and amyloid. It also discusses disorders in the metabolism and structure of key extracellular matrix components like collagen and elastin. Specific conditions that affect the extracellular matrix are explained in detail, such as disorders of collagen synthesis and structure, abnormalities in proteoglycan content, and amyloid deposition. Staining techniques used to identify different extracellular matrix abnormalities are also outlined.
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Amyloidosis is a condition caused by the deposition of abnormal protein fibrils called amyloid in tissues and organs. The document discusses the definition, history, and properties of amyloid proteins. It notes that amyloidosis can be inherited or inflammatory in nature. Amyloid proteins have a cross beta-pleated sheet structure, form non-branching fibrils 7.5-10 nm in diameter, and stain with Congo red. Major forms include AL, AA, and Aβ proteins, while minor forms include transthyretin and β2-microglobulin. The name "amyloid" comes from its similarity to starch when viewed microscopically.
Recent advances in amyloidosis
This document provides an overview of amyloidosis, including:
- Amyloidosis is caused by the extracellular deposition of misfolded proteins forming fibrils. There are different types classified by the precursor protein involved.
- Systemic forms include AL amyloidosis associated with plasma cell disorders and AA amyloidosis associated with inflammatory conditions.
- Diagnosis involves biopsy of tissues like fat pad or organs stained with Congo red to identify amyloid deposits. Immunohistochemistry identifies the precursor protein type.
- Organ involvement varies but kidney, heart, liver and spleen are commonly affected. Clinical manifestations depend on the organs involved and may include proteinuria, heart failure, hepatomegaly or neurological symptoms.
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- Risk factors that can lead to coronary artery blockage include hypertension, hyperlipidemia, diabetes, and smoking.
- A thrombus or embolism in a coronary artery cuts off the blood supply, causing cell death in the affected heart muscle area.
- The location and size of the infarction depends on which coronary artery is blocked. Transmural infarcts that penetrate the full heart wall thickness are more likely to cause complications than smaller subendocardial infarcts.
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- Amyloidosis is characterized by the abnormal deposition of amyloid protein in tissues and organs. The amyloid protein forms non-branching fibrils that take on an abnormal beta-pleated sheet configuration.
- There are multiple subtypes of amyloidosis based on the type of amyloid protein deposited, including AL amyloidosis associated with plasma cell dyscrasias and AA amyloidosis associated with chronic inflammatory conditions.
- Amyloidosis can be systemic, involving multiple organ systems, or localized to a single organ. Common sites of involvement include the kidneys, liver, spleen, heart, and skin. Deposition of amyloid protein in organs can lead to organ dysfunction and failure.
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This document summarizes different types of intracellular accumulations and cellular aging. It discusses how accumulations of substances like lipids, proteins, glycogen and pigments can occur in cells due to metabolic disturbances and can cause injury if progressive. Specific accumulations mentioned include fatty change/steatosis in the liver from alcohol abuse, cholesterol deposits in atherosclerosis and gallbladder disease, carbon pigment in lung tissues, and calcium salts in dystrophic and metastatic calcification. Cellular aging is described as the gradual decline in function over time due to genetic factors and buildup of molecular damage through mechanisms like DNA damage and limited replicative capacity.
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by post graduates from Maratha Mandal's NathajiRao Halgekar Institute of Dental Sciences, Belgavi.
A step wise presentation of Amylodosis covering,
INTRODUCTION
DEFINITION
HISTORY
PHYSICAL NATURE
CHEMICAL NATURE
CLASSIFICATION
PATHOGENESIS
STAINING CHARACTERISTICS
DIAGNOSTIC TESTS
MORPHOLOGY
CLINICAL FEATURES
TREATMENT
PROGNOSIS
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This document discusses sideroblastic anemia, including:
- It is characterized by abnormal iron deposits in erythroblast mitochondria, producing ringed sideroblasts instead of healthy red blood cells.
- It can be hereditary or acquired. Hereditary types often have normocytic or microcytic anemia while acquired types are usually normocytic or macrocytic.
- Causes include genetic disorders affecting heme synthesis, alcohol use, vitamin deficiencies, and exposures like lead.
- Symptoms depend on severity of anemia but can include fatigue, weakness, and heart/organ damage from iron overload.
- Diagnosis involves blood tests showing elevated iron levels and ringed siderImmunopathology 6
Amyloidosis is a group of diseases caused by abnormal protein deposits in tissues. There are different types of amyloid proteins that can deposit, including immunoglobulin light chains (AL), serum amyloid A (AA), and beta-amyloid. The deposits disrupt organ function over time and can affect the kidneys, heart, liver, spleen, and tongue. Symptoms vary by the organs involved but may include kidney failure, heart failure, digestive issues, and enlarged tongue. The prognosis depends on the type and extent of amyloidosis. Treatment focuses on managing the underlying condition that causes protein deposition or targeting the amyloid deposits directly.
Amyloidosis
This document discusses amyloidosis, including:
- Amyloidosis occurs when proteins aggregate into insoluble fibrils called amyloid that deposit abnormally in tissues. Over 30 proteins can form amyloid fibrils.
- Deposition can result from excessive protein production, mutations causing improper folding, or defective degradation of extracellular proteins. Deposits damage tissues.
- The main types are AL amyloidosis from immunoglobulin light chains, AA amyloidosis from serum amyloid A, and ATTR amyloidosis from transthyretin.
- Amyloidosis can be systemic, affecting multiple organs, or localized to single organs. Common sites for biopsy include kidney, rectum, abdominal fat. Congo red staining demonstrates amyloid's pink
Amyloidosis
The document discusses amyloidosis, beginning with definitions, mechanisms of formation, and common characteristics. It classifies amyloidosis as either systemic or localized, acquired or inherited. The most common types discussed are AL and AA amyloidosis. AL amyloidosis is caused by immunoglobulin light chains and commonly affects the kidneys and heart. Treatment aims to reduce monoclonal protein production and use chemotherapy. AA amyloidosis is linked to chronic inflammatory conditions and deposits serum amyloid A protein, primarily affecting the kidneys. Treatment focuses on the underlying inflammatory disease.
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This document summarizes various blood disorders that affect red blood cells. It begins by describing anemia of blood loss from acute hemorrhage or chronic blood loss. It then discusses hemolytic anemias, where red blood cells are destroyed faster than normal, including hereditary spherocytosis, sickle cell anemia, and thalassemia. Hereditary spherocytosis is caused by inherited defects in the red blood cell membrane. Sickle cell anemia results from a genetic mutation that causes hemoglobin to polymerize and distort the red blood cells into a sickle shape. Thalassemias are caused by mutations that decrease alpha or beta globin synthesis. The document also reviews impaired red cell production and other acquired
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Megaloblastic anemia is caused by a deficiency of vitamin B12 or folate, which are essential for DNA synthesis and the production of red blood cells. This leads to large, abnormally developed red blood cells seen in the bone marrow. Symptoms include anemia, fatigue, and neurological issues. Diagnosis involves blood tests to check vitamin B12 and folate levels. Treatment consists of lifelong vitamin B12 injections or high dose oral supplements to replenish stores, along with folate supplements for a period of time.
AMYLOIDOSIS
The document discusses amyloidosis and summarizes key information:
1) Amyloidosis occurs when amyloid proteins deposit abnormally in tissues, appearing pink and amorphous under microscopy. Amyloid shows apple-green birefringence with Congo red staining under polarized light.
2) Amyloid is composed mainly of fibril proteins that form beta-pleated sheets. The two major types are AL and AA amyloid.
3) Organs commonly affected include kidney, heart, liver, spleen and brain. Kidney amyloidosis often causes nephrotic syndrome. Diagnosis involves tissue biopsy and Congo red staining of deposits.
Amyloidoisis
Amyloidosis is caused by deposition of abnormal amyloid proteins in tissues, damaging their structure and function. There are different types depending on the precursor protein, but all amyloid proteins form insoluble fibrils with beta-pleated sheet structures. The two main types are primary amyloidosis associated with plasma cell dyscrasias and secondary amyloidosis linked to chronic inflammatory conditions. Amyloid deposits can affect many organs like kidneys, heart, liver and spleen, causing organ dysfunction. On staining, amyloid takes up Congo red dye and exhibits apple-green birefringence under polarized light microscopy.
AMYLOIDDFHGDDSCBJUUFFFVVXFTGGVVBOSIS.pdf
This document provides an overview of amyloidosis, including:
- Amyloidosis is caused by the deposition of abnormal protein fibrils in tissues, which can damage organs.
- There are different types of amyloid proteins including light chains, serum amyloid A, and beta-amyloid.
- Amyloidosis can be primary (associated with plasma cell disorders), secondary (associated with chronic inflammation), hereditary, or localized.
- Organs commonly involved include the kidneys, heart, liver, spleen, and tongue. Deposits appear pink with Congo red staining and apple-green under polarized light.
amyloidosis 2.pdf
Amyloidosis is a condition characterized by the abnormal deposition of amyloid protein fibrils in tissues and organs. The fibrils form when normally soluble proteins misfold and aggregate extracellularly. Amyloidosis has many subtypes classified by the precursor protein involved, pattern of organ involvement, and hereditary versus inflammatory causes. Diagnosis involves tissue biopsy with Congo red staining to identify the apple-green birefringence of amyloid under polarized light, as well as immunohistochemistry to determine the subtype. Advanced imaging and molecular PET can also detect amyloid plaques in neurodegenerative diseases like Alzheimer's.
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This document discusses pathology related to the extracellular matrix and connective tissue. It describes abnormalities that can occur in the extracellular matrix, including abnormal accumulations of proteins like fibrinoid, hyaline, and amyloid. It also discusses disorders in the metabolism and structure of key extracellular matrix components like collagen and elastin. Specific conditions that affect the extracellular matrix are explained in detail, such as disorders of collagen synthesis and structure, abnormalities in proteoglycan content, and amyloid deposition. Staining techniques used to identify different extracellular matrix abnormalities are also outlined.
Amyloidosis 1
Amyloidosis is a condition caused by the deposition of abnormal protein fibrils called amyloid in tissues and organs. The document discusses the definition, history, and properties of amyloid proteins. It notes that amyloidosis can be inherited or inflammatory in nature. Amyloid proteins have a cross beta-pleated sheet structure, form non-branching fibrils 7.5-10 nm in diameter, and stain with Congo red. Major forms include AL, AA, and Aβ proteins, while minor forms include transthyretin and β2-microglobulin. The name "amyloid" comes from its similarity to starch when viewed microscopically.
Recent advances in amyloidosis
This document provides an overview of amyloidosis, including:
- Amyloidosis is caused by the extracellular deposition of misfolded proteins forming fibrils. There are different types classified by the precursor protein involved.
- Systemic forms include AL amyloidosis associated with plasma cell disorders and AA amyloidosis associated with inflammatory conditions.
- Diagnosis involves biopsy of tissues like fat pad or organs stained with Congo red to identify amyloid deposits. Immunohistochemistry identifies the precursor protein type.
- Organ involvement varies but kidney, heart, liver and spleen are commonly affected. Clinical manifestations depend on the organs involved and may include proteinuria, heart failure, hepatomegaly or neurological symptoms.
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This document provides an overview of pathological alterations and degenerations. It defines alteration as pathological changes to cells, tissues, and organs that disrupt normal function. Degenerations are classified based on localization of metabolism and deposition of substances. Common intracellular accumulations involve excess water, lipids, proteins or carbohydrates. Parenchymal degenerations can result in hyaline-drop, hydropic, or granular changes in cells. Amyloidosis is characterized by extracellular deposition of abnormal fibrillar proteins that can be systemic or localized. Histological examination of biopsies is important for diagnosing suspected amyloidosis.
Infarction
This document provides information about myocardial infarction including:
- Myocardial infarction is caused by interruption of blood supply to the heart muscle, usually due to blockage of a coronary artery.
- Risk factors that can lead to coronary artery blockage include hypertension, hyperlipidemia, diabetes, and smoking.
- A thrombus or embolism in a coronary artery cuts off the blood supply, causing cell death in the affected heart muscle area.
- The location and size of the infarction depends on which coronary artery is blocked. Transmural infarcts that penetrate the full heart wall thickness are more likely to cause complications than smaller subendocardial infarcts.
5 immunology-csbrp
- Amyloidosis is characterized by the abnormal deposition of amyloid protein in tissues and organs. The amyloid protein forms non-branching fibrils that take on an abnormal beta-pleated sheet configuration.
- There are multiple subtypes of amyloidosis based on the type of amyloid protein deposited, including AL amyloidosis associated with plasma cell dyscrasias and AA amyloidosis associated with chronic inflammatory conditions.
- Amyloidosis can be systemic, involving multiple organ systems, or localized to a single organ. Common sites of involvement include the kidneys, liver, spleen, heart, and skin. Deposition of amyloid protein in organs can lead to organ dysfunction and failure.
intracellular accumulations, calcifications and cellular ageing.
This document summarizes different types of intracellular accumulations and cellular aging. It discusses how accumulations of substances like lipids, proteins, glycogen and pigments can occur in cells due to metabolic disturbances and can cause injury if progressive. Specific accumulations mentioned include fatty change/steatosis in the liver from alcohol abuse, cholesterol deposits in atherosclerosis and gallbladder disease, carbon pigment in lung tissues, and calcium salts in dystrophic and metastatic calcification. Cellular aging is described as the gradual decline in function over time due to genetic factors and buildup of molecular damage through mechanisms like DNA damage and limited replicative capacity.
Amylodosis
by post graduates from Maratha Mandal's NathajiRao Halgekar Institute of Dental Sciences, Belgavi.
A step wise presentation of Amylodosis covering,
INTRODUCTION
DEFINITION
HISTORY
PHYSICAL NATURE
CHEMICAL NATURE
CLASSIFICATION
PATHOGENESIS
STAINING CHARACTERISTICS
DIAGNOSTIC TESTS
MORPHOLOGY
CLINICAL FEATURES
TREATMENT
PROGNOSIS
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- It is characterized by abnormal iron deposits in erythroblast mitochondria, producing ringed sideroblasts instead of healthy red blood cells.
- It can be hereditary or acquired. Hereditary types often have normocytic or microcytic anemia while acquired types are usually normocytic or macrocytic.
- Causes include genetic disorders affecting heme synthesis, alcohol use, vitamin deficiencies, and exposures like lead.
- Symptoms depend on severity of anemia but can include fatigue, weakness, and heart/organ damage from iron overload.
- Diagnosis involves blood tests showing elevated iron levels and ringed siderImmunopathology 6
Amyloidosis is a group of diseases caused by abnormal protein deposits in tissues. There are different types of amyloid proteins that can deposit, including immunoglobulin light chains (AL), serum amyloid A (AA), and beta-amyloid. The deposits disrupt organ function over time and can affect the kidneys, heart, liver, spleen, and tongue. Symptoms vary by the organs involved but may include kidney failure, heart failure, digestive issues, and enlarged tongue. The prognosis depends on the type and extent of amyloidosis. Treatment focuses on managing the underlying condition that causes protein deposition or targeting the amyloid deposits directly.
Amyloidosis
This document discusses amyloidosis, including:
- Amyloidosis occurs when proteins aggregate into insoluble fibrils called amyloid that deposit abnormally in tissues. Over 30 proteins can form amyloid fibrils.
- Deposition can result from excessive protein production, mutations causing improper folding, or defective degradation of extracellular proteins. Deposits damage tissues.
- The main types are AL amyloidosis from immunoglobulin light chains, AA amyloidosis from serum amyloid A, and ATTR amyloidosis from transthyretin.
- Amyloidosis can be systemic, affecting multiple organs, or localized to single organs. Common sites for biopsy include kidney, rectum, abdominal fat. Congo red staining demonstrates amyloid's pink
Amyloidosis
The document discusses amyloidosis, beginning with definitions, mechanisms of formation, and common characteristics. It classifies amyloidosis as either systemic or localized, acquired or inherited. The most common types discussed are AL and AA amyloidosis. AL amyloidosis is caused by immunoglobulin light chains and commonly affects the kidneys and heart. Treatment aims to reduce monoclonal protein production and use chemotherapy. AA amyloidosis is linked to chronic inflammatory conditions and deposits serum amyloid A protein, primarily affecting the kidneys. Treatment focuses on the underlying inflammatory disease.
Megaloblastic anaemia
ALL ABOUT VIT B12 DEFICIENCY ANAEMIA AND FOLIC ACID DEFICIENCY ANAEMIA BY STUDENTS OF IMS AND SH,BHUBANESWAR
1 edema
The document discusses edema and fluid balance in the body. It describes the normal circulation of fluid between blood and tissues, mediated by hydrostatic and oncotic pressures. Edema occurs when there is increased hydrostatic pressure, decreased oncotic pressure, increased capillary permeability, or impaired lymphatic drainage. Specific types of edema discussed include cardiac, hepatic, pulmonary, cerebral, and lymphatic edema. Sites of common edema and clinical significance are also reviewed.
Pathology of blood
This document summarizes various blood disorders that affect red blood cells. It begins by describing anemia of blood loss from acute hemorrhage or chronic blood loss. It then discusses hemolytic anemias, where red blood cells are destroyed faster than normal, including hereditary spherocytosis, sickle cell anemia, and thalassemia. Hereditary spherocytosis is caused by inherited defects in the red blood cell membrane. Sickle cell anemia results from a genetic mutation that causes hemoglobin to polymerize and distort the red blood cells into a sickle shape. Thalassemias are caused by mutations that decrease alpha or beta globin synthesis. The document also reviews impaired red cell production and other acquired
Megaloblastic anemia
Megaloblastic anemia is caused by a deficiency of vitamin B12 or folate, which are essential for DNA synthesis and the production of red blood cells. This leads to large, abnormally developed red blood cells seen in the bone marrow. Symptoms include anemia, fatigue, and neurological issues. Diagnosis involves blood tests to check vitamin B12 and folate levels. Treatment consists of lifelong vitamin B12 injections or high dose oral supplements to replenish stores, along with folate supplements for a period of time.
AMYLOIDOSIS
The document discusses amyloidosis and summarizes key information:
1) Amyloidosis occurs when amyloid proteins deposit abnormally in tissues, appearing pink and amorphous under microscopy. Amyloid shows apple-green birefringence with Congo red staining under polarized light.
2) Amyloid is composed mainly of fibril proteins that form beta-pleated sheets. The two major types are AL and AA amyloid.
3) Organs commonly affected include kidney, heart, liver, spleen and brain. Kidney amyloidosis often causes nephrotic syndrome. Diagnosis involves tissue biopsy and Congo red staining of deposits.
Amyloidoisis
Amyloidosis is caused by deposition of abnormal amyloid proteins in tissues, damaging their structure and function. There are different types depending on the precursor protein, but all amyloid proteins form insoluble fibrils with beta-pleated sheet structures. The two main types are primary amyloidosis associated with plasma cell dyscrasias and secondary amyloidosis linked to chronic inflammatory conditions. Amyloid deposits can affect many organs like kidneys, heart, liver and spleen, causing organ dysfunction. On staining, amyloid takes up Congo red dye and exhibits apple-green birefringence under polarized light microscopy.
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AMYLOIDDFHGDDSCBJUUFFFVVXFTGGVVBOSIS.pdf
This document provides an overview of amyloidosis, including:
- Amyloidosis is caused by the deposition of abnormal protein fibrils in tissues, which can damage organs.
- There are different types of amyloid proteins including light chains, serum amyloid A, and beta-amyloid.
- Amyloidosis can be primary (associated with plasma cell disorders), secondary (associated with chronic inflammation), hereditary, or localized.
- Organs commonly involved include the kidneys, heart, liver, spleen, and tongue. Deposits appear pink with Congo red staining and apple-green under polarized light.
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Amyloidosis is a condition characterized by the abnormal deposition of amyloid protein fibrils in tissues and organs. The fibrils form when normally soluble proteins misfold and aggregate extracellularly. Amyloidosis has many subtypes classified by the precursor protein involved, pattern of organ involvement, and hereditary versus inflammatory causes. Diagnosis involves tissue biopsy with Congo red staining to identify the apple-green birefringence of amyloid under polarized light, as well as immunohistochemistry to determine the subtype. Advanced imaging and molecular PET can also detect amyloid plaques in neurodegenerative diseases like Alzheimer's.
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- Amyloidosis is a group of diseases where an abnormal protein builds up in tissues and organs. This protein forms fibrils that disrupt normal function.
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Amyloidosis is a group of diseases characterized by abnormal protein deposits in tissues called amyloid. There are different types depending on the protein involved, including AL amyloid from plasma cells and AA amyloid from inflammatory conditions. The deposits disrupt tissue structure and function. The disease is diagnosed through biopsy showing amyloid's green birefringence with Congo red staining. Treatment focuses on the underlying cause when possible to stop further amyloid accumulation.
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This document provides an overview of amyloidosis, including:
- Amyloidosis is characterized by extracellular deposition of misfolded proteins that form insoluble fibrils, damaging tissues.
- There are different types classified by the misfolded protein involved, including AL, AA, and rare forms.
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This document summarizes cutaneous amyloidosis, beginning with an introduction defining amyloid and its classification. It then discusses the pathophysiology, epidemiology, and clinical features of localized cutaneous amyloidosis (papular, macular, nodular) and systemic amyloidosis (primary, secondary, hereditary). The key points are that amyloidosis involves the abnormal deposition of amyloid proteins which can occur locally or systemically, with localized forms involving the skin and systemic forms potentially affecting multiple organs. The clinical manifestations vary depending on the type and location of amyloid deposition.
Amyloidosis presentation
Amyloidosis refers to a group of protein misfolding diseases characterized by deposition of amyloid proteins in organs and tissues. The amyloid proteins form fibrils that take on a characteristic beta-pleated sheet structure and stain red with Congo red dye. There are two main types - AL amyloidosis involves deposition of immunoglobulin light chains and is associated with plasma cell disorders like multiple myeloma. AA amyloidosis involves serum amyloid A proteins and is secondary to chronic inflammatory conditions. Amyloid deposition damages tissues by compressing cells and restricting blood flow, commonly affecting the spleen, liver and kidneys. This can lead to organ failure and death if the underlying cause is not resolved.
Amyloidosis
Amyloidosis is a condition caused by deposition of abnormal extracellular protein fibrils in tissues, which damages organs and impairs function. It can be hereditary or associated with chronic inflammatory diseases. The abnormal proteins form fibrils with a characteristic beta-pleated sheet structure that takes up Congo red stain. The kidney is most commonly involved, which can lead to proteinuria and renal failure. Cardiac involvement also carries a poor prognosis. Diagnosis requires biopsy of affected tissues with staining to identify the amyloid deposits. The prognosis depends on the type and extent of organ involvement.
Amyloidosis in head and neck manifestation
This document summarizes amyloidosis, a condition characterized by extracellular deposition of fibrillary proteins. Amyloidosis can occur systemically or locally in organs. The deposition forms beta-sheet rich fibrils that take up Congo red dye, appearing apple-green under microscopy. Normally misfolded proteins are degraded, but in amyloidosis these quality control mechanisms fail, allowing accumulation. Systemic types include AL amyloidosis associated with multiple myeloma and AA amyloidosis in chronic infections/inflammation. Localized amyloidosis can affect the larynx in rare cases, presenting as slowly progressive dysphonia from diffuse thickening or discrete lesions.
Presentation1.pptx
This document outlines amyloidosis, a disease characterized by abnormal protein deposits in tissues. Amyloidosis has several subtypes depending on the type of misfolded protein involved. The deposits have characteristic staining properties including apple-green birefringence under polarized light when stained with Congo red. Clinically, amyloidosis can affect many organs, with kidney, heart and liver among the most commonly involved. Deposits in organs like kidney can lead to nephrotic syndrome and renal failure. The prognosis depends on the extent and location of protein deposits in the body.
What is amyloidosis
Amyloidosis is a group of diseases characterized by abnormal protein deposits in tissues and organs. The protein deposits are called amyloid and can damage organs such as the heart, kidneys, liver, spleen, nervous system, and gastrointestinal tract. There are different types of amyloidosis depending on the type of protein deposited. The deposition of amyloid proteins is due to their abnormal folding and aggregation outside cells. Normally protein quality control mechanisms degrade misfolded proteins, but in amyloidosis this fails, causing damage as amyloid builds up in tissues over time. Clinical features vary depending on the organs affected but can include weakness, weight loss, organ enlargement, and organ dysfunction.
Amyloidosis.pptx
Amyloidosis is a condition characterized by the pathological deposition of amyloid protein in tissues and organs. Amyloid forms fibrils that stain with Congo red and show green birefringence under polarized light. There are two main types - primary amyloidosis resulting from plasma cell dyscrasias and secondary amyloidosis associated with chronic inflammatory conditions. Deposition of amyloid fibrils interferes with organ function and can lead to organ failure of the liver, kidneys, heart and other tissues over time.
Classification of Amyloidosis
Amyloidosis is a condition associated with a number of inherited and inflammatory disorders in which extracellular deposits of fibrillar proteins are responsible for tissue damange and functional compromise. (Robbins Basic Pathology, 9th Edition)
The following slideshow deals with the classification of Amyloidosis:
Amyloidosis
Amyloidosis is caused by abnormal protein deposits in tissues and organs. There are two main types of amyloid proteins that comprise amyloid deposits: fibril proteins (95%) and non-fibrillar components (5%). Amyloidosis can be systemic, affecting multiple organs, or localized affecting one or two sites. Diagnosis involves biopsy of affected tissues to identify the type of amyloid protein involved. Treatment seeks to suppress amyloid protein development and depends on the type and extent of amyloidosis.
Amyloidosis - pathophysiology (PHARM D)
Amyloidosis is a group of diseases characterized by deposition of abnormal fibrillar proteins in tissues and organs. The document discusses the physical and chemical nature of amyloid, including that it is composed mainly of fibril proteins arranged in beta-pleated sheets, as well as non-fibrillar components. It describes the different types of fibril proteins that can compose amyloid deposits, including immunoglobulin light chains (AL), serum amyloid A (AA), and others. The document provides details on the staining characteristics, diagnosis, morphologic features in organs, and prognosis of amyloidosis.
Amyloidosis of kidney. Morphological characteristics, outcomes, complications
Amyloidosis of kidney. Morphological characteristics, outcomes, complicationsSemey State Medical University
The document discusses amyloidosis of the kidney, including its morphological characteristics, outcomes, and complications. It describes the types and classifications of amyloidosis, the microscopic and macroscopic appearance of amyloid deposits in the kidney, the development stages of renal amyloidosis from latent to nephrotic to uremic, and common complications such as infections. The document contains a detailed plan and sections on the introduction, characteristics, development, complications, and microscopic/macroscopic descriptions of renal amyloidosis.Amyloidosis 2
This document discusses amyloidosis, including its pathogenesis, classification, and specific entities. The basic mechanism involves the abnormal folding and accumulation of proteins into fibrils, which can damage tissues through pressure effects, vessel wall infiltration, and cytotoxicity. Amyloidosis is classified as either generalized/systemic, involving multiple organs, or localized, affecting a single tissue. Specific entities discussed include reactive systemic amyloidosis associated with chronic inflammation; hemodialysis-associated amyloidosis involving beta-2 microglobulin; and hereditary forms like familial Mediterranean fever and familial amyloidotic neuropathy.
Amyloid aware booklet
There are several types of amyloidosis classified according to the precursor protein involved. The most common type, AL amyloidosis, arises from plasma cells in the bone marrow producing abnormal immunoglobulin light chains. Familial amyloidosis can be inherited and results from mutations in proteins like transthyretin. Secondary amyloidosis, such as AA amyloidosis, develops due to chronic inflammatory conditions and causes amyloid to deposit in the kidneys and liver. Early and accurate diagnosis of the specific type of amyloidosis is important for determining appropriate treatment.
Renal amyloidosis
Amyloidosis is characterized by the deposition of insoluble protein fibrils in tissues. There are different types based on the precursor protein, such as immunoglobulin light chain (AL), serum amyloid A (AA), and transthyretin (ATTR). In the kidney, amyloid deposits can involve the glomeruli, vessels, tubules, and interstitium. On microscopy, amyloid appears as an eosinophilic hyaline material that shows apple-green birefringence under polarized light after Congo red staining. Typing is important for management and involves immunohistochemistry for different precursor proteins. Treatment involves controlling the underlying condition driving amyloid formation and may include chemotherapy, transplantation, or controlling inflammation.
5. amyloidosis dr. sinhasan, mdzah
Amyloid is an abnormal protein that aggregates into unbranched fibrils. It is caused by misfolding of normal or mutant proteins. There are different types classified by the precursor protein such as AL, AA, and Aβ. Amyloidosis involves deposition of amyloid fibrils in tissues and organs which can cause organ dysfunction. Diagnosis involves staining methods like Congo red that show apple-green birefringence under polarized light. Biopsies of affected tissues may be needed to confirm amyloidosis.
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Title: Sense of Smell
Presenter: Dr. Faiza, Assistant Professor of Physiology
Qualifications:
MBBS (Best Graduate, AIMC Lahore)
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Describe the primary categories of smells and the concept of odor blindness.
Explain the structure and location of the olfactory membrane and mucosa, including the types and roles of cells involved in olfaction.
Describe the pathway and mechanisms of olfactory signal transmission from the olfactory receptors to the brain.
Illustrate the biochemical cascade triggered by odorant binding to olfactory receptors, including the role of G-proteins and second messengers in generating an action potential.
Identify different types of olfactory disorders such as anosmia, hyposmia, hyperosmia, and dysosmia, including their potential causes.
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Olfactory Genes:
3% of the human genome accounts for olfactory genes.
400 genes for odorant receptors.
Olfactory Membrane:
Located in the superior part of the nasal cavity.
Medially: Folds downward along the superior septum.
Laterally: Folds over the superior turbinate and upper surface of the middle turbinate.
Total surface area: 5-10 square centimeters.
Olfactory Mucosa:
Olfactory Cells: Bipolar nerve cells derived from the CNS (100 million), with 4-25 olfactory cilia per cell.
Sustentacular Cells: Produce mucus and maintain ionic and molecular environment.
Basal Cells: Replace worn-out olfactory cells with an average lifespan of 1-2 months.
Bowman’s Gland: Secretes mucus.
Stimulation of Olfactory Cells:
Odorant dissolves in mucus and attaches to receptors on olfactory cilia.
Involves a cascade effect through G-proteins and second messengers, leading to depolarization and action potential generation in the olfactory nerve.
Quality of a Good Odorant:
Small (3-20 Carbon atoms), volatile, water-soluble, and lipid-soluble.
Facilitated by odorant-binding proteins in mucus.
Membrane Potential and Action Potential:
Resting membrane potential: -55mV.
Action potential frequency in the olfactory nerve increases with odorant strength.
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Rapid adaptation within the first second, with further slow adaptation.
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Camphoraceous, Musky, Floral, Pepperminty, Ethereal, Pungent, Putrid.
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Behavioral and emotional influences of smell.
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From olfactory cells to glomeruli in the olfactory bulb, involving lateral inhibition.
Primitive, less old, and new olfactory systems with different path
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Selection of food based on metabolic needs
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Taste buds on the tongue
Influence of sense of smell, texture of food, and pain stimulation (e.g., by pepper)
Primary and Secondary Taste Sensations:
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Interaction of taste substances with receptors on microvilli
Signal transduction pathways for Umami, Sweet, Bitter, Sour, and Salty tastes
Taste Sensitivity and Adaptation:
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Rapid adaptation of taste sensation
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Dissolution of tastants to reach receptors
Washing away the stimulus
Taste Preferences and Aversions:
Mechanisms behind taste preference and aversion
Influence of receptors and neural pathways
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Degeneration of taste buds if the sensory nerve fiber is cut
Abnormalities of Taste Detection:
Conditions: Ageusia, Hypogeusia, Dysgeusia (parageusia)
Causes: Nerve damage, neurological disorders, infections, poor oral hygiene, adverse drug effects, deficiencies, aging, tobacco use, altered neurotransmitter levels
Neurotransmitters and Taste Threshold:
Effects of serotonin (5-HT) and norepinephrine (NE) on taste sensitivity
Supertasters:
25% of the population with heightened sensitivity to taste, especially bitterness
Increased number of fungiform papillae
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3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. Chapter 3, Cardiology Explained, https://www.ncbi.nlm.nih.gov/books/NBK2214/
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Amyloidosis
- 1. AMYLOIDOSIS 94 ANANYA JOHN 96 P SRI SAI SANJANA
- 2. AMYLOIDS • Misfolded proteins that deposit in extracellular spaces. • Can be associated with inherited/inflammatory disorders. • Deposits cause tissue damage. • “Amyloids” because staining characteristics resemble amylose • With progressive accumulation, amyloids can encroach & cause pressure necrosis on adjacent cells.
- 3. CHARACTERISTICS • Multiple proteins can aggregate to form amyloid. (It doesn’t have to be only 1 type of protein) • Aggregated proteins usually have cross ß pleated sheath configuration. • This makes them pick up Congo Red stain. • Have Apple Green birefringence under polarized light.
- 4. Source: Pathoma – Fundamentals of Pathology CONGO RED STAIN Amyloid deposits Blood vessel
- 5. Source: Pathoma – Fundamentals of Pathology APPLE GREEN BIREFRINGENCE
- 6. PATHOGENESIS • Generally, misfolded proteins are degraded Intracellularly: in proteosomes Extracellularly: in macrophages • In amyloidosis, these degradation mechanisms fail.
- 7. CLASSIFICATION Amyloidosis Systemic Localized Primary Secondary Involving multiple organ systems Involving only 1 organ Ex: Immunoglobulin light chain amyloidosis Ex: Reactive systemic amyloidosis Ex: • Medullary carcinoma of thyroid • Senile cardiac amyloidosis Hemodialysis associated amyloidosis
- 8. IMMUNOGLOBULIN LIGHT CHAIN AMYLOIDOSIS (PRIMARY) • Deposition of AL amyloids. • Derived from Ig light chains. • Plasma cell abnormalities Abnormal overproduction of light chains Deposition • Not all free chains produce amyloids. Amyloidogenic potential of a light chain is determined by its specific amino acid sequence.
- 9. REACTIVE SYSTEMIC AMYLOIDOSIS (SECONDARY) • Deposition of AA protein • Derived from SAA protein • SAA is an acute phase reactant, i.e., its levels rise in chronic inflammation • Ex: Rheumatoid arthritis, Ankylosing spondylitis, Crohn’s disease, Ulcerative colitis, etc. • Infections associated with pricking of skin in narcotic use can inc. risk of amyloidosis. AA levels rise
- 10. FAMILIAL MEDITERRANEAN FEVER • Autoinflammatory syndrome • Inc. cytokine IL-1 production • Attacks of fever along with inflammation of serosal surfaces is seen. Rashes can also be present. Inc. IL-1 Inc. SAA Inc. AA Amyloidosis
- 11. HAEMODIALYSIS ASSOCIATED AMYLOIDOSIS Long term hemodialysis • In the past, B2- microglobulin could not be filtered through dialysis membranes, and was retained in circulation. With new dialysis filters, this complication has been reduced. B2 microglobulin deposition Joints, muscles, tendons/ligaments affected Common presentation: Carpal Tunnel Syndrome
- 12. LOCALIZED AMYLOIDOSIS 1. Senile cardiac amyloidosis – non-mutated serum transthyretin deposited 2. Medullary carcinoma of thyroid – Procalcitonin deposited 3. Alzheimers – Aß protein gets deposited. Precursor: Amyloid precursor protein 4. Other endocrine amyloids – seen in Islets of Langerhans in Type 2 DM, pheochromocytoma.
- 13. CLINICAL FEATURES • Renal amyloidosis – Proteinuria, nephrotic syndrome • Cardiac amyloidosis – Congestive heart failure • Gastrointestinal amyloidosis – Generally asymptomatic • Vascular amyloidosis – Vascular fragility
- 14. NORMAL GLOMERULUS GLOMERULUS AFFECTED BY AL AMYLOIDOSIS
- 15. TESTS • Tissue biopsy • Abdominal fat pad and rectum are easily accessible • Biopsy of bone marrow/affected organ can also be taken • Echocardiogram (for heart related)
- 16. TREATMENT MEDICATIONS: • Chemotherapy and blood thinners SURGICAL: • Autologous blood stem cell transplant • Dialysis – If kidney is affected • Organ transplant – in cases of severe damage
- 17. Source: Robbins & Cotran Pathological Basis of Disease OVERVIE W:
- 18. REFERENCES • Robbins & Cotran Pathological Basis of Diseases • Pathoma: Fundamentals of Pathology
- 19. THANK YOU