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    Oral Pathology Amylodosis

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    This is a seminar on AMYLODOSIS

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    Oral Pathology Amylodosis

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    ms.sathe35
    4 views13 pages
    This is a seminar on AMYLODOSIS

    Original Title

    ORAL PATHOLOGY AMYLODOSIS

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    This is a seminar on AMYLODOSIS

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    4 views13 pages

    Oral Pathology Amylodosis

    Uploaded by

    ms.sathe35
    This is a seminar on AMYLODOSIS

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    of 13

    ORAL PATHOLOGY

    SEMINAR : AMYLOIDOSIS

    Submitted by: satheerdhya M S


    Year of study: third year
    Roll no: 160020788
    CONTENTS
    INTRODUCTION

    CLASSIFICATION

    STRUCTURE

    SYMPTOMS AND CAUSES

    CLASSES OF AMYLODOSIS

    CHEMICAL COMPOSITION

    COMPLICATIONS

    ORAL MANIFESTATION

    HISTOLOGY AND STAINS

    DIAGNOSIS

    TREATMENT

    CONCLUSION
    AMYLOIDOSIS
    INTRODUCTION
    Amyloid is an abnormal proteinaceous substance that is deposited
    between cells in tissues and organs of the body in a variety of clinical
    disorders. This amyloid build up can make the organs not work
    properly.

    Using routine stains, it is seen as an intercellular pink translucent


    material by light microscopy. Despite its morphologic uniformity, it is
    quite clear that amyloid is a complex material with at least two
    distinct forms ( type A and type B).

    CLASSIFICATION OF AMYLOIDOSIS
    . Primary amyloidosis
    . Reactive systemic amyloidosis

    . Hemodialysis associated amyloidosis

    . Localized amyloidosis

    . Endocrine amyloidosis

    . Amyloid of amyloidosis
    STRUCTURE OF AMYLOID

    By electron microscopy, X-ray crystallography and infrared


    spectroscopy, amyloid appears to by a made up largely of non
    branching fibrils with a characteristic “ beta pleated sheet
    conformation”, which is unique among mammalian fibrillar proteins.
    SYMPTOMS
    Symptoms can vary depending on which organs are affected.

    .Severe fatigue and weakness

    . Shortness of breath

    .Numbness, tingling or pain in the hands or feet

    .Swelling of the ankles and legs

    .Diarrhea, possibly with blood or constipation

    .An enlarged tongue, with sometimes looks rippled around edge

    .Skin changes, such as thickening or easy bruising and purplish


    patches around eye.

    CAUSES
    There are many different types of amyloidosis. Some types are
    hereditary, others are caused by outside factors, such as
    inflammatory disease or long term dialysis, may effect multiple
    organs other affect only one part of the body

    TYPES OF AMYLOIDOSIS INCLUDE:

    .AL amyloidosis (immunoglobulin light chain amyloidosis)

    .AA amyloidosis

    .Hereditary amyloidosis (familial amyloidosis

    .Wild-type amyloidosis

    .Localized amyloidosis
    CLASSES OF AMYLOIDOSIS
    Two major classes of amyloid identified include amyloid light chain
    (AL), composed if immunoglobulin light chain, amyloid associated
    (AA), made up of non immunoglobulin protein.

    Type A (secondary) amyloid.

    Type A amyloid is a fibrillar protein of unknown origin that is seen in


    prolonged inflammatory disease, genetic disease and symptoms such
    as familial Mediterranean fever.

    Type B (primary) amyloid

    Is thought to be immune origin because of its sequence hemology


    with the NH2 terminal end of immunoglobulin. Light chains
    commonly seen in patients with multiple myeloma and
    macroglobulinemia. Clinically asymptomatic patients are found to
    have type b amyloid serum and urine immunoglobulin abnormalities.

    Type C amyloid

    Includes, amyloid of ageing, localized non specific amyloid, amyloid


    adjacent to amine precursor uptake and decarboxylase (APUD)
    Tumors, that is, pheochromocytoma.
    CHEMICAL COMPOSITION Chemical composition and structure
    of human amyloid is high until 36 forms of this protein have been
    identified.

    DISEASE ASSOCIATED WITH AMYLOID

    The most common disease predisposing to amyloidosis are collagen


    diseases particularly rheumatoid arthritis, chronic infections such as
    tuberculosis and osteomyelitis, regional enteritis, ulcerative colitis
    and certain malignant disease particularly multiple myeloma,
    Hodgkin disease and renal cell carcinoma.

    Since modern surgery and medicine have largely eliminated chronic


    superlative diseases, rheumatoid arthritis and myeloma are now
    chief predisposing causes of amyloidosis.

    RISK FACTORS

    Factors that increase the risk of amyloidosis include.

    AGE: Most people diagnosed with amyloidosis are between ages 60-
    70.

    SEX: Men is more commonly affected

    OTHER DISEASE: Having chronic infections or inflammatory disease


    increases the risk of AA amyloidosis.

    FAMILY HISTORY: Some types of amyloidosis is hereditary

    KIDNEY DISEASE: Dialysis can’t always remove large protein from the
    blood. If you are on dialysis abnormal protein can build up in your
    blood and eventually be deposited in tissue. This condition is less
    common with more modern dialysis techniques.
    RACE: People of African descent appear to be higher risk of carrying a
    genetic mutation associated with a type of amyloidosis that can
    harm the heart.

    COMPLICATIONS
    Amyloidosis can seriously damage the:

    HEART: Amyloid reduces the hearts ability to fill with blood between
    heartbeats. Less blood is pumped with each heartbeat. This can
    cause shortness of breath. If amyloidosis is effects hearts electrical
    system, its can causes heart rhythm problems and can become life
    threatening.

    KIDNNEY: Amyloid can harm kidneys filtering system, this effects


    their ability to remove waste products from the body. It can
    eventually cause kidney failure.

    NERVOUS SYSTEM: Nerve damage can cause pain, numbness or


    tingling of the fingers and feet. If amyloid effects the nerves that
    control bowel function, it can cause periods of alternating
    constipation and diarrhea. Damage to the nerves that control blood
    pressure can make people feel faint, if they stand up too quickly.

    ORAL MAIFESTATION
    Oral manifestation of systemic amyloidosis most commonly involves
    the tongue.

    . amyloid deposition in the tongue results in macroglossia. It has


    been suggested that amyloidosis of the tongue be considered a
    paraneoplastic manifestations of some underlying plasma cell
    dyscrasias, particularly myeloma.

    . commonly appreciated in gingiva, because of commonly reported


    frequency of amyloid in gingival tissue, it has often been
    recommended that gingival biopsy convenient for diagnosis.

    . In recent types of amyloidosis labial mucosa is used as a source


    tissue for histological examination foe the detection of amyloid.

    .Xerostomia and xeropthalmia is reported in patients as a result of


    infiltration of amyloid protein into the salivary and lacrimal glands.

    HISTOLOGY
    HISTOLOGY AND STAINS USED IN AMYLOIDOSIS

    Amyloidosis may or may not be appear on microscopic examination.


    However, when the cut surface of suspected organ is painted with
    iodine and sulfuric acid, a peculiar mahogany brown staining of
    amyloid deposit is revealed. If large amount of amyloid are
    accumulated, then the affected organ is frequently enlarged and the
    tissue appears gray with a waxy firm consistency.

    Histologically, the deposition always begins between the cells and


    eventually surrounds and destroys the trapped native cells. However,
    quite recently a unique histological presentation of amyloidosis has
    been reported, the amyloid protein was seen to be present
    intracellularly within the striated muscle cell of buccal mucosa.

    Amyloid in microscopic sections of the involved tissue appears as


    hyalinized, homogeneous material, often perivascular in distribution,
    especially in the immune associated form. It is best demonstrated by
    using special stains such as Congo red and Crystal violet or by
    Thioflavin T fluorescent technique.

    Under polarized light, the Congo red stained amyloid shows green
    birefringence. This reaction is shared by all forms of amyloid and is
    due to the crossed beta pleated configuration of amyloid fibrils.

    AA and AL amyloid can be distinguished in histological sections. AA


    protein loses affinity to Congo red after incubation of tissue sections
    with potassium permanganate whereas AL protein do not. The
    Crystal violet, which stains similarly, positive staining is noted with
    the fluroscent dye, thioflavin T. In suspected case of amyloidosis,
    diagnostics workshop should include evaluation of serum and urine
    protein electrophoresis and immunoelectrophoresis.

    DIAGNOSIS
    Early can help prevent further organ damage.

    LABORATORY TESTS

    Blood and urine may be analyzed for abnormal protein that can
    indicate amyloidosis people with certain symptoms may also need
    thyroid and kidney function test.

    BIOPSY

    A tissue sample can be check for amyloidosis. The biopsy can be


    taken from the fat under the skin on the abdomen or from bone
    marrow. Some people may need a biopsy of an affected organ, such
    as liver and kidney.

    IMAGING TESTS

    .Echocardiogram
    .Magnetic resonance imaging (MRI)

    .Nuclear imaging

    helps to distinguish between different types of amyloidosis


    which can guide treatment decisions.

    TREATMENT
    There is no cure for amyloidosis. But treatment can help manage
    signs and symptoms and limit further production of amyloid protein.
    If amyloidosis has been triggered by another conditions, such as
    rheumatoid arthritis or tuberculosis, treating the underlying
    condition can be helpful.

    MEDICATIONS

    CHEMOTHERAPY: some cancer drugs are used in AL amyloidosis to


    stop the growth of abnormal cells that produce protein that forms
    amyloid.

    HEART MEDICATIONS: blood thinner to reduce the risk of clots,


    medication to control heart rate, drugs that increase urination can
    reduce the strain of your heart and kidney.

    TARGETED THERAPIES: drugs such as patisiran (onpattro) and


    inotersen (Tegsedi) can interfere with the commands send by faulty
    genes that create amyloid. Other drugs such as tafamidis (Vyndamax,
    vyndaqel) and diflunisal can stabilize bits of proteins in the blood
    stream and prevent them from getting transformed into amyloid
    protein.

    SURGICAL AND OTHER PROCEDURE: Autologous blood stem cell


    transplant, Dialysis, Organ transplant
    CONCLUSION
    Amyloidosis is a chronic disorder affecting several organs with
    significant associated morbidity and mortality. Although it is
    incurable, certain types of amyloidosis have a better prognosis than
    other. Advances in the underlying the molecular mechanisms
    involved in amyloid formation and tissue damage have stimulated
    outgoing research in novel treatment strategies. Diagnosis and early
    initiation of treatment in some cases may improve the outcome.
    REFFERENCE
    .Shafer’s oral pathology textbook
    .Mayoclinic Article

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