Save Life Amyloidosis Trough Multiple Myeloma

Nonfiction, Science & Nature, Science
Cover of the book Save Life Amyloidosis Trough Multiple Myeloma by Maurice Vahedifar, D.M.D., M.S., Lulu.com
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Author: Maurice Vahedifar, D.M.D., M.S. ISBN: 9781365660573
Publisher: Lulu.com Publication: January 5, 2017
Imprint: Lulu.com Language: English
Author: Maurice Vahedifar, D.M.D., M.S.
ISBN: 9781365660573
Publisher: Lulu.com
Publication: January 5, 2017
Imprint: Lulu.com
Language: English
Amyloidosis comprises a group of disorders of diverse etiology, in which different proteins undergo abnormal folding, leading to their deposition in tissues and concomitant tissue toxicity. Amyloidosis is diseases characterized by deposits of altered proteins in the tissues. The amyloid deposit is always extracellular and presents a fibrillary conformation. 85% of the amyloid protein is constituted of a specific protein of each variety of amyloidosis, while the other 15% consists of other proteins and glycoproteins common to all types of amyloidosis. The same amyloid protein can be associated with various clinical forms and, inversely, different proteins can give the same clinical expression. It is therefore preferable to adopt a biochemical classification of amyloidosis. This classification is based on the identification of the various amyloid proteins by immunohistochemically analysis.
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Amyloidosis comprises a group of disorders of diverse etiology, in which different proteins undergo abnormal folding, leading to their deposition in tissues and concomitant tissue toxicity. Amyloidosis is diseases characterized by deposits of altered proteins in the tissues. The amyloid deposit is always extracellular and presents a fibrillary conformation. 85% of the amyloid protein is constituted of a specific protein of each variety of amyloidosis, while the other 15% consists of other proteins and glycoproteins common to all types of amyloidosis. The same amyloid protein can be associated with various clinical forms and, inversely, different proteins can give the same clinical expression. It is therefore preferable to adopt a biochemical classification of amyloidosis. This classification is based on the identification of the various amyloid proteins by immunohistochemically analysis.

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