Amyloidosis More Condition_treatment What Is Primary Amyloidosis With Cardiomyopathy?

What is primary amyloidosis with cardiomyopathy? - amyloidosis more condition_treatment

Background: Patients often with nonspecific symptoms such as weakness and weight loss. The symptoms depend on the current version of the TTR and the organ (s) in question. Amyloid deposits in a particular organ, leading to a corresponding clinical consequences, and therefore with similar complaints, regardless of the type of amyloid deposits. For example, cardiac symptoms and cause similar cardiac attr AL. The most common sites of deposition are:

* Participation in Cardiovascular --

Heart patients often deposit or symptoms of heart failure (eg, dyspnea, peripheral edema) and / or cardiac arrhythmia (eg palpitations, dizziness) syncope.

Deposition or in the sub-endothelium of peripheral vessels may cause severe orthostatic hypotension.

Background: Amyloidosis is a disease of protein secondary structure, which forms deposits of protein fibrils normally insoluble extracellular soluble, leading to organ failure. All types of amyloid fibrils contain a protein importantWhich defines the type of amyloid, in addition to the components of lesser importance. Twenty different fibril proteins have been described in human amyloidosis, each with a different picture (see Amyloidosis, overview). One of the 20 human proteins, the amyloid fibrils is transthyretin (TTR).

TTR is a serum protein that transports thyroxine and retinol-binding protein. It circulates as a tetramer of 4 identical subunits of every 127 amino acids. TTR earlier Prealbumin because it migrates anodally in serum protein electrophoresis, albumin, but this name is misleading, because TTR is not a precursor of protein. The TTR monomer contains 8 fields antiparallel beta sheet structure. TTR is mainly produced in the liver and the plexus and the retina. Its gene is located on chromosome 18, and consists of 4 exons.

Systemic amyloidosis is also a capital A (for amyloid called) by the abbreviation of the chemical identity of the fibril protein. For example, short attr TTR amyloidosis, amyloidosis, and immunoglobulin light type of string is the abbreviated form of the AHL.

Pathophysiology: Both TTR and variant TTR amyloidosis normal consequence of the form. Forms TTR cardiac amyloidosis normal order in which the elderly and is as senile cardiac amyloidosis (SCA). If one accepts that SCA is often due to microscopic deposits in many other organs, accompanied by another title for the systemic senile amyloidosis (SSA) has been proposed. Both terms are used frequently.

TTR mutations accelerate the process of TTR amyloid formation and the most important risk factor for the development of clinically significant ATTR. More than 85 amyloidogenic TTR variants cause systemic amyloidosis family. The time of onset of symptoms, the nature of the participation of agencies and the progression of the disease varies, but most mutations with heart disease and related / or participation and the nerves. The gastrointestinal tract, vitreous, and the wrist band are also frequently affected.

Amyloidogenic TTR mutations destabilize TTR-monomers or tetramers, and the molecule can easily make an amyloidogenic intermediate conformation. Another,unknown factors also play a role in the formation of amyloid TTR, because the clinical picture of the disease varies not only from individuals that have the same TTR variant.

When peripheral nerves are prominently affected, the disease is a family amyloid polyneuropathy (FAP). If the heart is heavily involved, but the nerves do not, the disease called amyloid cardiomyopathy Family (FAC). Whatever the body is much more general term is simply the nature of transthyretin amyloidosis, abbreviated Attr