The condition is rare and caused by the accumulation of amyloid proteins in the tissues.
There are a few different types of the disease and their symptoms are varied, depending on which organs are affected (ranging from abdominal pain to heart failure).
The diagnosis, after suspicion, is simple, but due to the large number and variety of symptoms that may present, the suspicion does not always appear immediately.
There is no sure cure for the disease and its intensity is extremely variable. In some cases, the disease may not even show symptoms, while in others it can be fatal.
Although there are situations in which it can be cured, treatment is usually ineffective and consists of controlling the effects of the protein (treating secondary conditions). The best results are obtained when the disease is treated at the beginning, before affecting the heart, for example, which is usually fatal.
Approximately 50,000 people are affected by amyloidosis each year.
There are about 25 different types of amyloidosis, each differentiated from the other by the type of amyloid protein present. Most of them are very rare, and several have extremely similar manifestations. The four most common types are as follows:
This type of amyloidosis is called AA because of serum amyloid protein A, Reactive Amyloidosis or Secondary Amyloidosis (as it is always the result of a condition that causes chronic inflammation), being the most common type of the disease.
When there are inflammations in our body, serum amyloid A increases in our body. With chronic inflammation (that is, lasting weeks or months), it is always present and increasing, which leads to build-ups over time.
Accumulation usually begins in the kidneys, but it is common for other organs to be affected over time.
Type AA amyloidosis is the only one that causes childhood amyloidosis as a result of juvenile rheumatoid arthritis (which is a chronic inflammation).
Interestingly, although the disease appears in response to chronic inflammation (such as arthritis), it is extremely rare in people with lupus erythematosus, which is a chronic inflammation, and no one knows why.
It is important to note that subtype AA is not the only one classified as secondary amyloidosis (other subtypes can also be caused by non-inflammatory diseases), but it is the most common subtype and is necessarily due to chronic inflammation.
Type AL amyloidosis is caused by the immunoglobulin light chain amyloid protein . This type of disease is called primary amyloidosis , which means that it is not normally caused by another condition, at least at first.
However, it turns out that AL amyloidosis is caused by plasma cell dyscrasias , a type of failure in some cells of the immune system, the plasma cells, which are produced in the bone marrow.
It is worth mentioning that the cause cannot always be identified and, even when it can, AL amyloidosis is still called primary.
The dyscrasia that most often causes AL amyloidosis is multiple myeloma , a type of plasmacytic cancer .
Caused by the amyloid protein Transtirretina , this is the most common genetic version (among the several). It is also called familial amyloidosis. It usually manifests itself from middle age.
The protein, known as pre-albumin , is produced in the liver and has functions related to thyroid hormone (such as regulating metabolism, heart rate and blood filtration, among others) and vitamin A.
When it has problems, it can cause manifestations in several organs, especially the nervous system and the heart. It can even affect the eyes.
Interestingly, it is a version of the disease whose progression can be prevented through a liver transplant, which in turn begins to produce the protein correctly.
The fourth subtype among the most common involves the amyloid protein Beta-2-Microglobulin .
The version of the disease is also called amyloidosis associated with dialysis because it is exclusive to those undergoing hemodialysis, as some toxins are not adequately filtered by the procedure, which can result in the accumulation of amyloid in the organs.
A few years ago, a type of filter was used that was inefficient for some substances, which caused practically 100% of people who underwent hemodialysis for more than 15 years to develop Abeta-2-M amyloidosis.
Currently, filters that are better suited to their function make these toxins more efficiently eliminated.
Patients on hemodialysis for long periods are still at risk of developing amyloidosis, but the time it takes for this to happen is much longer than 15 years now.
Systemic amyloidosis is the most common among and most of the 25 types of the disease fit it.
In such cases, amyloid protein accumulates throughout the body. Often, specific organs are more affected than others, but over time, any place will accumulate.
The localized amyloid is specific to a region or organ. In this context, the accumulation of amyloid proteins does not occur throughout the body and, for diagnosis, it is not enough to examine any region in search of proteins.
This is the case, for example, of senile cardiac amyloidosis, which appears with age and is limited to the heart.
Frequent manifestations in the body
There are some types of amyloidosis that are worth mentioning. They are not separated here by the causative protein, but by the affected organ. Are they:
Cardiac amyloidosis is the accumulation of amyloid proteins in the heart. It is the most serious diagnosis possible since in most cases it manifests itself when the disease is not treated long enough for various organs, including the heart, to be affected.
Because of the accumulation of amyloid proteins, the heart muscle becomes hardened and weakened, which can cause problems that can be fatal.
The treatment of cardiac amyloidosis is extremely difficult as organ damage is often irreversible and fatal.
Heart transplantation is possible, but it usually poses a great risk since other organs may be damaged, which makes it difficult for the patient to survive when undergoing surgery.
Some medications can be used to relieve symptoms, but a cure is unlikely.
Cutaneous amyloidosis is a type of accumulation of amyloid proteins in the skin. It can present itself in different ways, one of the most famous being macular amyloidosis , which causes brown spots to appear on the skin in places where there is protein accumulation.
It can also be presented in other forms, such as nodules and the treatment is varied since it depends mainly on the type of amyloid protein.
Renal amyloidosis appears when the kidneys are affected by the accumulation of amyloid proteins. Usually the glomeruli (part of the kidneys responsible for filtering blood) are affected.
The result is usually kidney failure, as the organ fails to do its job properly, allowing toxins to stay in the body.
Kidney transplantation may temporarily resolve the problem, but if the cause is not treated, nothing prevents amyloid proteins from continuing to accumulate in the new kidney.
When the patient is affected by liver amyloidosis, the liver is being affected. The condition is usually associated with AA amyloidosis, but it is not exclusive to it.
In general, it is common for the gastrointestinal tract to also be affected.
The term cerebral amyloidosis is rarely used, but it represents the deposition of amyloid proteins in the brain. This type of amyloidosis is directly related to Alzheimer’s disease, which arises when there are deposits of beta-amyloid plaques in the brain.
It is extremely rare that amyloidosis is spontaneous, that is, without a cause. The different types of the disease, in turn, have different causes. Among the most common – but not unique – are:
Hemodialysis is a blood filtering process that is used when the kidneys have problems. Until a few years ago, hemodialysis filters used pores that were not able to eliminate all toxins.
In this case, the Beta-2-Microglobulin protein – which causes amyloidosis – ended up remaining in the body.
It takes a long time for it to accumulate enough to cause the disease, but virtually all hemodialysis patients had symptomatic kidney amyloidosis after 15 years of therapy.
Currently, filters with more suitable pores are used, but it is still not perfect and the disease only takes longer to appear.
This type of amyloidosis is very rare since it takes many years of hemodialysis for the protein to accumulate, but it happens.
It is believed that peritoneal dialysis, which uses the peritoneum (a membrane that covers the digestive organs and abdominal walls) as a filter, can also cause amyloidosis for the same reason, but it is not possible to do this type of dialysis for prolonged periods of time. time, which prevents amyloidosis from developing.
Inflammatory diseases are the major causes of AA amyloidosis. Inflammatory processes cause the body to produce amyloid proteins that can cause changes in the body.
The psoriatic arthritis , the rheumatoid arthritis and juvenile chronic arthritis are among the main causes. And of the 3, rheumatoid arthritis is the main cause of AA amyloidosis.
This is because synovial cells, which lubricate the joints and become inflamed because of rheumatoid arthritis, produce the protein responsible for AA amyloidosis when they are in this state.
The juvenile chronic arthritis in turn has the particularity of being almost always the cause of a possible child amyloidosis . The AA version of amyloidosis is the only one that affects children, precisely because of this version of arthritis.
Like arthritis, Crohn ‘s disease is an inflammatory condition. It can increase the production of amyloid proteins in the body, causing amyloidosis.
The tuberculosis is a long-term infection, which can cause inflammatory processes cause the accumulation of amyloid proteins that can trigger AA amyloidosis.
It is one of the main causes of the disease in regions where infections such as tuberculosis are able to spread easily.
The leprosy , and TB, is an infection that can cause various inflammatory processes that can result in the accumulation of amyloid proteins.
Like tuberculosis, it is more common in regions with less health resources, which facilitates the transmission of the disease and makes it more difficult to treat.
Plasmacytic dyscrasias are changes in plasma cells, responsible for the production of antibodies. They can manifest themselves through cancer, as is the case of multiple myeloma or leukemia of the plasma cells .
These changes are the causes of AL amyloidosis, which despite being frequently triggered by these diseases, is still called primary amyloidosis .
Some types of amyloidosis are genetic and are therefore called familial amyloidosis . A gene causes the high production of amyloid proteins that accumulate in the organs. This is the case of ATTR amyloidosis, the main one of familial amyloidosis.
Is amyloidosis contagious?
It is not possible to contract amyloidosis from another person. It is a change in the way your body produces, filters or metabolizes some proteins and it is not transmissible. There are some cases, however, in which contagious diseases can cause amyloidosis.
Among the contagious diseases that can trigger amyloidosis are leprosy , also known as leprosy, and tuberculosis .
Some factors increase the risk of developing amyloidosis. Are they:
Amyloidosis is a disease that is more likely to manifest itself in old age, from 50 years, since it takes time for the protein to accumulate in the organs and start to cause problems.
There is also a relationship between the ATTR type and the elderly, even in cases where there is no genetic history.
The only situation in which amyloidosis occurs in children is in the case of Juvenile Rheumatoid Arthritis.
Infection or chronic inflammatory diseases
Chronic infections or infections are largely responsible for amyloidosis. AA amyloidosis is always the result of chronic inflammation, so if you have any – arthritis or Crohn’s disease, for example – it’s important to keep an eye on.
Familial Mediterranean fever
The fever familiar Mediterranean is a rare inflammatory genetic disorder that usually affects people with offspring of the middle east and the Mediterranean region, such as Arabs, Turks, Lebanese, Italian and Greek.
It stands out from other inflammatory diseases for being responsible for approximately 60% of cases of secondary amyloidosis in the Middle East.
This type of cancer of the immune cells can be the cause of AL amyloidosis. About 10% of multiple myeloma patients develop an accumulation of amyloid proteins. The treatment for both is chemotherapy.
Since some types of the disease are genetic, if there are any cases in your family, your chances of developing the condition also increase in relation to the general population.
Finding out whether a relative’s version of amyloidosis is genetic can be relevant to whether you are in the risk group.
The symptoms of amyloidosis are nonspecific and varied. They depend on the organ or organs affected and are not always obvious. Amyloid protein deposits are often widespread , that is, they are present throughout the body.
This means that numerous combinations of symptoms can occur, which makes diagnosis of the disease very difficult, especially since basically all of these symptoms can be present in numerous other conditions.
The organs that can be affected and the most common symptoms are:
The presence of accumulation of amyloid proteins in the heart is extremely serious and severely limits patient survival. Some of the symptoms that can appear if the heart is affected are:
Thickening of the cardiac walls
This thickening happens because of the accumulation of amyloid protein in the heart, but it is misleading. Muscle tissue is actually stunted due to pressure, but the volume of proteins makes the heart appear larger.
The pectoris is a chest pain caused by reduced blood flow into the heart, which may be due to the hardening of the heart muscle because of amyloidosis.
Pain in the jaw.
Pain in the chewing muscles can present because of deposits of amyloid proteins in the carotid arteries.
The kidneys are usually affected by AA and AL amyloidoses and the glomeruli (the structure of the kidney that performs blood filtration) are the most affected by the condition. The signs that they are being hit are:
- Nephromegaly (enlarged kidneys).
In addition to these, there may also be:
Presence of protein in the urine that can generate several symptoms, manifesting swelling in the abdomen, eyes and feet, changes in appetite and changes in the urine (which becomes more foamy due to the presence of proteins).
The presence of amyloid proteins in the kidneys can cause blockages and clots in the renal veins (which carry blood out of the kidneys), which in turn can lead to thrombosis .
In general, symptoms are mild when the condition is chronic (that is, it develops gradually). However, in patients who have an acute (sudden) manifestation, back pain , fever, vomiting and blood in the urine may appear .
Gastrointestinal tract and liver
The presence of amyloid proteins in the liver and gastrointestinal system is often associated with AA amyloidosis. Symptoms include:
- Hepatomegaly (enlarged liver);
- Abdominal pain;
Rarely, amyloid proteins can cause blockages in the intestine, which can be total or partial, making it difficult or preventing evacuation.
In addition to reducing stool elimination, pain in the abdomen, nausea, vomiting and fever may appear.
It is possible that the body is not able to absorb all nutrients during digestion because of the presence of amyloid proteins.
The skeleton and muscles can also be affected by amyloidosis. The main signs are:
The swelling of the tongue is due to the presence of amyloid proteins growing between the cells, just as it happens in the heart, kidneys, liver and other organs. The volume gets bigger and sometimes the frequency of bites on the side of the tongue can be an indicator of this.
As in the tongue, heart, kidneys and liver, the patient’s muscles can be misleading due to the presence of amyloid proteins between cells.
They are also called “shoulder pads sign” or “shoulder pads sign”. Amyloid proteins can accumulate in the shoulders and soft tissues, making it look as if the patient has placed shoulder pads under the skin.
Although similar to muscle pseudohypertrophy, the shoulder pads are, in general, more prominent.
The growth of amyloid proteins in the bones can cause severe pain, as well as the apparent increase in bone mass.
The same growth of proteins in the bones can make them fragile, facilitating fractures.
There are situations in which the blood can be affected by amyloid proteins. The result of this may be the bleeding tendency:
Each amyloid protein has a greater affinity for a specific tissue. Several of them have an affinity with the coagulation Factor X, present in the blood.
This causes proteins to “sequester” these clotting factors, thereby increasing bleeding as clotting is reduced.
Normally, when it affects the lungs, amyloidosis has no symptoms. However, some of them may appear rarely:
Due to the accumulation of amyloid proteins in the vocal cords, hoarseness may occur, which may be associated with breathing difficulties and the feeling that there is something in the throat.
Recurrent pleural effusion
The pleural effusion occurs when fluid builds up between the chest and the lungs, reducing the body’s capacity expansion and making breathing difficult. It can often terminate because of amyloid proteins.
When there are amyloid deposits on the skin, they usually stay below the tissue and cause no symptoms. Skin thickening is possible, but it is rarely noticeable. However, a characteristic sign of amyloidosis is the sign of the trauma-free raccoon .
This sign is caused by bleeding under the skin, often around the eyes (which is why it is called the raccoon sign), and is usually a sign of a skull fracture. However, if there is no trauma, it is possible that there is amyloidosis.
Peripheral nervous system
Some extremely rare types of amyloidosis can affect the peripheral nervous system.
This is the case of Familial Paramiloidosis, also called PAF (Familial Amyloid Polyneuropathy), or foot disease, which gets its name because neuropathy causes atrophy of the feet.
When amyloidosis affects the peripheral nervous system, that is, the nerves, it can cause:
- Numbness and tingling;
- Difficulty in feeling temperatures;
- Muscle weakness;
- Heart palpitations;
- Constipation and diarrhea;
- Carpal tunnel syndrome (compression of a nerve in the wrist).
Central nervous system
AA and AL amyloidoses do not affect the central nervous system, but there is a so-called cerebral amyloidosis , which is the accumulation of beta-amyloid proteins in the brain.
It is important to note that amyloid proteins have their function in the human body. In the brain, so-called beta-amyloid proteins have a protective function. However, it is possible for them to form plaques and block electrical signals between neurons. This is how Alzheimer’s disease develops
How is amyloidosis diagnosed?
The diagnosis of amyloidosis is complicated because the disease is rare and its symptoms are also present in several other diseases. Although it is not difficult to diagnose the condition when it is suspected, it is rarely the first suspect.
This is because the disease can show many signs, but there is only one of them that certainly means amyloidosis: the presence of amyloid proteins in the tissue.
It is mandatory to have a biopsy, because without this confirmation, it is still possible that the symptoms are caused by something else.
Even in cases where a doctor is almost certain that the patient suffers from amyloidosis, a biopsy is necessary as there is always the possibility of being something else.
Biopsy is the removal of a piece of tissue for microscopic examination, and it is possible to find amyloid proteins in the tissue.
The most suitable place to perform the exam would be the affected organ, which is identified from the symptoms.
However, in the case of amyloidosis, there is a problem. The disease makes the organ it affects more susceptible to bleeding when punctured (cut or punctured). This happens because of the deposition of amyloid protein on the walls of blood vessels.
If a biopsy is performed on the organ, the risk of bleeding is high, causing other regions to be considered for the exam.
Since most amyloidoses are systemic , although certain organs have more prominent deposits, any part of the body will have deposits of amyloid protein, making it possible to collect samples from other tissues
The safest and most accurate place to take a sample is abdominal subcutaneous fat .
In addition, the rectal mucosa or samples of the salivary glands of the lips are also removed, as they are also safe and reliable in the diagnosis.
However, it is important to note that if none of these sites have amyloid proteins but the suspicion remains, biopsy of the organ directly involved is necessary, even with the risk of bleeding.
It may be the case of a localized amyloidosis, which will present deposits only in the affected organ and not in the whole body.
After the biopsy is performed and amyloidosis is confirmed, it is necessary to correctly identify the type of amyloid protein that is causing it. Each version has different treatments, so it is necessary.
They are used the techniques of immunohistochemistry as immunofluorescence and enzyme immunoassay .
Immunofluorescence uses specific dyes that dye only the proteins you are looking for, making them appear differently under the microscope. It is possible to identify most of the proteins that cause amyloidosis in this way.
The immunoenzymatic assay, also known as ELISA, immerses the sample cells in a liquid that changes color in the presence of a specific reaction, and then antibodies are added that react with the amyloid proteins.
With this reaction, the color change reveals the presence of a specific type of protein.
Although these methods are extremely accurate for identifying AA and ATTR amyloidoses, unfortunately the same is not true for the AL version.
The correct identification of AL amyloidosis is extremely important because its treatment is very aggressive, especially when compared to the treatments of the other versions.
If there is no confirmation of the type of protein using immunohistochemistry techniques, mass spectrometry must be performed , an examination that uses a light spectrum to identify the atomic mass of a material or the bone marrow biopsy (which consists of taking a tissue sample from the bone marrow).
However, if the person has amyloid deposits not identified by immunohistochemistry and at the same time has a cancer related to plasma cells, such as multiple myeloma or Waldenström’s macroglobulinemia, the diagnosis can be closed as LA.
Chemotherapy treatment will be indicated, since before anything else, the patient has cancer.
Is amyloidosis curable?
No , except in some cases of ATTR amyloidosis, as liver transplantation can stop the progression of the condition. But in general, amyloidosis is chronic and there is no cure for the condition, only treatments that can relieve symptoms and increase the patient’s survival time.
What is the treatment?
The treatment of amyloidosis depends on the type of amyloidosis. The options are as follows:
Secondary amyloidosis (AA)
In the case of secondary amyloidosis , the main method is to treat the condition that causes the disease, which can be complicated because not all causes are easy to treat.
When adequate treatment is not achieved, amyloidosis cannot be cured.
The treatments are numerous since the primary diseases are many. Fortunately, medicine has means of treatment for various diseases, including auto-inflammatory diseases, such as arthritis.
Primary amyloidosis (AL)
Unfortunately, the treatment of primary amyloidosis is aggressive and has low success rates when the disease is already advanced, which means that early diagnosis is extremely important.
However, when the condition is diagnosed early, despite the aggressiveness of the treatment, the chances of a cure are good.
AL amyloidosis happens because of a failure in the plasma cells , which are part of the immune system and are produced in the bone marrow.
For years, the treatment indicated was chemotherapy with the drug called melphalan , but even with this treatment, many patients ended up dying.
It turns out that melphalan is a very effective drug for controlling plasma cells, and higher doses than those normally used could be effective. The problem is that the drug is extremely toxic to the spinal cord.
Currently, there is an alternative that is more aggressive, but it works very well.
The Autologous Hematopoietic Cell Transplantation accompanied by very high doses of chemotherapy with melphalan is an option.
These cells, also called hematopoietic stem cells , are transferred from one person to another in a bone marrow transplant. But in this case it is different, as the transplant is autologous . This means that the transferred hematopoietic stem cells belong to the patient himself.
They are drawn from the patient’s blood, and then he undergoes high doses of melphalan chemotherapy. All altered plasma cells are destroyed, as well as healthy bone marrow cells .
This would normally mean the patient’s death, however the hematopoietic stem cells removed earlier are replaced in the body, thus completing a patient’s bone marrow transplant to himself.
As the cells were already the patient’s, the chances of rejection are minimal, as well as the side effects.
The big problem with this therapy is that it is too aggressive . If the patient is already weakened in any way, the chances of him surviving chemotherapy and transplantation are slim. Amyloidosis itself, if not in the beginning, can compromise organs like the heart.
In these cases, the treatment is chemotherapy with melphalan in normal doses, which still has a chance of cure and is not as aggressive.
Familial amyloidosis (ATTR)
Familial amyloidosis gets its name because it is a genetic disease, transmitted from generation to generation. Its cure is technically simple. Since what causes the disease is a liver that produces proteins in the wrong way, a liver transplant is enough .
The concept is simple, but in practice it is not that easy. Although liver transplantation solves the problem, since the new liver will not produce altered proteins, the risks are now related to the procedure itself.
There is the possibility of rejection of the organ, for example, which is always a concern with transplants. This without considering the difficulties related to finding a donor.
Beta-2-M amyloidosis, which is caused by hemodialysis, can also be resolved through a transplant. Abandoning dialysis solves the problem, and the best way to do this is through a kidney transplant .
So, instead of needing dialysis for blood filtration, a new kidney can do this.
In the case of localized amyloidoses, it is possible to perform transplants of the affected organ, surgical removal of the amyloid accumulations, in addition to using radiation to reduce the progress of the disease.
These solutions are not always permanent, but they can increase patient survival.
Medicines for amyloidosis
Several of the diseases that cause amyloidosis can be treated with medications. We list here some of the main ones, but not all of them, since there are many. Without knowing the cause of the disease, the drug cannot be selected. Are they:
- Melfalana ;
- Dexamethasone ;
- Colchicine ;
- Infliximab ;
- Etanercept ;
- Cyclophosphamide ;
NEVER self-medicate or stop using a medication without first consulting a doctor. Only he will be able to tell which medication, dosage and duration of treatment is the most suitable for his specific case. The information contained in this website is only intended to inform, not in any way intended to replace the guidance of a specialist or serve as a recommendation for any type of treatment. Always follow the instructions on the package insert and, if symptoms persist, seek medical or pharmaceutical advice.
Unfortunately, amyloidosis has no cure and the prognosis is not usually positive. Treatment can increase patient survival by controlling and alleviating symptoms, but in most cases, the disease is not cured.
The prognosis varies according to the type of amyloidosis and stage, considering which organs are affected.
One of the worst possible prognoses is that of cardiac amyloidosis , since it is common that when the heart is affected, other organs are also seriously compromised and treatments such as heart transplantation can represent high risks to the patient.
The affection of other organs can also result in risks to life, such as the impairment of the gastrointestinal system , which can considerably reduce their quality of life and cause the patient’s death.
When the kidneys are affected, hemodialysis may be necessary. Kidney transplantation is an option, but it does not prevent the disease from returning.
The most frequent risks of death related to amyloidosis occur when there is:
- Renal insufficiency;
- Cardiac arrhythmias;
- Gastrointestinal bleeding;
- Respiratory failure;
- Cardiac insufficiency;
The complications related to the various amyloidoses are numerous. Could have:
- Renal failure;
- Respiratory failure;
- Heart failure;
- Intestinal block;
- Carpal syndrome;
- Weight loss;
- Immunological problems;
- Muscle losses;
- Sexual impotence;
Complications are not necessarily linked to specific types of amyloidosis, but are more related to Organs affected organs. However, as it is common for the condition to be generalized, several of these complications can appear at the same time.
Treatment can help to reduce them, but it is not always possible to avoid them all. It all depends on the type of amyloidosis and how early it is detected.
How to prevent amyloidosis?
There is no adequate way to prevent amyloidosis. It can be genetic, caused by other diseases or spontaneous. Therefore, there is great difficulty in its prevention.
The important thing is to keep an eye out for symptoms and visit the doctor if any appear, especially if you are part of the risk groups. Treating autoinflammatory diseases is also very important because reducing your symptoms can decrease the chances of an amyloidosis.
Is amyloidosis cancer?
No , amyloidosis is not cancer.
Some cancers can cause amyloidosis, such as multiple myeloma. Cancer is a defective multiplication of our own cells. Amyloidosis is the accumulation of defective proteins produced by the body itself, which, when it is unable to filter them, accumulates them.
Unlike cancer cells, amyloid proteins are not cells, they are not alive and they do not reproduce.
Therefore, although amyloidosis is sometimes treated similarly to cancer, it is not.
Amyloidosis in Sharpei
The Sharpei is a breed of dog that can develop amyloidosis, due to another disease of the breed: Sharpei Fever .
This is a genetic autoinflammatory disease that affects the dog’s joints. There is no certainty, but some studies indicate the possibility that it is caused by hyaluronic acid, which is the same compound that causes the dog’s skin to have that characteristic wrinkled skin.
Inflammation, being chronic, can cause amyloidosis in the same way it does in humans. Therefore, it is important to treat the animal that develops Sharpei Fever to control inflammation and prevent amyloidosis in the dog.