Support and Information
The following sections provide information on prion disease, the services we offer and research into prion disease (CJD).
Prions and Prion Disease
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs) are a group of progressive neurodegenerative conditions. These illnesses exist in both animals and humans. Scrapie, a disease affecting sheep and goats, was the first prion disease to be identified in the 1730s. In more recent years other prion diseases have been seen in animals, including bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease (CWD) in deer. Various forms of the disease have been identified since Creutzfeldt and Jakob first described the illness later known as CJD (Creutzfeldt-Jakob disease) in the 1920s. These diseases in humans are now grouped together according to whether they are sporadic, inherited, or aquired.
Most cases of prion disease are sporadic; that is, they arise spontaneously for no known reason. More rarely prion disease is inherited due to a faulty gene, or acquired by medical procedures, transfusions, or contaminated food. Sporadic and inherited prion disease occurs worldwide in all populations. The incidence of sporadic CJD is around 1-2 per million of the population per annum resulting in a lifetime risk of 1 in 5000; males and females are equally affected. The incidence of the various acquired prion diseases, however, is more localised to specific groups and populations.
What Causes Prion Disease?
Prion diseases are associated with the build up in the brain (and some other organs) of an abnormal or ‘rogue’ form of a naturally occurring cellular protein, known as the prion protein. The rogue protein results from a change in shape of the normal prion protein. Once formed in the body these rogue proteins recruit and convert more of the normal prion protein into the abnormal form, setting off a kind of chain reaction which leads to a progressive accumulation of the rogue protein. In the normal course of events, once they have served their purpose, prion proteins are broken down by enzymes in the body. The abnormal prions however are more resistant to this process; so they accumulate and cause damage in the brain, which interferes with normal brain functioning. All forms of the disease are thought to be associated with an incubation period. This is a clinically ‘silent phase’ during which replication of the rogue protein is thought to be taking place.
The function of the normal form of the protein remains unclear, though it is thought they may possibly play a role in the transport of messages between specific brain cells (synaptic transmission), or the maintenance of cables around nerves.
Genetic Susceptibility
At present the most important and well defined genetic factor which influences the susceptibility of an individual to developing prion disease relates to a common variation in the prion protein gene itself. At a particular position in the prion gene known as codon 129, there are two possible genetic types, which in turn specify the body to produce different amino acids at this position. These amino acids are called methionine and valine, or M and V for short. In most countries, MM and MV frequencies in the population are roughly equal (40-50%). It has been known for some years that individuals, who are MV, are at much less risk of developing prion disease than are MM or VV individuals. Nearly all definite cases of vCJD have been MM. One definite patient and one suspected patient who did not have a post mortem, were MV.
Prion Disease and Infection Control
Prion disease is not contagious; there is no evidence to suggest it can be spread from person to person by close contact. Once a person has developed prion disease, central nervous system tissues (brain, spinal cord and eye tissue) are thought to be extremely infectious. However this is only relevant for those handling infected tissue directly, which does not include carers looking after a person with the disease.
Infectivity in the rest of the body varies in different types of prion disease but is generally much less than in brain tissue. People with any form of prion disease are requested not to be blood or organ donors, and are requested to inform their doctor and dentist prior to any invasive medical procedures or dentistry.
As prions cannot be completely destroyed by conventional sterilisation procedures, transmission has also occurred inadvertently through the use of surgical instruments previously used during neurosurgery on a person with sporadic prion disease. Current Department of Health guidelines are that all surgical instruments used on medium or high infectivity tissues in a patient with suspected prion disease are quarantined and not re-used unless an alternative diagnosis is confirmed. Instruments used on patients with known prion disease are not reused.
Guidelines about infection control can be found at the Advisory Committee for Dangerous Pathogens website.
The sporadic form of the disease, also known as sporadic Creutzfeldt-Jakob disease (CJD), or classical CJD, accounts for approximately 85% of all recognised prion disease. Sporadic CJD occurs in every country with a remarkably similar incidence: approximately one person in every million develops sporadic CJD per year.
What Causes Sporadic Prion Disease?
Sporadic prion disease occurs 'out of the blue', at random in the population. What initially triggers this 'chain reaction' in sporadic CJD is unknown, it may simply represent an unlucky event whereby this change occurs spontaneously in the brain and involves sufficient prion protein molecules to trigger off a self-sustaining process. An alternative hypothesis is that one or more cells in the body may have a mutation in the gene which encodes the prion protein and these cells then produce a faulty prion protein which will tend to form the rogue form spontaneously. This type of fault is called a 'somatic' mutation and is quite distinct from inherited mutations seen in the inherited prion diseases, where a faulty gene has been inherited from a parent (Refer to the inherited prion disease page). Somatic mutations are not passed on to children.
Characteristic Features of Sporadic Prion Disease
The disease usually affects people between the ages of 45-75, the average age of onset being around 65. The duration of the illness varies, for most people it is less than a year and may be as short as 6 weeks. For a minority, the illness duration can be up to 3 years.
Symptoms of the disease can vary though classically sporadic prion disease is recognised as a rapidly progressive dementia affecting many aspects of functioning. Typically there is an insidious onset followed by a very rapid decline.
Early non-specific symptoms may include dizziness, headaches, fatigue, sleep disturbance and weight loss. Behavioural symptoms such as mood swings and loss of interest may also be seen. Because of these initial symptoms the person may at first be thought to be suffering from depression or other psychiatric disease. Refer to the signs and symptoms page for further information.
Unusual Presentation of Sporadic Prion Disease
In a minority of people the illness can present in a different (atypical) way. A number of types of such atypical CJD are recognised; examples are of an illness in which the prominent features are a disturbance of balance and movement, or alternatively visual deterioration. Occasionally the disease will resemble a stroke, having an extremely sudden onset.
In inherited prion disease, also known as familial prion disease, a genetic mutation (fault in the gene that codes for the prion protein) causes abnormal prion proteins to be produced in the body, which themselves are predisposed to undergo the change in shape that leads to production of rogue proteins.
Genetics
The disease runs in families in what is known as an “autosomal dominant” pattern of inheritance. That is, each child who has a parent with inherited prion disease has a 50% chance of having the faulty gene. Those individuals, who do not inherit the mutation and are therefore unaffected, cannot pass the disease on to any of their children. This means that in any affected family it is possible that some; none or all of the offspring will inherit the illness.
Sometimes the disease will skip a generation. This can occur because someone with a mutation may die of an unrelated cause before the prion disease has developed, but after passing on the gene to their children. There is often considerable variation in the age of onset in different members of the same family and in some the onset may be so late that dying from another cause (unrelated to prion disease) is quite likely. It is possible that some individuals with certain mutations may not develop the disease at all even if they live to an advanced age.
The familial forms of the disease account for about 15% of human prion disease. A person with the faulty gene is most likely to develop symptoms between the ages of 30-75 and the duration of illness can vary from six weeks to over 10 years.
Prion Mutations
To date over 30 different mutations have been identified in the prion gene. Traditionally these have been named according to the doctors that first described the condition, as either inherited Creutzfeldt-Jakob Disease (CJD), Gerstmann-Straussler-Scheinker Disease (GSS) or Fatal Familial Insomnia (FFI).
Depending on which mutation has been inherited, there will be variation in the age of onset and duration of disease. To some extent each different fault will also produce a slightly different set of symptoms which characterises the illness in a specific way. However, even within the same family, all of whom would have the same genetic fault, the presentation of the illness may be very different.
Features of Inherited Prion Disease
Common features do exist between all three forms of the familial disease and for this reason these illnesses have more recently been classified as inherited prion disease, followed by the number associated with the particular mutation. For example, P102L, 6-OPRI or E200K. Initial signs are usually fairly subtle; fatigue, insomnia, weight loss, headaches and ill-defined pain sensations are sometimes the first signs of illness. Individuals may complain of altered sensations, for example, numbness, tingling or pain in the arms or legs. Refer to the signs and symptoms page for further information.
Diagnostic Testing
When prion disease is suspected a blood sample is taken to look for a genetic fault/mutation in the prion protein gene. It is also possible to extract DNA from a saliva sample, but blood is the preferred sample type, as it yields DNA more reliably. Because of the potential implications that the test may have, not only for the person being tested but also for any siblings, children and other family members, the doctor needs to obtain consent for this test.
Predictive Testing
It is possible to carry out the same test on adults who have no symptoms of the illness, but who have a parent or other close relative that has died of inherited prion disease. This test can determine whether a person is likely to develop the disease when they are older or not. The issues around genetic testing are complex and the decision of whether or not to proceed with the test is a difficult one. Genetic counselling, which may occur over a several month period, is therefore carried out before any blood sample is taken. The decision to have the blood test should be a personal one, without pressure from other family members or health professionals, and people must be over 18 years of age.
PRE-IMPLNATATION GENETICS
It may be possible to use techniques similar to in-vitro fertilization ("test-tube baby") to help families have a baby that they know will not carry the faulty gene. You can discuss this with doctors at the NPC.
In the acquired prion diseases, the rogue prion proteins have inadvertently been introduced into the individual as a result of accidental inoculation during medical procedures (termed Iatrogenic CJD (iCJD)) or by exposure to food products contaminated with BSE (variant CJD (vCJD) or human BSE). vCJD is the only type of human prion disease thought to be caused by exposure to BSE. Kuru is also an acquired prion disease (more information can be found about Kuru within the research section of the website).
There are 3 ways iCJD has been acquired:
Growth hormone and gonadotrophin administration
Between 1958 and 1985 thousands of children were treated worldwide with injections of growth hormone to correct growth problems. Approximately 1,900 children were treated with human derived growth hormone in the UK yet relatively few people have developed CJD. To date there have been approximately 200 cases world-wide. The growth hormone in these cases was extracted from large numbers of pituitary glands (a small gland at the base of the brain which produces growth hormone) obtained from bodies after death i.e. cadaver sourced growth hormone. A number of glands were thought to be derived from patients who, unbeknown at the time of donation, had been suffering from CJD. Use of this material in the UK and USA ceased in 1985 and a little later in France when artificially synthesised growth hormone, which does not carry this risk, became available.
A small number of women have also developed CJD after being treated with human derived pituitary gonadotrophin (sometimes used for treatment of infertility).
Growth hormone induced iCJD affects young adults as most treatments were given to children with restricted growth. The disease has a long incubation period that can exceed three decades. At present there are 0-6 new cases diagnosed each year in the UK. In the early stages the illness is predominantly a disorder of co-ordination and balance (ataxia), sometimes with psychiatric disturbances. The duration of the illness is variable but is usually 8-18 months.
Implantation of cadaver sourced dura.
The dura is a tough membrane covering the brain and lying immediately under the skull. Material obtained from several dead patients was used to repair defects in the dura of patients who had undergone surgical procedures on the brain which left substantial defects in the dura and occasionally for other reasons e.g. aneurysm repair. Since 1992 human dural grafts have not been used, having been replaced with a synthetic substitute. The majority of iCJD cases as a result of dural grafting have been reported from Japan, where 154 cases had been notified by 2018, with very few from the UK. Data from Japan indicates a wide age range of onset of CJD in these cases as would be expected from the variable age at which the initial graft was under taken (15-80 years median age 57 years ). The incubation period is also variable, ranging from 1 to 25years (median approximately 13 years); as a few cases are still occurring it is not possible to given a maximum incubation period.
There are 2 main presentation with iCJD resulting from dural grafting - most frequently the initial symptoms are problems with memory and cognition (dementia), and the subsequent progression is similar to that seen in sCJD (refer to sporadic prion disease section for further information). Less frequently, ataxia is the predominant initial symptom, affecting people's coordination and ability to carry out purposeful movements.
Other surgical procedures
Historically there have been less than 10 cases of CJD resulting from surgical procedures on the brain using instruments previously used for neurosurgical operations on a patient known to have sCJD. There have been no such cases for decades in the UK.
Two cases of CJD have been reported in patients who have received corneal grafts to repair damage to the cornea (the transparent part of the front of the eye). The grafted tissue is sourced from deceased patients. These two cases may represent a chance coincidence of sCJD in a grafted patient. Even if the recipient’s CJD was truly related the risk in general must be very small given the large numbers of grafts done each year.
Variant CJD (vCJD) and Bovine Spongiform Encephalopathy (BSE)
Dietary exposure through consumption of BSE infected food products has resulted in vCJD. There have been less than 200 cases in the UK. After ingestion of infected meat the abnormal prion protein invades the lymphatic tissues (tonsils, lymphatic areas of the gut and the spleen). It then travels in the nerves from the gut (autonomic nervous system) to the spinal cord and brain. vCJD has been in decline since 1999/2000 and at present there are no known cases in the UK. There is however considerable uncertainty whether the epidemic is over given the potential for extremely long incubation periods in prion diseases which is partly dependent on genetic factors. All but 2 cases of vCJD were methionine-methionine homozygous at position 129 in the prion gene - in 2008 a patient was clinically diagnosed with a different type of the prion protein gene, methionine-valine at this position. Also, in 2017 we reported a patient with vCJD with methionine-valine at position 129.
vCJD tends to affect young adults (average 26 years in females and 28 years in males, range 12-74 years) and occurs equally in males and females. There are early psychiatric and behavioural symptoms, for example, mood disturbance and delusions. Persistent pain can be experienced in the lower limbs and is unrelated to anxiety levels. As the disease advances, unsteadiness develops and cognition becomes affected. All these symptoms progress, culminating in a moribund state in 13 -14 months on average. The duration of the illness is however variable.
Five cases of possible infection with vCJD transmitted by blood transfusion have been reported. Three of the cases developed and died of vCJD and in two cases there was evidence of trasmission, with infection in the lymphatic system, but the brain was normal; these patient died of an unrelated cause. As a result of these observations a variety of surveillance measures have been instigated to assess the likelihood of silent infection being present in patients who have received a large amount of blood or blood products. Meanwhile, a number of measures have been put in place to minimise the risk of transmission of vCJD from blood or blood product transfusion. These include, withdrawal and recall of blood or blood components obtained from any individual who later develops vCJD; leukodepletion of blood used for transfusion (the white blood cell fraction which carries a substantial proportion of the infective material, is removed). From March 2004 recipients of blood transfusions have been excluded from donating blood as an added precaution to protect the blood supply.
For further information on progression of all types of acquired prion disease refer to the signs and symptoms section.
The National Prion Clinic also supports patients with other conditions caused by proteins being transferred between people. These conditions are different to acquired prion diseases, but people at risk of acquired prion diseases might also be at risk of these more recently described conditions. You can read more about acquired prion diseases here
Aquired Amyloid-Beta Disease
Amyloid-beta is a protein. It is associated with two diseases – Alzheimer’s disease, in which people develop dementia, and cerebral amyloid angiopathy, in which people develop brain haemorrhages.
In 2015, ground-breaking research from the National Prion Clinic showed that people who had died from iatrogenic CJD – an acquired prion disease caused by medical treatment (in this case, treatment with cadaveric human growth hormone ) – also had unusually high amounts of another protein, called amyloid-beta, in their brains. The authors concluded that the amyloid-beta protein had been transmitted to these people via their medical treatments. You can read the paper here. After this initial publication, several other institutions around the world reported similar findings.
Researchers from the MRC Prion Unit and National Prion Clinic later showed that historical samples of cadaveric human growth hormone contained measurable amounts of amyloid-beta protein, and could still be used to transmit amyloid-beta in an experimental model. You can read the paper here.
You can find out more about treatment with human derived pituitary growth hormone here
Iatrogrenic Cerebral Amyloid Angiopathy
We now know that a number of people have developed brain haemorrhages following medical treatments, often in childhood. These brain haemorrhages were caused by a condition called iatrogenic cerebral amyloid angiopathy, also called iatrogenic CAA.
Most cases of iatrogenic CAA have occurred after procedures using cadaveric dura. The dura is a tough membrane covering the brain and lying immediately under the skull. Material obtained from several dead patients was used during certain brain operations, and to treat abnormally growing blood vessels. Since 1992 human dura grafts have not been used, having been replaced with a synthetic substitute.
Some people with iatrogenic CAA had brain operations which did not use cadaveric dura, and it is thought that they acquired amyloid-beta during the operation itself.
The National Prion Clinic is involved in a number of research studies that aim to better understand the causes and consequences of iatrogenic CAA. We work closely with the UCL Stroke Research Centre, which has extensive expertise in the diagnosis and treatment of brain haemorrhage, in trying to better understand this new condition. You can find out more about this research here
Whilst there is no proven treatment for prion disease, it is possible to alleviate specific symptoms through medication, other therapies, trying out different caring strategies and adapting the environment. The National Prion Clinic works closely with local teams to provide a clinical service for people with or suspected prion disease. The person affected will eventually become dependent on carers to carry out all activities of daily living. The following symptoms are commonly experienced.
Behavioural Symptoms
Often mood disturbance e.g. aggression or loss of interest and personality changes persist into the illness. Anxiety and depression are fairly common features. There may also be a lack of social judgement and disinhibition. People may prefer to keep to familiar routines, changes in the regular daily pattern of events, or new faces may cause distress and anxiety.
Communication Problems
Speech tends to become slurred (dysarthria) and quiet and as a result speech may become hard to understand, making communication difficult. There is often a reduction in the content of language, word finding difficulties and there may be repetition of words or sentences. Eventually the person can become mute. As the illness progresses the ability to read and write are gradually lost. Problems may occur with understanding written material and with spelling and signing forms; the person may also have difficulty following instructions.
Memory/Cognitive Deficits
Problems develop with memory and thinking and there is often a general decline in intellect. There may be forgetfulness of day to day events, often accompanied by disorientation and poor concentration or attention. Everyday skills that we take for granted may be lost. Typically the person affected will forget the day and date. They may also start to forget how to carry out everyday skills, for example making a cup of tea. In the latter stages of the disease the person may become increasingly unaware of their immediate environment and the people around them.
Movement Problems
Initially there may be a disturbance in balance and gait, leading to unsteadiness (ataxia). Walking will therefore be affected and so extra care will have to be taken to try to prevent falls. Involuntary rhythmic muscle contractions leading to jerky movements (myoclonus) and difficulties co-ordinating hand movements leading to apparent clumsiness. Shakiness (tremor) and stiffness (rigidity) are often seen. As movements become increasingly uncoordinated the individual will need help with carrying out their daily activities, for example, personal hygiene and use of the toilet.
Swallowing Problems
With the progression of the disease there may also be difficulty in swallowing. There are a number of strategies, which may make swallowing easier and an assessment by a speech and language therapist can identify problems and give advice regarding strategies to help.
As swallowing becomes increasingly difficult in the later stages of the disease, it may be suggested that nutrition be supplemented with tube feeding. This issue will require careful consideration and is rarely done in prion disease. Relatives need support in making an informed decision. A speech and language therapist, Macmillan nurse, dietician as well as your own GP may be able to offer advice.
Visual/Perceptual Problems
Visual problems include double vision and difficulty moving eyes to follow objects. Hallucinations are fairly common. There may be a failure to understand and correctly interpret visual stimuli. There may be misidentification of objects/people, whereby something/someone may not be recognised accurately.
Some patients may suffer from what is known as cortical blindness, a condition in which an individual appears to be blind (although the eyes themselves are normal), due to damage in the visual processing and interpretation areas of the brain.
Seizures
Very occasionally a person may suffer from seizures in the later stages of the disease. Medication is available to help control seizures should they occur.
In reaching a diagnosis your doctor will first consider the symptoms and their progression over time, the past medical history, family illnesses and also examination findings. In prion diseases the early symptoms can be shared with many other common illnesses, such as insomnia, altered mood, unusual behaviour, dizziness, or tingling of part of the body. Depending on which symptoms and examination findings predominate in the early stages, your doctor might refer you to a neurologist, psychiatrist or other physician for help. At this first specialist appointment, prion diseases are not always considered because they are rare and the typical signs may not be present, but problems with thinking skills or balance will certainly be noted.
Further information click here
At the National Prion Clinic (NPC) our nursing philosophy is to provide an atmosphere of comfort while delivering care to the public we serve. It is our belief that the dignity and worth of the individual must be respected and preserved. We further believe that the nursing care must be consistent with and specifically designed to meet the needs of the patient, family members and the community in which the patient lives. The following information explains how the nurses and medical staff at the NPC can help, with difficulties that patients and their families may experience, due to prion disease. We work closely with colleagues from local teams and those from the National CJD Research & Surveillance Unit based in Edinburgh.
Further information here
Bereavement is a profound experience that acknowledges the impact of losing someone significant in our lives. It encompasses a range of emotional, psychological, and physical sensations that individuals experience after a death.
For further information click here.
The rapid progression and unexpected nature of prion disease can be difficult for patients and families to come to terms with. At the National Prion Clinic (NPC) specialist nurses are available to provide information, signposting and ongoing emotional support. The nurses can arrange to visit you at home, an alternative convenient location, or can be contacted by telephone or by e-mail. There are four nurses at the NPC. We aim to make available around a day each per week specifically for information and emotional support. If it is felt that counselling is required, we have a neuro-psychologist within the team who can provide help, or we could help you to access counselling in your local area.
THE NATIONAL CJD SUPPORT NETWORK
The CJD Support Network isThe CJD Support Network was established in 1995 by relatives of people who have died with CJD and is now recognised as the leading charity for all forms of CJD. Its aims are to offer practical and emotional support to individuals and families concerned with all forms of CJD and financial support for families in need. The Network runs a 24-hour helpline and an annual Family Support Meeting.
Website: www.cjdsupport.net/
Helpline tel: 0800 774 7317
Email: support@cjdsupport.net
GENETIC COUNSELLING
If you are concerned about inherited prion disease, it may be beneficial to see a genetic counsellor who will work in a Clinical Genetics team at a local NHS hospital. Finding out whether you have a gene mutation which leads to prion disease is a complex and personal decision. Genetic counselling offers an opportunity for individuals who are at risk of inherited prion disease to find out about the possible implications of a positive or negative test result. Follow up support and advice may also be available from these teams
The British society of Human genetics provides information about genetic counselling for patients and families www.bsgm.org.uk/
The Association of Genetic Nurses and Counsellors Code of Ethics can be found at www.agnc.org.uk
The National Prion Clinic performs comprehensive investigations and assessment to provide diagnosis and care for all forms of suspected prion disease: Inherited/Familial, Iatrogenic, Sporadic and Variant. We routinely perform the following tests and investigations: genetic testing (diagnostic and predictive), imaging, neurophysiology, neuropsychology, tissue diagnosis and tonsil biopsy (as a means of diagnosing vCJD).
The clinic receives approximately 12 new referrals a month. Families and local teams are contacted the day the referral is made and we aim to review new patients throughout the UK within a week. We are a mobile service and act as support for local health services. Our support services include information on prion disease presentation and progression, symptom management, family information days and training workshops. At their discretion we normally see patients and their families for the duration of the illness.
Each patient is allocated a named nurse who will manage their care for the duration of their involvement in the clinic. Their nurse will be available via telephone or email, be present at outpatient appointments, carry out home visits, and attend case conferences as necessary. The nurses at the prion clinic are also available to provide emotional and practical support for patients and their families.
www.uclh.nhs.uk/prion provides further information on our NHS services.
Additional information, support and advice can be obtained from a variety of voluntary organisations as well as statutory bodies. It is possible that there is little or no experience in service provision for people with prion disease in your local area. It will be important for national organisations with experience of this condition to be involved supporting families and professionals in order to facilitate services locally which meet each family's individual needs.
Click here for further information.
NHS Choices is an information website that exists to meet your health information needs.
Please click on the links below to view a video presented by Professor John Collinge of the National Prion Clinic that explains different variants of CJD and the second video that covers real life stories of how CJD can effect your life.
Background
Between 1959 and 1985, nearly 2000 individuals in the UK were treated with human growth hormone (hGH) extracted from the pituitary glands of people who had died. This type of growth hormone is sometime called cadaveric growth hormone (c-hGH) or pituitary-derived growth hormone. The treatment was given for severe short stature, particularly growth hormone deficiency, and it was given by several injections per week over months or years.
Creutzfeldt-Jakob Disease
In 1985, one of the people treated with this c-hGH died from the rare brain disease Creutzfeldt-Jakob Disease (CJD), and a link to the treatments was suspected, so the use of this type of hGH was stopped. Further cases of CJD occurred over subsequent years, and the link was established beyond doubt. Cases occurred in other countries around the world, related to c-hGH produced abroad. Since this type of c-hGH was withdrawn, a synthetic growth hormone has been used and this does not carry this risk of developing CJD. CJD is a prion disease, in which an abnormal or rogue form of a normal body protein causes a progressive and fatal neurological illness. We assume that transmission of this rogue protein was from the pituitaries of the gland donors. This type of CJD is iatrogenic (iCJD), meaning it was caused by a medical accident. You can read more about iCJD here
Our role
The National Prion Clinic provides specific support for recipients of human derived pituitary growth hormone.
Cases of CJD continue to occur, with very long intervals (decades) from the time of treatment to illness onset. There have been 81 cases in the UK up to August 2022. We have been involved with most of these people and their families.
If you need further advice or more information, please contact:
Kirsty McNiven Kirsty.McNiven@nhs.net
Gargi Banerjee gargi.banerjee@nhs.net
You can also contact the National Prion Clinic on 020 7679 5142 or 020 7679 5036 and either Kirsty or Gargi will get back to you as soon as they can.
Our Research
We are interested in the long-term health of people who received treatment with human derived pituitary growth hormone. You can find out more about this research here
We have a list of common questions and answers here.
If you have a question you would like us to answer please email: uclh.prion.help@nhs.net