Mark Pepys

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Sir Mark Pepys
Born
Mark Brian Pepys

(1944-09-18) 18 September 1944 (age 78) [1]
Cape Town, South Africa
NationalityBritish
Alma mater
Awards FRS (1998) [2]
Scientific career
Fields
Institutions University College London
Thesis Role of complement in induction of the allergic response  (1973)
Website www.royalfree.nhs.uk/services/staff-a-z/professor-mark-pepys

Sir Mark Brian Pepys FRCP FRCPath FMedSci FRS [2] [3] (born 18 September 1944) is a South African-born British academic of medicine. He was until 2011 Professor of Medicine at University College London and Head of Medicine at the Hampstead Campus and the Royal Free Hospital. [4]

Contents

Education

Pepys was born in Cape Town, South Africa, the son of physician Jack Pepys FRCP FRCPE FRCPath and Rhoda Gertrude Pepys (née Kussel). He moved to the UK in 1948. [5] He finished his early education at the University of Cambridge, and then qualified as a medical doctor at University College London Medical School. He then returned to Cambridge where he was awarded a PhD in Immunology in 1973.

Awards and honours

Pepys won the GlaxoSmithKline Prize in 2007 "for his excellent work as a clinical scientist who has identified specific proteins as new therapeutic targets and developed novel drugs with potential use in amyloidosis, Alzheimer's disease and cardiovascular disease". [6] In 1998, Pepys was elected a Fellow of the Royal Society (FRS). [7] His nomination reads:

Pepys has made seminal contributions in three areas: complement and immune response, the pentraxin proteins, and amyloidosis, and is a leading authority on these subjects in the UK and internationally. He discovered the role of complement in induction of antibody production and antigen localisation to germinal centres. He has pioneered work on the structure, function and clinical applications of the pentraxins, C-reactive protein (CRP) and serum amyloid P component (SAP), and identified most of the known members of this valuable aid to patient management. He discovered the capacity of SAP for calcium-dependent binding, which underlies its universal deposition in amyloid, described its interaction with DNA in-vivo and in-vitro, and its ability to solubilise chromatin, and identified SAP as a normal tissue protein. He introduced radiolabelled SAP as a diagnostic in-vivo tracer for amyloid, which has revolutionised knowledge of the natural history of amyloidosis and its response to treatment. He has discovered that variants of lysozyme can form amyloid and identified the first mutations in the human lysozyme gene, as well as novel amyloidogenic variants of apolipoprotein AI and transthyretin. [2]

In 1999, he became director of the University College London Centre for Amyloidosis and Acute Phase Proteins.

Mark Pepys has recently won the 2008 Ernst Chain Prize for his work on amyloid diseases, established by Imperial College London in recognition of leaders in their fields.[ citation needed ]

Pepys was knighted in the 2012 New Year Honours for services to biomedicine. [8]

See also

Related Research Articles

<span class="mw-page-title-main">Amyloidosis</span> Metabolic disease involving abnormal deposited amyloid proteins

Amyloidosis is a group of diseases in which abnormal proteins, known as amyloid fibrils, build up in tissue. There are several non-specific and vague signs and symptoms associated with amyloidosis. These include fatigue, peripheral edema, weight loss, shortness of breath, palpitations, and feeling faint with standing. In AL amyloidosis, specific indicators can include enlargement of the tongue and periorbital purpura. In wild-type ATTR amyloidosis, non-cardiac symptoms include: bilateral carpal tunnel syndrome, lumbar spinal stenosis, biceps tendon rupture, small fiber neuropathy, and autonomic dysfunction.

<span class="mw-page-title-main">Transthyretin</span> Serim protein related to amyloid diseases

Transthyretin (TTR or TBPA) is a transport protein in the plasma and cerebrospinal fluid that transports the thyroid hormone thyroxine (T4) and retinol to the liver. This is how transthyretin gained its name: transports thyroxine and retinol. The liver secretes TTR into the blood, and the choroid plexus secretes TTR into the cerebrospinal fluid.

<span class="mw-page-title-main">Cerebral amyloid angiopathy</span> Disease of blood vessels of the brain involving amyloid-beta build-up

Cerebral amyloid angiopathy (CAA) is a form of angiopathy in which amyloid beta peptide deposits in the walls of small to medium blood vessels of the central nervous system and meninges. The term congophilic is sometimes used because the presence of the abnormal aggregations of amyloid can be demonstrated by microscopic examination of brain tissue after staining with Congo red. The amyloid material is only found in the brain and as such the disease is not related to other forms of amyloidosis.

<span class="mw-page-title-main">Serum amyloid P component</span>

The serum amyloid P component (SAP) is the identical serum form of amyloid P component (AP), a 25kDa pentameric protein first identified as the pentagonal constituent of in vivo pathological deposits called "amyloid". APCS is its human gene.

<span class="mw-page-title-main">Familial amyloid polyneuropathy</span> Medical condition

Familial amyloid polyneuropathy, also called transthyretin-related hereditary amyloidosis, transthyretin amyloidosis abbreviated also as ATTR, or Corino de Andrade's disease, is an autosomal dominant neurodegenerative disease. It is a form of amyloidosis, and was first identified and described by Portuguese neurologist Mário Corino da Costa Andrade, in 1952. FAP is distinct from senile systemic amyloidosis (SSA), which is not inherited, and which was determined to be the primary cause of death for 70% of supercentenarians who have been autopsied. FAP can be ameliorated by liver transplantation.

<span class="mw-page-title-main">Pentraxins</span>

Pentraxins (PTX), also known as pentaxins, are an evolutionary conserved family of proteins characterised by containing a pentraxin protein domain. Proteins of the pentraxin family are involved in acute immunological responses. They are a class of pattern recognition receptors (PRRs). They are a superfamily of multifunctional conserved proteins, some of which are components of the humoral arm of innate immunity and behave as functional ancestors of antibodies (Abs). They are known as classical acute phase proteins (APP), known for over a century.

<span class="mw-page-title-main">Cardiac amyloidosis</span> Medical condition

Cardiac amyloidosis is a subcategory of amyloidosis where there is depositing of the protein amyloid in the cardiac muscle and surrounding tissues. Amyloid, a misfolded and insoluble protein, can become a deposit in the heart's atria, valves, or ventricles. These deposits can cause thickening of different sections of the heart, leading to decreased cardiac function. The overall decrease in cardiac function leads to a plethora of symptoms. This multisystem disease was often misdiagnosed, with diagnosis previously occurring after death during autopsy. However, recent advancements of technologies have increased the diagnosis of the disease. Cardiac amyloidosis has multiple sub-types including light chain, familial, and senile. One of the most studied types is light chain cardiac amyloidosis. Prognosis depends on the extent of the deposits in the body and the type of amyloidosis. New treatment methods are actively being researched in regards to the treatment of heart failure and specific cardiac amyloidosis problems.

Sir David Keith Peters is a retired Welsh physician and academic. He was Regius Professor of Physic at the University of Cambridge from 1987 to 2005, where he was also head of the School of Clinical Medicine.

<span class="mw-page-title-main">CPHPC</span> Chemical compound

CPHPC is a proline-derived small molecule able to strip amyloid P (AP) from deposits by reducing levels of circulating serum amyloid P (SAP). The SAP-amyloid association has also been identified as a possible drug target for anti-amyloid therapy, with the recent development and first stage clinical trials of CPHPC for amyloidosis.

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<span class="mw-page-title-main">LECT2 amyloidosis</span> Medical condition

LECT2 Amyloidosis (ALECT2) is a form of amyloidosis caused by the LECT2 protein. It was found to be the third most common cause of amyloidosis in a set of more than 4,000 individuals studied at the Mayo Clinic; the first and second most common forms the disorder were AL amyloidosis and AA amyloidosis, respectively. Amyloidosis is a disorder in which the abnormal deposition of a protein in organs and/or tissues gradually leads to organ failure and/or tissue injury.

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References

  1. "Pepys, Prof. Mark Brian". Who's Who. doi:10.1093/ww/9780199540884.013.U30545. ISBN   978-0-19-954088-4 . Retrieved 28 April 2019.
  2. 1 2 3 "EC/1998/26: Pepys, Mark Brian". London: The Royal Society. Archived from the original on 13 July 2015.
  3. "Iris View Profile". iris.ucl.ac.uk. Retrieved 13 December 2017.
  4. Booth, D. R.; Sunde, M; Bellotti, V; Robinson, C. V.; Hutchinson, W. L.; Fraser, P. E.; Hawkins, P. N.; Dobson, C. M.; Radford, S. E.; Blake, C. C.; Pepys, M. B. (1997). "Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis". Nature. 385 (6619): 787–93. Bibcode:1997Natur.385..787B. doi:10.1038/385787a0. PMID   9039909. S2CID   4347837.
  5. "Prof Sir Mark Pepys". Institutional Research Information Service. Retrieved 28 April 2019.
  6. "The Royal Society GlaxoSmithKline Prize and Lecture (1976) (2002)". royalsociety.org. Archived from the original on 9 June 2008. Retrieved 3 April 2009.
  7. "Mark Pepys". royalsociety.org. Retrieved 13 December 2017.
  8. "No. 60009". The London Gazette (Supplement). 31 December 2011. p. 1.