Michael Berridge

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Sir Michael Berridge

FRS FMedSci FBPhS
Born
Michael John Berridge [1]

(1938-10-22)22 October 1938
Gatooma
Southern Rhodesia [2]
Died13 February 2020(2020-02-13) (aged 81) [1]
Education University College of Rhodesia and Nyasaland (Bsc)
University College (PhD)
Known for Cell signaling research
Discovery of inositol trisphosphate as second messenger
Awards King Faisal International Prize in Science
Louis-Jeantet Prize for Medicine
Knight Bachelor
Canada Gairdner International Award
Albert Lasker Award for Basic Medical Research
Royal Medal
Dr H. P. Heineken Prize for Biochemistry and Biophysics
Shaw Prize in Life Science and Medicine
Scientific career
Fields Physiology
Biochemistry
Institutions University of Virginia
Case Western Reserve University
University of Cambridge
Babraham Institute
Thesis The physiology of excretion in the cotton stainer, Dysdercus fasciatus Signoret (Hemiptera, Pyrrhocoridae)  (1964)
Doctoral advisor Vincent Wigglesworth
Notable students Antony Galione [3]

Sir Michael John "Mike" Berridge FRS FMedSci FBPhS [4] (22 October 1938 - 13 February 2020) was a British physiologist and biochemist. He was known for his work on cell signaling, in particular the discovery that inositol trisphosphate acts as a second messenger, linking events at the plasma membrane with the release of calcium ions (Ca2+) within the cell.

Contents

Early life and education

Berridge was born in Gatooma (now Kadoma, Zimbabwe) in Southern Rhodesia (now Zimbabwe). His high school biology teacher convinced him and his parents that he should pursue tertiary education, and he entered the newly founded University of Rhodesia and Nyasaland (now University of Zimbabwe), [5] earning his Bsc in zoology and chemistry in 1960. [6]

He became interested in insect physiology after helping with his physiology professor's research on tsetse flies, and went to the United Kingdom to study with Vincent Wigglesworth, regarded as the father of insect physiology, at the Department of Zoology of the University of Cambridge. Berridge became a member at the Gonville and Caius College, where Wigglesworth was a fellow, [5] and obtained his PhD in 1965. [7]

Career

Initially intending to return to Southern Rhodesia (now Zimbabwe) after his PhD, Berridge's plan was thwarted by the Rhodesian Bush War. He migrated to the United States instead, joining the Department of Biology of the University of Virginia as a postdoctoral fellow. [5] A year later, he moved to the Developmental Biology Center of Case Western Reserve University. He became a research associate under Bodil Schmidt-Nielsen at the Department of Biology of the same university in 1967. [7]

In 1969, John Treherne invited Berridge to return to the University of Cambridge and join the new Unit of Invertebrate Chemistry and Physiology that he was setting up in the Department of Zoology. [5] He first joined as a senior scientific officer, and was promoted to principal scientific officer in 1972. He became a senior principal scientific officer at the Unit of Insect Neurophysiology and Pharmacology, also at the University of Cambridge, in 1978. [7]

In 1990, Berridge joined the Babraham Institute as the Deputy Chief Scientific Officer of the Laboratory of Molecular Signalling, before serving as the Head of Signalling in 1996 until retiring in 2003. [8] After retirement, Berridge was appointed as Babraham's first emeritus Babraham Fellow. [9]

Berridge was a fellow of the Trinity College of the University of Cambridge from 1972 until his death. [6]

Berridge maintained an online textbook on cell signalling, now hosted by Portland Press under the Biochemical Society. [10]

Research

Berridge had been studying cell signaling when he was at Case Western Reserve University, where he received advice from Theodore W. Rall, co-discoverer of the second messenger cyclic AMP with Earl Wilbur Sutherland Jr., who had also worked at Case Western Reserve. [11] Working on the salivary glands of a blow fly species, Berridge showed cyclic AMP produced the same physiological effect as serotonin, dramatically increasing saliva secretion. [12] The idea of second messenger was new at the time, and his finding supported cyclic AMP as a second messenger of serotonin.

He continued studying cyclic AMP after returning to the University of Cambridge, and conducted experiments to study how serotonin and cyclic AMP affected the movement of ions, as ion concentration difference across the salivary gland epithelium controlled the movement of water across the epithelium through osmosis. Berridge measured the difference in electric potential across the epithelium since ions are charged. [11]

Surprisingly, he found that serotonin and cyclic AMP produced opposite effect to ion movement. While the former reduced the transepithelial potential difference closer to zero, the latter caused an even more negative difference. This suggested cyclic AMP caused positively-charged ions to move across the epithelium from the extracellular fluid to the inside of the salivary gland (known as the lumen). [13]

Berridge suspected calcium ions (Ca2+) could explain the distinct electrical but similar physiological effects of serotonin and cyclic AMP. In 1971, Howard Rasmussen, one of the first researchers to recognise the role of Ca2+ as a second messenger, was on a sabbatical at Cambridge. [5] He and Rasmussen worked together and found serotonin triggered the release of Ca2+ from a storage inside the cell. [14] Later, he confirmed that serotonin activated two distinct receptor system, one through cyclic AMP and the other through Ca2+. [15]

Berridge then wanted to identify the connection between cell surface receptor activation and the release of intracellular Ca2+ from storage. He was inspired by a review article by Robert H. Michell in 1975, which proposed receptor activation caused the breakdown of phosphatidylinositol, which in turn opened Ca2+ channels on the cell membrane to allowing Ca2+ influx into cells. [16] He hypothesised phosphatidylinositol was hydrolysed into a form of inositol phosphate and diglyceride (DAG), and the former was eventually broken down into inositol. He applied lithium ions to blow fly salivary glands to inhibit the conversion of inositol phosphate to inositol.

With help from Rex Malcolm Chaplin Dawson, who was studying inositol at the Babraham Institute near Cambridge, Berridge found that phosphatidylinositol was hydrolysed into IP3 and DAG. [17] Later the same year, he confirmed IP3 released Ca2+ from the intracellular storage, which he identified as the endoplasmic reticulum. [18] This report, together with Yasutomi Nishizuka's discovery that DAG was a second messenger in its own right and could activate protein kinase C, [19] marked the start of the field of calcium signaling. [20]

Awards and honours

The Sir Michael Berridge Prize at the Babraham Institute was named in his honour and established with his endowment. [41]

Related Research Articles

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Adenylate cyclase is an enzyme with systematic name ATP diphosphate-lyase . It catalyzes the following reaction:

<span class="mw-page-title-main">Cyclic adenosine monophosphate</span> Cellular second messenger

Cyclic adenosine monophosphate is a second messenger, or cellular signal occurring within cells, that is important in many biological processes. cAMP is a derivative of adenosine triphosphate (ATP) and used for intracellular signal transduction in many different organisms, conveying the cAMP-dependent pathway.

<span class="mw-page-title-main">G protein-coupled receptor</span> Class of cell surface receptors coupled to G-protein-associated intracellular signaling

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<span class="mw-page-title-main">G protein</span> Type of proteins

G proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). When they are bound to GTP, they are 'on', and, when they are bound to GDP, they are 'off'. G proteins belong to the larger group of enzymes called GTPases.

Inositol trisphosphate or inositol 1,4,5-trisphosphate abbreviated InsP3 or Ins3P or IP3 is an inositol phosphate signaling molecule. It is made by hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2), a phospholipid that is located in the plasma membrane, by phospholipase C (PLC). Together with diacylglycerol (DAG), IP3 is a second messenger molecule used in signal transduction in biological cells. While DAG stays inside the membrane, IP3 is soluble and diffuses through the cell, where it binds to its receptor, which is a calcium channel located in the endoplasmic reticulum. When IP3 binds its receptor, calcium is released into the cytosol, thereby activating various calcium regulated intracellular signals.

<span class="mw-page-title-main">Sodium–potassium pump</span> Enzyme found in the membrane of all animal cells

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<span class="mw-page-title-main">Calcium in biology</span> Use of calcium by organisms

Calcium ions (Ca2+) contribute to the physiology and biochemistry of organisms' cells. They play an important role in signal transduction pathways, where they act as a second messenger, in neurotransmitter release from neurons, in contraction of all muscle cell types, and in fertilization. Many enzymes require calcium ions as a cofactor, including several of the coagulation factors. Extracellular calcium is also important for maintaining the potential difference across excitable cell membranes, as well as proper bone formation.

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<span class="mw-page-title-main">CREB</span> Class of proteins

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<span class="mw-page-title-main">Cyclic nucleotide–gated ion channel</span> Family of transport proteins

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<span class="mw-page-title-main">Calcium signaling</span> Intracellular communication process

Calcium signaling is the use of calcium ions (Ca2+) to communicate and drive intracellular processes often as a step in signal transduction. Ca2+ is important for cellular signalling, for once it enters the cytosol of the cytoplasm it exerts allosteric regulatory effects on many enzymes and proteins. Ca2+ can act in signal transduction resulting from activation of ion channels or as a second messenger caused by indirect signal transduction pathways such as G protein-coupled receptors.

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<span class="mw-page-title-main">Nicotinic acid adenine dinucleotide phosphate</span> Chemical compound

Nicotinic acid adenine dinucleotide phosphate (NAADP) is a Ca2+-mobilizing second messenger synthesised in response to extracellular stimuli. Like its mechanistic cousins, IP3 and cyclic adenosine diphosphoribose (Cyclic ADP-ribose), NAADP binds to and opens Ca2+ channels on intracellular organelles, thereby increasing the intracellular Ca2+ concentration which, in turn, modulates sundry cellular processes (see Calcium signalling). Structurally, it is a dinucleotide that only differs from the house-keeping enzyme cofactor, NADP by a hydroxyl group (replacing the nicotinamide amino group) and yet this minor modification converts it into the most potent Ca2+-mobilizing second messenger yet described. NAADP acts across phyla from plants to humans.

<span class="mw-page-title-main">2-Aminoethoxydiphenyl borate</span> Chemical compound

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<span class="mw-page-title-main">Phospholipase C</span> Class of enzymes

Phospholipase C (PLC) is a class of membrane-associated enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which play an important role in eukaryotic cell physiology, in particular signal transduction pathways. Phospholipase C's role in signal transduction is its cleavage of phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), which serve as second messengers. Activators of each PLC vary, but typically include heterotrimeric G protein subunits, protein tyrosine kinases, small G proteins, Ca2+, and phospholipids.

In the field of molecular biology, the cAMP-dependent pathway, also known as the adenylyl cyclase pathway, is a G protein-coupled receptor-triggered signaling cascade used in cell communication.

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

Calcium encoding (also referred to as Ca2+ encoding or calcium information processing) is an intracellular signaling pathway used by many cells to transfer, process and encode external information detected by the cell. In cell physiology, external information is often converted into intracellular calcium dynamics. The concept of calcium encoding explains how Ca2+ ions act as intracellular messengers, relaying information within cells to regulate their activity. Given the ubiquity of Ca2+ ions in cell physiology, Ca2+ encoding has also been suggested as a potential tool to characterize cell physiology in health and disease. The mathematical bases of Ca2+ encoding have been pioneered by work of Joel Keizer and Hans G. Othmer on calcium modeling in the 1990s and more recently they have been revisited by Eshel Ben-Jacob, Herbert Levine and co-workers.

<span class="mw-page-title-main">Antony Galione</span> British pharmacologist (born 1963)

Antony Giuseppe Galione is a British pharmacologist. He is a professor and Wellcome Trust senior investigator in the Department of Pharmacology at the University of Oxford.

References

  1. 1 2 "Sir Michael Berridge, biochemist behind a paradigm shift in cell science – obituary". The Telegraph . 23 February 2020. Archived from the original on 27 February 2020. Retrieved 27 February 2020.
  2. 1 2 3 4 "Prof. Dr. Michael J. Berridge" (PDF). Ernst Schering Foundation. 21 November 2017. Archived from the original (PDF) on 3 November 2023. Retrieved 3 November 2023.
  3. ↑ "Antony Galione". New College, Oxford. Archived from the original on 6 November 2023. Retrieved 6 November 2023.
  4. ↑ Petersen, Ole H. (2024). "Sir Michael John Berridge. 22 October 1938 — 13 February 2020". Biographical Memoirs of Fellows of the Royal Society. 76.
  5. 1 2 3 4 5 Berridge, Michael J. (2005). "Unlocking the secrets of cell signaling". Annual Review of Physiology . 67 (1): 1–21. doi: 10.1146/annurev.physiol.67.040103.152647 . PMID   15709950.
  6. 1 2 "Autobiography of Michael Berridge". Shaw Prize. Archived from the original on 7 November 2023. Retrieved 7 November 2023.
  7. 1 2 3 4 5 "Sir Michael John Berridge". Academia Europaea. Archived from the original on 8 November 2023. Retrieved 8 November 2023.
  8. ↑ "In tribute: Sir Michael Berridge FRS". Babraham Institute. 13 February 2020. Archived from the original on 11 November 2023. Retrieved 11 November 2023.
  9. 1 2 "The Prize in Life Science & Medicine 2005". Shaw Prize. Archived from the original on 11 November 2023. Retrieved 11 November 2023.
  10. ↑ "Cell Signalling Biology". Biochemical Society. Archived from the original on 19 December 2023. Retrieved 19 December 2023.
  11. 1 2 Berridge, Mike (2005). "Interview with Mike Berridge". BioEssays . 27 (2): 201–210. doi:10.1002/bies.20186. PMID   15666351 . Retrieved 23 November 2023.
  12. ↑ Berridge, M. J.; Patel, N. G. (1968). "Insect Salivary Glands: Stimulation of Fluid Secretion by 5-Hydroxytryptamine and Adenosine-3′,5′-monophosphate". Science . 162 (3852): 462–463. doi:10.1126/science.162.3852.462. PMID   4300804. S2CID   45803569 . Retrieved 23 November 2023.
  13. ↑ Berridge, Michael J.; Prince, William T. (1972). "Transepithelial potential changes during stimulation of isolated salivary glands with 5-hydroxytryptamine and cyclic AMP". Journal of Experimental Biology . 56 (1): 139–153. doi: 10.1242/jeb.56.1.139 . PMID   4339528. Archived from the original on 28 November 2023. Retrieved 28 November 2023.
  14. ↑ Prince, William T.; Berridge, Michael J.; Rasmussen, Howard (1972). "Role of Calcium and Adenosine-3′:5′-Cyclic Monophosphate in Controlling Fly Salivary Gland Secretion". Proceedings of the National Academy of Sciences of the United States of America . 69 (3): 553–557. doi: 10.1073/pnas.69.3.553 . PMC   426505 . PMID   4335064.
  15. ↑ Berridge, Michael John. (1981). "Electrophysiological evidence for the existence of separate receptor mechanisms mediating the action of 5-hydroxytryptamine". Molecular and Cellular Endocrinology . 23 (1): 91–104. doi:10.1016/0303-7207(81)90119-2. PMID   6266901. S2CID   38874406 . Retrieved 29 November 2023.
  16. ↑ Robert H., Michell (1975). "Inositol phospholipids and cell surface receptor function". Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes . 415 (1): 81–147. doi:10.1016/0304-4157(75)90017-9. PMID   164246 . Retrieved 29 November 2023.
  17. ↑ Berridge, Michael J.; Dawson, Rex M. C.; Downes, C. Peter; Heslop, John P.; Irvine, Robin F. (1983). "Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides". Biochemical Journal . 212 (2): 473–482. doi:10.1042/bj2120473. PMC   1152070 . PMID   6309146.
  18. ↑ Streb, H.; Irvine, R. F.; Berridge, M. J.; Schulz, I. (1983). "Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate". Nature . 306 (5938): 67–69. Bibcode:1983Natur.306...67S. doi:10.1038/306067a0. PMID   6605482. S2CID   4359904 . Retrieved 19 December 2023.
  19. ↑ Nishizuka, Yasutomi (1984). "The role of protein kinase C in cell surface signal transduction and tumour promotion". Nature. 308 (5961): 693–698. Bibcode:1984Natur.308..693N. doi:10.1038/308693a0. PMID   6232463. S2CID   4240505.
  20. ↑ Berridge, Michael J.; Bootman, Martin D.; Roderick, H. Llewelyn (2003). "Calcium signalling: dynamics, homeostasis and remodelling". Nature Reviews Molecular Cell Biology . 4 (7): 517–529. doi:10.1038/nrm1155. PMID   12838335. S2CID   1152297 . Retrieved 19 December 2023.
  21. ↑ "Michael Berridge". Royal Society. Archived from the original on 17 November 2023. Retrieved 17 November 2023.
  22. ↑ "Professor Michael J. Berridge". King Faisal Prize. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  23. ↑ "Professor Michael BERRIDGE". Louis-Jeantet Foundation. October 2017. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  24. ↑ "Michael J. Berridge". Gairdner Foundation. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  25. ↑ "Sir Michael Berridge". Academia Europaea. Archived from the original on 17 November 2023. Retrieved 17 November 2023.
  26. ↑ "1989 Albert Lasker Basic Medical Research Award". Lasker Award. Archived from the original on 2 November 2023. Retrieved 2 November 2023.
  27. ↑ "Michael J. Berridge". European Molecular Biology Organization. Archived from the original on 17 November 2023. Retrieved 17 November 2023.
  28. ↑ "BERRIDGE Michael". Royal Academy of Medicine of Belgium (Académie royale de médecine de Belgique). Archived from the original on 29 January 2023. Retrieved 29 January 2023.
  29. ↑ "Award winners : Royal Medal". Royal Society. Archived from the original on 20 November 2023. Retrieved 20 November 2023.
  30. ↑ "Sir Michael J. Berridge". Heineken Prizes. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  31. ↑ "Michael J. Berridge". Wolf Foundation. 10 December 2018. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  32. ↑ "Massry Prize Winners ( 1996 – Present )". Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  33. ↑ "No. 54993". The London Gazette (1st supplement). 30 December 1997. p. 1.
  34. ↑ "Gonville and Caius College". Cambridge University Reporter . Vol. CXXIX, no. 6. 4 November 1998. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  35. ↑ "Sir Michael Berridge FRS FMedSci". Academy of Medical Sciences. Archived from the original on 20 November 2023. Retrieved 20 November 2023.
  36. ↑ "Michael J. Berridge". Ernst Schering Foundation. Archived from the original on 14 November 2023. Retrieved 14 November 2023.
  37. ↑ "Michael J. Berridge". National Academy of Sciences. Archived from the original on 20 November 2023. Retrieved 20 November 2023.
  38. ↑ "Michael John Berridge". American Academy of Arts and Sciences. 31 May 2023. Archived from the original on 20 November 2023. Retrieved 20 November 2023.
  39. ↑ "Honorary Members". Biochemical Society. Archived from the original on 20 November 2023. Retrieved 20 November 2023.
  40. ↑ "Sir Michael J. Berridge". American Philosophical Society. Archived from the original on 2 November 2023. Retrieved 2 November 2023.
  41. ↑ "The Sir Michael Berridge Prize". Babraham Institute. Archived from the original on 11 November 2023. Retrieved 11 November 2023.
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