Barbara Illingworth Brown

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Barbara Illingworth Brown
Born
Barbara A. Illingworth

May 12, 1924 [1]
Hartford, CT
DiedSeptember 27, 2016 [1]
Alma materYale University
Scientific career
Thesis Effects of purified growth hormone on glycogen storage  (1950)
Doctoral advisor Jane Anne Russell

Barbara Illingworth Brown was an American biochemist. She worked primarily at Washington University in St. Louis.

Contents

Education and career

Brown was born in Hartford, Connecticut and later moved to Pennsylvania when her father's job in insurance moved the family. [2] Brown graduated from Smith College in 1946. She worked with Jane Anne Russell at Yale University [2] and received her PhD in physiological chemistry in 1950. [3] [4] Following her Ph.D., Brown applied to work with the Nobel Prize-winner Gerty Cori [2] and became a Research Associate Professor of Biochemistry at Washington University in St. Louis and Established Investigator of the American Heart Association. [5] She later also worked with Cori's husband and fellow Nobel Prize winner Carl Ferdinand Cori. [2] She retired in 1989. [2]

Brown served on the National Advisory General Medical Sciences Council at the National Institutes of Health from 1972 to 1974. [6] She was awarded the Wilbur Cross Medal from Yale in 1983. [7]

Research

Her work was primarily devoted to the biochemistry of inherited metabolic diseases. [1] She investigated the structure of glycogen and amylopectins, [2] [8] and defined the pathway and mechanisms of phosphorylase enzymes. [9] [10] Her research included the discovery of enzymes [11] in a previously unknown pathway to process glycogen. [12] She went on to research diseases related to the storage of glycogen where these enzymes were absent. [13] [14] She applied some of Carl Cori's findings to medical cases, [15] and confirmed the second known case of fructose bisphosphatase deficiency, a rare metabolic disorder, in 1970. [16] [17] She played a similar role in therapeutic research into glycogen storage disease type I. [18] [19]

Personal life

Her husband, David H. Brown, was also a scientist and they collaborated on research on polysaccharide synthesis and glycogen storage diseases. [2]

Selected publications

Related Research Articles

<span class="mw-page-title-main">Glycogen storage disease type V</span> Human disease caused by deficiency of a muscle enzyme

Glycogen storage disease type V, also known as McArdle's disease, is a metabolic disorder, one of the metabolic myopathies, more specifically a muscle glycogen storage disease, caused by a deficiency of myophosphorylase. Its incidence is reported as one in 100,000, roughly the same as glycogen storage disease type I.

<span class="mw-page-title-main">Glycogen phosphorylase</span> Class of enzymes

Glycogen phosphorylase is one of the phosphorylase enzymes. Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.

<span class="mw-page-title-main">Glucose 1-phosphate</span> Chemical compound

Glucose 1-phosphate is a glucose molecule with a phosphate group on the 1'-carbon. It can exist in either the α- or β-anomeric form.

<span class="mw-page-title-main">Glycogen synthase</span> Enzyme class, includes all types of glycogen/starch synthases

Glycogen synthase is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase that catalyses the reaction of UDP-glucose and n to yield UDP and n+1.

<span class="mw-page-title-main">Glycogen debranching enzyme</span> Mammalian protein found in Homo sapiens

A debranching enzyme is a molecule that helps facilitate the breakdown of glycogen, which serves as a store of glucose in the body, through glucosyltransferase and glucosidase activity. Together with phosphorylases, debranching enzymes mobilize glucose reserves from glycogen deposits in the muscles and liver. This constitutes a major source of energy reserves in most organisms. Glycogen breakdown is highly regulated in the body, especially in the liver, by various hormones including insulin and glucagon, to maintain a homeostatic balance of blood-glucose levels. When glycogen breakdown is compromised by mutations in the glycogen debranching enzyme, metabolic diseases such as Glycogen storage disease type III can result.

<span class="mw-page-title-main">Glycogen branching enzyme</span> Mammalian protein involved in glycogen production

1,4-alpha-glucan-branching enzyme, also known as brancher enzyme or glycogen-branching enzyme is an enzyme that in humans is encoded by the GBE1 gene.

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

Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase “a” form over the less active glycogen phosphorylase b.

<span class="mw-page-title-main">PHKA2</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase regulatory subunit alpha, liver isoform is an enzyme that in humans is encoded by the PHKA2 gene.

<span class="mw-page-title-main">PHKG2</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase gamma catalytic chain, testis/liver isoform is an enzyme that in humans is encoded by the PHKG2 gene.

<span class="mw-page-title-main">Phosphorylase kinase, alpha 1</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKA1 gene. It is the muscle isoform of Phosphorylase kinase (PhK).

Immunophysics is a novel interdisciplinary research field using immunological, biological, physical and chemical approaches to elucidate and modify immune-mediated mechanisms and to expand our knowledge on the pathomechanisms of chronic immune-mediated diseases such as arthritis, inflammatory bowel disease, asthma and chronic infections.

David Mahan Knipe is the Higgins Professor of Microbiology and Molecular Genetics in the Department of Microbiology at the Harvard Medical School in Boston, Massachusetts and co-chief editor of the reference book Fields Virology. He returned to the Chair of the Program in Virology at Harvard Medical School in 2019, having previously held the position from 2004 through 2016 and served as interim Co-Chair of the Microbiology and Immunobiology Department from 2016 through 2018.

Jamey Marth is a molecular and cellular biologist. He is currently on the faculty of the SBP Medical Discovery Institute in La Jolla, California where he is Director of the Immunity and Pathogenesis program.

Glycogen phosphorylase, liver form (PYGL), also known as human liver glycogen phosphorylase (HLGP), is an enzyme that in humans is encoded by the PYGL gene on chromosome 14. This gene encodes a homodimeric protein that catalyses the cleavage of alpha-1,4-glucosidic bonds to release glucose-1-phosphate from liver glycogen stores. This protein switches from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 14. Activity of this enzyme is further regulated by multiple allosteric effectors and hormonal controls. Humans have three glycogen phosphorylase genes that encode distinct isozymes that are primarily expressed in liver, brain and muscle, respectively. The liver isozyme serves the glycemic demands of the body in general while the brain and muscle isozymes supply just those tissues. In glycogen storage disease type VI, also known as Hers disease, mutations in liver glycogen phosphorylase inhibit the conversion of glycogen to glucose and results in moderate hypoglycemia, mild ketosis, growth retardation and hepatomegaly. Alternative splicing results in multiple transcript variants encoding different isoforms [provided by RefSeq, Feb 2011].

BEAMing, which stands for beads, emulsion, amplification, magnetics, is a highly sensitive digital PCR method that combines emulsion PCR and flow cytometry to identify and quantify specific somatic mutations present in DNA.

<span class="mw-page-title-main">Member of the National Academy of Sciences</span> Award given by the National Academy of Sciences of the United States

Membership of the National Academy of Sciences is an award granted to scientists that the National Academy of Sciences (NAS) of the United States judges to have made “distinguished and continuing achievements in original research”. Membership is a mark of excellence in science and one of the highest honors that a scientist can receive.

Barbara Imperiali is a Professor of Biology and Chemistry at Massachusetts Institute of Technology and Affiliate Member of the Broad Institute. She is an elected member of the National Academy of Sciences and a Fellow of the Royal Society of Chemistry.

Paula Veronica Welander is a microbiologist and professor at Stanford University who is known for her research using lipid biomarkers to investigate how life evolved on Earth.

Barbara Baker is an American plant molecular geneticist working at the University of California, Berkeley and the United States Department of Agriculture She was elected to the National Academy of Sciences in 2021.

<span class="mw-page-title-main">Csaba Szabo (pharmacologist)</span>

Csaba Szabo, a physician and pharmacologist, is the Head of the Pharmacology Section of the University of Fribourg in Switzerland. The Public Library of Science Magazine, PLOS Biology, recognized Szabo in 2019 as one of the most cited researchers in the world.

References

  1. 1 2 3 "Brown, Barbara "Bobbie" (Illingworth)". madison.com. October 1, 2016.
  2. 1 2 3 4 5 6 7 Exton, John H. (2013). "Contributions of Barbara and David Brown". Crucible of science : the story of the Cori laboratory. New York: Oxford University Press. pp. 161–164. ISBN   978-0-19-986108-8. OCLC   843881801.
  3. ↑ Illingworth, Barbara A (1950). Effects of purified growth hormone on glycogen storage. New Haven. OCLC   42655887.{{cite book}}: CS1 maint: location missing publisher (link)
  4. ↑ "Wilbur Cross Medalists by Department" (PDF). Yale Graduate School of Arts and Sciences.
  5. ↑ "Washington University School of Medicine Bulletin". 1967.{{cite journal}}: Cite journal requires |journal= (help)
  6. ↑ "Dr. Brown Appointed to Council" (PDF). The NIH Record. 24 (4): 8. February 15, 1972.
  7. ↑ "List of Past Wilbur Cross Recipients | Yale Graduate School of Arts & Sciences". gsas.yale.edu.
  8. ↑ Illingworth, Barbara; Larner, Joseph; Cori, Gerty T. (1952-12-01). "Structure of Glycogens and Amylopectins: I. Enzymatic Determination of Chain Length*". Journal of Biological Chemistry. 199 (2): 631–640. doi: 10.1016/S0021-9258(18)38501-6 . ISSN   0021-9258. PMID   13022670.
  9. ↑ Illingworth, Barbara; Brown, David H.; Cori, Carl F. (1961-04-01). "The De Novo Synthesis of Polysaccharide by Phosphorylase". Proceedings of the National Academy of Sciences. 47 (4): 469–478. Bibcode:1961PNAS...47..469I. doi: 10.1073/pnas.47.4.469 . ISSN   0027-8424. PMC   221475 . PMID   13717528.
  10. ↑ Illingworth, Barbara; Jansz, Hendrik S.; Brown, David H.; Cori, Carl F. (1958-12-15). "Observations on the Function of Pyridoxal-5-Phosphate in Phosphorylase". Proceedings of the National Academy of Sciences. 44 (12): 1180–1191. Bibcode:1958PNAS...44.1180I. doi: 10.1073/pnas.44.12.1180 . ISSN   0027-8424. PMC   528705 . PMID   16590330.
  11. ↑ Brown, David H.; Illingworth, Barbara (1962-10-01). "The Properties of an Oligo-1,4 → 1,4-Glucantransferase from Animal Tissues". Proceedings of the National Academy of Sciences. 48 (10): 1783–1787. Bibcode:1962PNAS...48.1783B. doi: 10.1073/pnas.48.10.1783 . ISSN   0027-8424. PMC   221040 . PMID   14015933.
  12. ↑ Brown, David H.; Illingworth, Barbara; Cori, Carl F. (1963). "Enzymatic Debranching of Glycogen: Combined Action of Oligo-1,4→1,4-glucan-transferase and Amylo-1,6-glucosidase in Debranching Glycogen". Nature. 197 (4871): 980–982. Bibcode:1963Natur.197..980B. doi:10.1038/197980a0. ISSN   1476-4687. PMID   14015932. S2CID   4161911.
  13. ↑ Hauk, Rosalind; Illingworth, Barbara; Brown, David H.; Cori, Carl F. (1959-06-01). "Enzymes of glycogen synthesis in glycogen-deposition disease". Biochimica et Biophysica Acta. 33 (2): 554–556. doi:10.1016/0006-3002(59)90149-0. ISSN   0006-3002. PMID   13670930.
  14. ↑ Illingworth, Barbara; Kornfeld, Rosalind; Brown, David H. (1960). "Phosphorylase and uridinediphosphoglucose-glycogen transferase in pyridoxine deficiency". Biochimica et Biophysica Acta. 42: 486–489. doi:10.1016/0006-3002(60)90827-1. PMID   13717529.
  15. ↑ Correspondence with Carl Cori, David and Barbara Brown Papers, Collection FC179, Becker Archives, Washington University School of Medicine.
  16. ↑ Brockhoff, Dorothy (Spring 1971). "Her Present Is Her Health". Outlook Magazine. 8 (2): 16–18.
  17. ↑ Pagliara, Anthony S.; Karl, Irene E.; Keating, James P.; Brown, Barbara I.; Kipnis, David M. (1 August 1972). "Hepatic fructose-1,6-diphosphatase deficiency: A cause of lactic acidosis and hypoglycemia in infancy". The Journal of Clinical Investigation. 51 (8): 2115–2123. doi: 10.1172/JCI107018 . ISSN   0021-9738. PMC   292368 . PMID   4341015.
  18. ↑ Malatack, J. Jeffrey; Finegold, David N.; Iwatsuki, Shunzaburo; Shaw, Byers W.; Gartner, J. Carlton; Zitelli, Basil J.; Roe, Thomas; Starzl, Thomas E. (14 May 1983). "Liver Transplantation for Type I Glycogen Storage Disease". Lancet. 1 (8333): 1073–1075. doi:10.1016/s0140-6736(83)91910-4. ISSN   0140-6736. PMC   3022514 . PMID   6133106.
  19. ↑ Starzl, T E; Putnam, C W; Porter, K A; Halgrimson, C G; Corman, J; Brown, B I; Gotlin, R W; Rodgerson, D O; Greene, H L (October 1973). "Portal diversion for the treatment of glycogen storage disease in humans". Annals of Surgery. 178 (4): 525–539. doi:10.1097/00000658-197310000-00015. ISSN   0003-4932. PMC   1355694 . PMID   4517839.
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