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Nancy Hogg

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Nancy Hogg FMedSci is an immunologist who has made major contributions in the field of adhesion molecules, focusing on the integrins expressed by leukocytes.[1] Hogg was elected to the Academy of Medical Sciences in 2002 and currently holds an emeritus position at the Francis Crick Institute, London.

Nancy Hogg
Known forStudy of Leukocyte Integrins
Scientific career
FieldsImmunology

Education and academic career

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Nancy Hogg studied for a BSc at the University of Toronto. She was awarded a PhD working with Rodney Porter firstly at the University of London and then at Department of Biochemistry, University of Oxford. This was followed by a post–doctoral period at National Institute for Medical Research and finally a position at the Imperial Cancer Research Fund (which became Cancer Research UK London Research Institute and is now part of the Francis Crick Institute). Hogg was located initially at University College London followed by a move to the main laboratories in Lincoln’s Inn Fields where she set up her laboratory focusing initially on the function of macrophages, but then increasingly on the adhesion molecules termed integrins expressed by all leukocytes.

Research interests

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Nancy Hogg’s PhD project involved the protein sequencing of immunoglobulin heavy chains identifying for the first time the heterogeneity that accounts for immunoglobulin specificity.[2] During a postdoctoral period at the Imperial Cancer Research Fund she co-discovered the protein that is now known as fibronectin.[3] Through study of leukocyte integrin LFA-1 and particularly special mAb 24, Hogg was the first to document that the state of integrin activity could be controlled by bound divalent cations.[4][5] The active forms are linked to different cytoskeletal proteins, namely talin for high affinity and a-actinin for clustered intermediate affinity LFA-1 .[6][7] The lab showed that the LFA-1 ligand ICAM-1 was a target for pathogen binding, for example the malaria parasite Plasmodium falciparum.[8] The generation of LFA-1 null mice revealed the central role of LFA-1 in leukocyte migration within lymph nodes in vivo.[9][10] Hogg also first identified and characterised unique Leukocyte Adhesion Deficiency-III patients that expressed inactive leukocyte integrins.[11] This integrin malfunction was due to mutation in protein kindlin-3.[12]

Hogg has also studied the S100A8/S100A9 proteins that constitute 45% of neutrophil cytosolic protein.[13][14] S100a9 null mice demonstrated that myeloid cells could function relatively normally without these proteins but they had a major role in responding to infections such as Streptococcus pneumoniae in terms of cytokine generation.[15]

Professional associations and awards

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  • Member of British Society of Immunology[16]
  • 1996 Co-founder of UK Adhesion Society, now UK Cell Adhesion Society[17]
  • In 2002 Hogg was elected to Academy of Medical Sciences.[1]
  • In 2013 Hogg was awarded the William Harvey Medal

References

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  1. ^ a b "Professor Nancy Hogg | The Academy of Medical Sciences". acmedsci.ac.uk. Retrieved 16 February 2019.
  2. ^ Press, E. M.; Hogg, N. M. (23 August 1969). "Comparative study of two immunoglobulin G Fd-fragments". Nature. 223 (5208): 808–810. Bibcode:1969Natur.223..807P. doi:10.1038/223807a0. ISSN 0028-0836. PMID 5799021. S2CID 4255320.
  3. ^ Hogg, Nancy M. (February 1974). "A Comparison of Membrane Proteins of Normal and Transformed Cells by Lactoperoxidase Labeling". Proceedings of the National Academy of Sciences of the United States of America. 71 (2): 489–492. Bibcode:1974PNAS...71..489H. doi:10.1073/pnas.71.2.489. ISSN 0027-8424. PMC 388032. PMID 4360946.
  4. ^ Dransfield, I; Hogg, N (1 December 1989). "Regulated expression of Mg2+ binding epitope on leukocyte integrin alpha subunits". The EMBO Journal. 8 (12): 3759–3765. doi:10.1002/j.1460-2075.1989.tb08552.x. ISSN 0261-4189. PMC 402061. PMID 2479549.
  5. ^ Dransfield, I.; Cabañas, C.; Craig, A.; Hogg, N. (1 January 1992). "Divalent cation regulation of the function of the leukocyte integrin LFA-1". The Journal of Cell Biology. 116 (1): 219–226. doi:10.1083/jcb.116.1.219. ISSN 0021-9525. PMC 2289255. PMID 1346139.
  6. ^ Stanley, Paula; Smith, Andrew; McDowall, Alison; Nicol, Alastair; Zicha, Daniel; Hogg, Nancy (9 January 2008). "Intermediate-affinity LFA-1 binds α-actinin-1 to control migration at the leading edge of the T cell". The EMBO Journal. 27 (1): 62–75. doi:10.1038/sj.emboj.7601959. ISSN 0261-4189. PMC 2147999. PMID 18079697.
  7. ^ Smith, Andrew; Carrasco, Yolanda R.; Stanley, Paula; Kieffer, Nelly; Batista, Facundo D.; Hogg, Nancy (4 July 2005). "A talin-dependent LFA-1 focal zone is formed by rapidly migrating T lymphocytes". The Journal of Cell Biology. 170 (1): 141–151. doi:10.1083/jcb.200412032. ISSN 0021-9525. PMC 2171377. PMID 15983060.
  8. ^ Hogg, Nancy; Newbold, Christopher I.; Marsh, Kevin; Sternberg, Michael J. E.; Bates, Paul A.; Craig, Alister G.; McDowall, Alison; Berendt, Anthony R. (10 January 1992). "The binding site on ICAM-1 for plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site". Cell. 68 (1): 71–81. doi:10.1016/0092-8674(92)90207-S. ISSN 0092-8674. PMID 1370656. S2CID 21267258.
  9. ^ Berlin-Rufenach, Cornelia; Otto, Florian; Mathies, Meg; Westermann, Juergen; Owen, Michael J.; Hamann, Alf; Hogg, Nancy (3 May 1999). "Lymphocyte Migration in Lymphocyte Function-associated Antigen (LFA)-1–deficient Mice". The Journal of Experimental Medicine. 189 (9): 1467–1478. doi:10.1084/jem.189.9.1467. ISSN 0022-1007. PMC 2193056. PMID 10224287.
  10. ^ Reichardt, Peter; Patzak, Irene; Jones, Kristian; Etemire, Eloho; Gunzer, Matthias; Hogg, Nancy (20 March 2013). "A role for LFA-1 in delaying T-lymphocyte egress from lymph nodes". The EMBO Journal. 32 (6): 829–843. doi:10.1038/emboj.2013.33. ISSN 0261-4189. PMC 3604724. PMID 23443048.
  11. ^ Hogg, Nancy; Stewart, Mairi P.; Scarth, Sarah L.; Newton, Rebecca; Shaw, Jacqueline M.; Law, S.K. Alex; Klein, Nigel (1 January 1999). "A novel leukocyte adhesion deficiency caused by expressed but nonfunctional β2 integrins Mac-1 and LFA-1". Journal of Clinical Investigation. 103 (1): 97–106. doi:10.1172/JCI3312. ISSN 0021-9738. PMC 407855. PMID 9884339.
  12. ^ Svensson, Lena; Howarth, Kimberley; McDowall, Alison; Patzak, Irene; Evans, Rachel; Ussar, Siegfried; Moser, Markus; Metin, Ayse; Fried, Mike (March 2009). "Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation". Nature Medicine. 15 (3): 306–312. doi:10.1038/nm.1931. ISSN 1078-8956. PMC 2680140. PMID 19234463.
  13. ^ Hogg, N.; Freemont, P.; Bennett, R.; Gorman, M.; Edgeworth, J. (25 April 1991). "Identification of p8,14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells". Journal of Biological Chemistry. 266 (12): 7706–7713. doi:10.1016/S0021-9258(20)89506-4. ISSN 0021-9258. PMID 2019594.
  14. ^ Hobbs, Josie A. R.; May, Richard; Tanousis, Kiki; McNeill, Eileen; Mathies, Margaret; Gebhardt, Christoffer; Henderson, Robert; Robinson, Matthew J.; Hogg, Nancy (April 2003). "Myeloid Cell Function in MRP-14 (S100A9) Null Mice". Molecular and Cellular Biology. 23 (7): 2564–2576. doi:10.1128/MCB.23.7.2564-2576.2003. ISSN 0270-7306. PMC 150714. PMID 12640137.
  15. ^ De Filippo, Katia; Neill, Daniel R.; Mathies, Meg; Bangert, Mathieu; McNeill, Eileen; Kadioglu, Aras; Hogg, Nancy (28 April 2014). "A new protective role for S100A9 in regulation of neutrophil recruitment during invasive pneumococcal pneumonia". The FASEB Journal. 28 (8): 3600–3608. doi:10.1096/fj.13-247460. ISSN 0892-6638. PMID 24776746. S2CID 23158329.
  16. ^ "British Society for Immunology |". www.immunology.org. Retrieved 16 February 2019.
  17. ^ "ukcelladhesion". Retrieved 16 February 2019.
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