Faculty of Medicine

Molecular Medicine

These images were obtained by Dr Valentina Caorsi using the FILM facility, and were published in the FILM calendar 2010. 

They represent different views of skeletal muscle obtained with a Leica SP5 upright microscope. One image was obtained by Second Harmonic Generation and using two-photon excitation at 850 nm to alter the fibre shape. The other images were obtained by using fluorescent labels on actin, on the myosin essential light chain or on myosin's reactive thiol SH1. The 'square' was obtained by photobleaching, to investigate the existence of FRET between two of the labels, thus demonstrating that their labelling sites are less than 10 nm apart.

  • Psoas skeletal muscle fibre labelled with Alexa488 on the essential light chain and Rhodamine Phalloidin on actin
  • Psoas skeletal muscle fibre labelled with Alexa594 on SH1
  • Psoas skeletal muscle fibre labelled with Alexa594 on SH1
  • Psoas skeletal muscle fibre

The Section of Molecular Medicine (MM) was created in August 2007, as a result of the merging of the sections of Molecular and Cellular Medicine and Biological Nanoscience. The Section is housed in the Sir Alexander Fleming Building on the South Kensington Campus of Imperial College. Most laboratories are found on the 2nd floor. MM regroups scientists with interests in fundamental aspects of cell and molecular biology, enhanced by expertise in physiology, biophysics, spectroscopy, single molecule imaging and state-of-the-art microscopies. The work extends research in the basic sciences at the National Heart and Lung Institute.

Current Principal Investigators in the Section include:

Research in the section is principally funded from programme and project grants from Research Councils (MRC, BBSRC) and charities (Wellcome Trust, British Heart Foundation and others).

Molecular Medicine Section - July 2009

Molecular Medicine Section - July 2009


Eighty six people currently work in the Section (March 2010), including 11 heads of laboratories, 26 PhD students, 23 Postdocs and researchers, 6 technicians and a number of MRes students, visitors and honorary researchers. Section Administrator Peter Moore 020 7594 3175 (Room 360)

Selected publications

Ali BR; Xu H; Akawi NA; John A; Karuvantevida NS; Langer R; Al-Gazali L; Leitinger B. (1 Jun 2010). Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients. Hum Mol Genet. 19:2239-2250.

Barclay, C.J., Woledge, R.C. & Curtin, N.A. (2010). Inferring crossbridge properties from skeletal muscle energetics. Progress in Biophysics and Molecular Biology 102, 53-71.

Cebecauer M; Spitaler M; Sergé A; Magee AI. (1 Feb 2010). Signalling complexes and clusters: functional advantages and methodological hurdles. J Cell Sci. 123:309-320

Frasa MA; Maximiano FC; Smolarczyk K; Frances RE; Betson ME; Lozano E; Goldenring J; Seabra MC; Rak A; Ahmadian MR & Braga VMM. (2010) Armus is a Rac1 effector protein that inactivates Rab7 and regulates E-cadherin degradation. Cur. Biol. 20(3):198-208.

Ko CW, Wei ZQ, Marsh RJ, Armoogum DA, Nicolaou N, Bain AJ, Zhou AW, Ying LM. (2009) Probing nanosecond motions of plasminogen activator inhibitor-1 by time-resolved fluorescence anisotropy. Mol. BioSyst., 5, 1025-1031.

Luther PK, Bennett PM, Knupp C, Craig R, Padrón R, Harris SP, Patel J, and Moss RJ. 2008. Understanding the organisation and role of myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscle. J Mol Biol. 384:60-72.

West TG, Hild G, Siththanandan VB, Webb MR, Corrie JET, Ferenczi MA (2009)  The time-course and strain dependence of ADP release during contraction of permeabilized muscle fibers. Biophysical Journal 96: 3281-3294.

 
FILM
FILM, the Facility for Imaging by Light Microscopy, is also hosted in the section.  FILM provides two wide-field and six confocal microscopes, with a variety of configurations, for achieving the highest quality images. We have upright and inverted microscopes, FLIM and FRET for a wide range of fluorophores, environmental chambers for live cell imaging, imaging software and data storage. FILM is run by Dr Martin Spitaler and a full time assistant.
Fluorescence Life Time Image

Fluorescence Life Time Image

Fluorescence Life Time Image of a mammalian muscle fibre labelled with a fluorescent nucleotide analogue. The striations are characteristic of skeletal muscle and reveal the sarcomeres, the repeating units containing the arrays of protein filaments responsible for muscle contraction. The nucleotide binds to the active site of myosin and the life-time reveals the ability of the myosin to interact with actin.
(DI García, PMP Lanigan, MR Webb, TG West, J Requejo Isidro, E Auksorius, CW Dunsby, MAA Neil, PMW French, MA Ferenczi (2007) Fluorescence lifetime imaging to detect actomyosin states in mammalian muscle sarcomeres. Biophysical Journal 93: 2091-2101.)