Near-infrared scattering spectrum differences between benign and malignant breast tumors measured in vivo with diffuse tomography

Author(s):  
Brian W. Pogue ◽  
Shudong Jiang ◽  
Xiaomei Song ◽  
Subhadra Srinivasan ◽  
Hamid Dehghani ◽  
...  
2006 ◽  
Vol 11 (4) ◽  
pp. 044005 ◽  
Author(s):  
Albert Cerussi ◽  
Natasha Shah ◽  
David Hsiang ◽  
Amanda Durkin ◽  
John Butler ◽  
...  

2009 ◽  
Vol 14 (2) ◽  
pp. 024020 ◽  
Author(s):  
Regine Choe ◽  
Soren D. Konecky ◽  
Alper Corlu ◽  
Kijoon Lee ◽  
Turgut Durduran ◽  
...  

2013 ◽  
Vol 18 (8) ◽  
pp. 089801
Author(s):  
Julia Eva Mathejczyk ◽  
Jutta Pauli ◽  
Christian Dullin ◽  
Ute Resch-Genger ◽  
Frauke Alves ◽  
...  

2005 ◽  
Vol 4 (5) ◽  
pp. 513-526 ◽  
Author(s):  
Subhadra Srinivasan ◽  
Brian W. Pogue ◽  
Ben Brooksby ◽  
Shudong Jiang ◽  
Hamid Dehghani ◽  
...  

Multi-wavelength Near-Infrared (NIR) Tomography was utilized in this study to non-invasively quantify physiological parameters of breast tumors using direct spectral reconstruction. Frequency domain NIR measurements were incorporated with a new spectrally constrained direct chromophore and scattering image reconstruction algorithm, which was validated in simulations and experimental phantoms. Images of total hemoglobin, oxygen saturation, water, and scatter parameters were obtained with higher accuracy than previously reported. Using this spectral approach, in vivo NIR images are presented and interpreted through a series of case studies (n=6 subjects) having differing abnormalities. The corresponding mammograms and ultrasound images are also evaluated. Three of six cases were malignant (infiltrating ductal carcinomas) and showed higher hemoglobin (34–86% increase), a reduction in oxygen saturation, an increase in water content as well as scatter changes relative to surrounding normal tissue. Three of six cases were benign, two of which were diagnosed with fibrocystic disease and showed a dominant contrast in water, consistent with fluid filled cysts. Scatter amplitude was the main source of contrast in the volunteer with the benign condition fibrosis, which typically contains denser collagen tissue. The changes monitored correspond to physiological changes associated with angiogenesis, hypoxia and cell proliferation anticipated in cancers. These changes represent potential diagnostic indicators, which can be assessed to characterize breast tumors.


2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


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