scholarly journals Characterization of the Pharmaceutical Effect of Drugs on Atherosclerotic Lesions in Vivo Using Integrated Fluorescence Imaging and Raman Spectral Measurements

2014 ◽  
Vol 86 (8) ◽  
pp. 3863-3868 ◽  
Author(s):  
Yi-Cyun Yang ◽  
Wei-Tien Chang ◽  
Shao-Kang Huang ◽  
Ian Liau
Keyword(s):  
Fluorescence Imaging ◽  
Spectral Measurements ◽  
Atherosclerotic Lesions ◽  
Raman Spectral

scholarly journals Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions

Blood ◽  
1987 ◽  
Vol 69 (4) ◽  
pp. 1038-1045 ◽  
Author(s):  
A Bini ◽  
J Jr Fenoglio ◽  
J Sobel ◽  
J Owen ◽  
M Fejgl ◽  
...  
Keyword(s):  
Amino Acid ◽  
Total Protein ◽  
Cyanogen Bromide ◽  
Fibrinogen Concentration ◽  
Beta Chain ◽  
Amino Terminal ◽  
Atherosclerotic Lesions ◽  
Predominant Component

Abstract Arterial thrombi and atherosclerotic lesions were analyzed immunochemically and examined histologically. The extent of in vivo proteolytic cleavage of the amino-terminal end of fibrinogen by thrombin and plasmin was determined and quantitated by specific radioimmunoassays. The samples were treated with cyanogen bromide (CNBr), and the total amount of fibrinogen and fibrin-derived protein was determined as NDSK, the NH2-terminal disulfide knot of fibrinogen. Thrombin-releasable fibrinopeptides A and B were used to quantitate fibrinogen and fibrin I. Previous plasmin cleavage of the B beta chain was inferred from the amount of B beta 1–42 and B beta 15–42 in undigested NDSK. The results obtained in both acute and organized thrombi indicate that approximately 60% of the total protein (as determined by amino acid analysis) was fibrinogen-derived and that 70% to 80% of the fibrinogen-derived material was fibrin II. These findings support the hypothesis that fibrin II as distinct from fibrin I is the predominant component in a thrombus. In samples from normal and atherosclerotic aortas, fibrinogen-derived protein comprised less than 10% of the total protein. Samples from grossly normal aortas contained only fibrinogen and fibrin I. Fibrinogen concentration decreased and fibrin II concentration increased with increasing severity of the lesions, suggesting that increased fibrin II formation is associated with progression of atheromas.

scholarly journals Preparation and Characterization of Highly Fluorescent, Glutathione-coated Near Infrared Quantum Dots for in Vivo Fluorescence Imaging

2008 ◽  
Vol 9 (10) ◽  
pp. 2044-2061 ◽  
Author(s):  
Takashi Jin ◽  
Fumihiko Fujii ◽  
Yutaka Komai ◽  
Junji Seki ◽  
Akitoshi Seiyama ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Fluorescence Imaging ◽  
Near Infrared ◽  
In Vivo Fluorescence ◽  
In Vivo Fluorescence Imaging

scholarly journals Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions

Blood ◽  
1987 ◽  
Vol 69 (4) ◽  
pp. 1038-1045 ◽  
Author(s):  
A Bini ◽  
J Jr Fenoglio ◽  
J Sobel ◽  
J Owen ◽  
M Fejgl ◽  
...  
Keyword(s):  
Amino Acid ◽  
Total Protein ◽  
Cyanogen Bromide ◽  
Fibrinogen Concentration ◽  
Beta Chain ◽  
Amino Terminal ◽  
Atherosclerotic Lesions ◽  
Predominant Component

Arterial thrombi and atherosclerotic lesions were analyzed immunochemically and examined histologically. The extent of in vivo proteolytic cleavage of the amino-terminal end of fibrinogen by thrombin and plasmin was determined and quantitated by specific radioimmunoassays. The samples were treated with cyanogen bromide (CNBr), and the total amount of fibrinogen and fibrin-derived protein was determined as NDSK, the NH2-terminal disulfide knot of fibrinogen. Thrombin-releasable fibrinopeptides A and B were used to quantitate fibrinogen and fibrin I. Previous plasmin cleavage of the B beta chain was inferred from the amount of B beta 1–42 and B beta 15–42 in undigested NDSK. The results obtained in both acute and organized thrombi indicate that approximately 60% of the total protein (as determined by amino acid analysis) was fibrinogen-derived and that 70% to 80% of the fibrinogen-derived material was fibrin II. These findings support the hypothesis that fibrin II as distinct from fibrin I is the predominant component in a thrombus. In samples from normal and atherosclerotic aortas, fibrinogen-derived protein comprised less than 10% of the total protein. Samples from grossly normal aortas contained only fibrinogen and fibrin I. Fibrinogen concentration decreased and fibrin II concentration increased with increasing severity of the lesions, suggesting that increased fibrin II formation is associated with progression of atheromas.

scholarly journals In-vitro and in-vivo characterization of CRANAD-2 for multi-spectral optoacoustic tomography and fluorescence imaging of amyloid-beta deposits in Alzheimer mice

2020 ◽  
Author(s):  
Ruiqing Ni ◽  
Alessia Villois ◽  
Xose Luis Dean-Ben ◽  
Zhenyue Chen ◽  
Markus Vaas ◽  
...  
Keyword(s):  
Fluorescence Imaging ◽  
Quantitative Detection ◽  
Optoacoustic Tomography ◽  
Cerebral Amyloidosis ◽  
Amyloid Aβ ◽  
In Vivo Characterization ◽  
The Brain

AbstractThe abnormal deposition of fibrillar beta-amyloid (Aβ) deposits in the brain is one of the major histopathological hallmarks of Alzheimer’s disease (AD). Here we characterize curcumin-derivative CRANAD-2 for multi-spectral optoacoustic tomography (MSOT) and fluorescence imaging of brain Aβ deposits in the arcAβ mouse model of AD cerebral amyloidosis. CRANAD-2 shows a specific and quantitative detection of A fibrils in vitro, even in complex mixtures, and it is capable to distinguish between monomeric and fibrillar forms of A. In vivo epifluorescence and MSOT after intravenous CRANAD-2 administration demonstrated higher retention in arcAβ compared to non-transgenic littermate mice. Immunohistochemistry showed co-localization of CRANAD-2 and Aβ deposits in arcAβ mouse brain sections, thus verifying the specificity of the probe. In conclusion, we demonstrate suitability of CRANAD-2 for fluorescence- and MSOT-based detection of Aβ deposits in animal models of AD pathology, which facilitates mechanistic studies and the monitoring of putative treatments targeting Aβ deposits.

Functional characterization of human brown adipose tissue metabolism

2020 ◽  
Vol 477 (7) ◽  
pp. 1261-1286 ◽  
Author(s):  
Marie Anne Richard ◽  
Hannah Pallubinsky ◽  
Denis P. Blondin
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Functional Characterization ◽  
Human Infants ◽  
Positron Emission ◽  
Brown Adipose ◽  
Treatment Of Obesity ◽  
And Function

Brown adipose tissue (BAT) has long been described according to its histological features as a multilocular, lipid-containing tissue, light brown in color, that is also responsive to the cold and found especially in hibernating mammals and human infants. Its presence in both hibernators and human infants, combined with its function as a heat-generating organ, raised many questions about its role in humans. Early characterizations of the tissue in humans focused on its progressive atrophy with age and its apparent importance for cold-exposed workers. However, the use of positron emission tomography (PET) with the glucose tracer [18F]fluorodeoxyglucose ([18F]FDG) made it possible to begin characterizing the possible function of BAT in adult humans, and whether it could play a role in the prevention or treatment of obesity and type 2 diabetes (T2D). This review focuses on the in vivo functional characterization of human BAT, the methodological approaches applied to examine these features and addresses critical gaps that remain in moving the field forward. Specifically, we describe the anatomical and biomolecular features of human BAT, the modalities and applications of non-invasive tools such as PET and magnetic resonance imaging coupled with spectroscopy (MRI/MRS) to study BAT morphology and function in vivo, and finally describe the functional characteristics of human BAT that have only been possible through the development and application of such tools.

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