In vivo imaging of apoptosis

Blankenberg, Francis G.

doi:10.4161/cbt.7.10.6934

Cited by 61 publications

(51 citation statements)

References 61 publications

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“…For the detection of apoptosis in vivo, molecular imaging techniques were used to image caspase activity or phosphatidylserine (PS) exposure. 4,8 Imaging the activation of the caspase cascade such as caspase 3 activity has been demonstrated in animals using positron emission tomography (PET). 9,10 However, no human data have ever been published and caspase 3 activation is not necessarily unique to apoptosis.…”

Section: Introductionmentioning

confidence: 99%

“…11,12 On the other hand, the PS externalization is thought to be an early event in apoptosis that closely follows caspase 3 activation. 4 Annexin V has been the most widely used PS-targeting human protein and allows MRI-, optical-, radionuclide-, and PET-detection via superparamagnetic iron oxide nanoparticle-, fluorescence-, radio-, and ( 18 F)-labeled techniques, respectively. It has been used in phase I and phase II clinical trials as a potential early surrogate marker of therapeutic efficacy in nonsmall cell lung cancer and non-Hodgkin's lymphoma.…”

Section: Introductionmentioning

confidence: 99%

“…This apoptosome then activates a cascade of cellular destruction events, beginning with the activation of death-execution effector caspases, such as caspase 3, followed by the activation of downstream caspases, ultimately resulting in the hallmark of apoptosis including condensation of nuclear and cytoplasmic contents, fragmentation of nuclear DNA, and membrane blebbing. 3,4 Insight into the molecular mechanism of apoptosis has opened new avenues to develop diagnostic, prognostic, and therapeutic tools for management of human diseases. 1,5,6 For example, apoptosis-based therapies have been used in the treatment of degenerative, neoplastic, and autoimmune disorders.…”

Section: Introductionmentioning

confidence: 99%

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Increase of reduced nicotinamide adenine dinucleotide fluorescence lifetime precedes mitochondrial dysfunction in staurosporine-induced apoptosis of HeLa cells

Yu¹,

Guo²,

Wang

et al. 2011

J. Biomed. Opt.

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Abstract.In vivo noninvasive detection of apoptosis represents a new tool that may yield a more definite diagnosis, a more accurate prognosis, and help improve therapies for human diseases. The intrinsic fluorescence of reduced nicotinamide adenine dinucleotide (NADH) may be a potential optical biomarker for the apoptosis detection because NADH is involved in the respiration for the mitochondrial membrane potential ( ) formation and adenosine-5'-triphosphate (ATP) synthesis, and the depletion of and ATP level is the hallmark of apoptosis. We have previously observed the NADH fluorescence lifetime change is associated with staurosporine (STS)-induced mitochondria-mediated apoptosis. However, its relationship with mitochondrial functions such as , ATP, and oxygen consumption rate is not clear. In this study, we investigated this relationship. Our results indicate that the NADH fluorescence lifetime increased when and ATP levels were equal to or higher than their values of controls and decreased before the depletion of and ATP, and the oxygen consumption rate did not change. These findings suggest that the increased NADH fluorescence lifetime in STS-induced cell death occurred before the depletion of and ATP and activation of caspase 3, and was not simply caused by cellular metabolic change. Furthermore, the NADH fluorescence lifetime change is associated with the pace of apoptosis. C 2011 Society of Photo-Optical Instrumentation Engineers (SPIE).

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Increase of reduced nicotinamide adenine dinucleotide fluorescence lifetime precedes mitochondrial dysfunction in staurosporine-induced apoptosis of HeLa cells

Yu¹,

Guo²,

Wang

et al. 2011

J. Biomed. Opt.

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“…Since we know that an early marker of apoptosis is the redistribution of PS between inner and outer plasma membranes (PS externalization) (Reutelingsperger et al, 1995;Blankenberg, 2009), PS externalization is specific to apoptotic cells with the exception of activated platelets and erythrocytes. Therefore, it is an attractive target for apoptosis detection (Blankenberg, 2008(Blankenberg, , 2009Smrz et al, 2008) and as means of providing an early indication of the success or failure of therapy for prion diseases.…”

Section: Logicmentioning

confidence: 99%

Past and Future of Diagnosis and Therapy of Transmissible Spongiform Encephalopathy

Tseng¹,

Tuszyński²

2012

Miscellanea on Encephalopathies

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“…I t is known that the majority of small-molecule chemotherapeutics function by inducing apoptosis in cancer cells (1). Both in vitro and in vivo, apoptosis occurs rapidly, typically within 6-72 h after exposure to a chemotherapeutic (2,3). Many proteases are activated during apoptosis (4), although the key effectors are the caspases, cysteine proteases that cleave intracellular elements and lead to cell death (5).…”

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confidence: 99%

Circulating proteolytic signatures of chemotherapy-induced cell death in humans discovered by N-terminal labeling

Wiita¹,

Hsu²,

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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It is known that many chemotherapeutics induce cellular apoptosis over hours to days. During apoptosis, numerous cellular proteases are activated, most canonically the caspases. We speculated that detection of proteolytic fragments released from apoptotic cells into the peripheral blood may serve as a unique indicator of chemotherapy-induced cell death. Here we used an enzymatic labeling process to positively enrich free peptide α-amines in the plasma of hematologic malignancy patients soon after beginning treatment. This N-terminomic approach largely avoids interference by high-abundance proteins that complicate traditional plasma proteomic analyses. Significantly, by mass spectrometry methods, we found strong biological signatures of apoptosis directly in the postchemotherapy plasma, including numerous caspase-cleaved peptides as well as relevant peptides from apoptotic and cell-stress proteins second mitochondria-derived activator of caspases, HtrA serine peptidase 2, and activating transcription factor 6. We also treated hematologic cancer cell lines with clinically relevant chemotherapeutics and monitored proteolytic fragments released into the media. Remarkably, many of these peptides coincided with those found in patient samples. Overall, we identified 153 proteolytic peptides in postchemotherapy patient plasma as potential indicators of cellular apoptosis. Through targeted quantitative proteomics, we verified that many of these peptides were indeed increased post-vs. prechemotherapy in additional patients. Our findings reveal that numerous proteolytic fragments are released from dying tumor cells. Monitoring posttreatment proteolysis may lead to a novel class of inexpensive, rapid biomarkers of cell death.

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In vivo imaging of apoptosis

Cited by 61 publications

References 61 publications

Increase of reduced nicotinamide adenine dinucleotide fluorescence lifetime precedes mitochondrial dysfunction in staurosporine-induced apoptosis of HeLa cells

Increase of reduced nicotinamide adenine dinucleotide fluorescence lifetime precedes mitochondrial dysfunction in staurosporine-induced apoptosis of HeLa cells

Past and Future of Diagnosis and Therapy of Transmissible Spongiform Encephalopathy

Circulating proteolytic signatures of chemotherapy-induced cell death in humans discovered by N-terminal labeling

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