Biodistribution of intracellularly acting peptides conjugated reversibly to Tat

Begley, Rebecca; Liron, Tamar; Baryza, Jeremy; Mochly‐Rosen, Daria

doi:10.1016/j.bbrc.2004.04.121

Cited by 77 publications

(93 citation statements)

References 38 publications

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“…In some animals, TAT 47-57 -conjugated RRNYRRNY or TAT 47-57 -conjugated RRPPYN control was administered by an i.p. injection (20 nmol in 200 μL of saline) 20 min before coronary artery occlusion, as indicated (19). At the end of the protocol, mice were heparinized and the hearts were rapidly excised and immersed into ice-cold saline (∼4°C).…”

Section: Methodsmentioning

confidence: 99%

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RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K ⁺ channels

Rottlaender

Boengler²,

Wolny³

et al. 2011

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

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Section: Methodsmentioning

confidence: 99%

“…injection into mice. To facilitate rapid biodistribution and in vivo transduction into cardiomyocytes, the peptide was conjugated to TAT 47-57 as an intracellular carrier (19,20). TAT 47-57 -conjugated RRPPYN served as a control (13,19).…”

Section: See Retraction Published December 10 2012mentioning

confidence: 99%

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K ⁺ channels

Rottlaender

Boengler²,

Wolny³

et al. 2011

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

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“…To further establish the requirement of PKC⑀ in this response, we used a pharmacological approach. The cell-permeable, Tat-fused peptide ⑀V1-2 selectively blocks the translocation and activation of PKC⑀ but not of other PKCs (40). As shown in Fig.…”

Section: Pkc⑀ Is Required For Tnf␣-induced Activation Of Nf-b In Lncapmentioning

confidence: 86%

Activation of Nuclear Factor κB (NF-κB) in Prostate Cancer Is Mediated by Protein Kinase C ϵ (PKCϵ)

Garg

Blando

Pérez

et al. 2012

Journal of Biological Chemistry

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Background: PKC⑀, a potential oncogene, is up-regulated in prostate cancer. Results: PKC⑀ facilitates the formation of TNFR-I complex to regulate the NF-B pathway via a C1 domain/diacylglycerol-dependent mechanism. Conclusion: PKC⑀ is an upstream regulator of NF-B signaling in prostate cancer. Significance: Mechanisms identified here may reveal novel PKC⑀ effectors that contribute to prostate cancer progression and highlight the potential relevance of this pathway for therapeutic purposes.

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“…Isozyme Selectivity in Vivo-To determine that activator peptides causing MARCKS phosphorylation and decreasing ischemia-reperfusion damage in heart also induce ⑀PKC translocation in vivo, we injected the respective peptides at 20 nmol in 200 l of saline into the peritoneum of 15-20 g mice, as reported previously (48). Fifteen minutes later, the mice were sacrificed, and heart and brain were collected.…”

Section: Methodsmentioning

confidence: 99%

“…Fifteen minutes later, the mice were sacrificed, and heart and brain were collected. Soluble and particulate fractions from mouse tissue were prepared as described previously (48). ␣-, ⑀-, -, and ␦PKC translocations were determined by Western blot analysis using selective anti-PKC antibodies from Santa Cruz Biotechnology and used at a 1:500 dilution.…”

Section: Methodsmentioning

confidence: 99%

Peptides Derived from the C2 Domain of Protein Kinase Cϵ (ϵPKC) Modulate ϵPKC Activity and Identify Potential Protein-Protein Interaction Surfaces

Brandman

Disatnik

Churchill

et al. 2007

Journal of Biological Chemistry

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Peptides derived from protein kinase C (PKC) modulate its activity by interfering with critical protein-protein interactions within PKC and between PKC and PKC-binding proteins (Souroujon, M. C., and Mochly-Rosen, D. (1998) Nat. Biotechnol. 16, 919 -924). We previously demonstrated that the C2 domain of PKC plays a critical role in these interactions. By focusing on ⑀PKC and using a rational approach, we then identified one C2-derived peptide that acts as an isozyme-selective activator and another that acts as a selective inhibitor of ⑀PKC. These peptides were used to identify the role of ⑀PKC in protection from cardiac and brain ischemic damage, in prevention of complications from diabetes, in reducing pain, and in protecting transplanted hearts. The efficacy of these two peptides led us to search for additional C2-derived peptides with PKC-modulating activities. Here we report on the activity of a series of 5-9-residue peptides that are derived from regions that span the length of the C2 domain of ⑀PKC. These peptides were tested for their effect on PKC activity in cells in vivo and in an ex vivo model of acute ischemic heart disease. Most of the peptides acted as activators of PKC, and a few peptides acted as inhibitors. PKC-dependent myristoylated alanine-rich C kinase substrate phosphorylation in ⑀PKC knock-out cells revealed that only a subset of the peptides were selective for ⑀PKC over other PKC isozymes. These ⑀PKC-selective peptides were also protective of the myocardium from ischemic injury, an ⑀PKC-dependent function (Liu, G. S., Cohen, M. V., Mochly-Rosen, D., and Downey, J. M. (1999) J. Mol. Cell. Cardiol. 31, 1937-1948), and caused selective translocation of ⑀PKC over other isozymes when injected systemically into mice. Examination of the structure of the C2 domain from ⑀PKC revealed that peptides with similar activities clustered into discrete regions within the domain. We propose that these regions represent surfaces of protein-protein interactions within ⑀PKC and/or between ⑀PKC and other partner proteins; some of these interactions are unique to ⑀PKC, and others are common to other PKC isozymes.The protein kinase C (PKC) 3 family of serine/threonine protein kinases is involved in normal cell functions such as apoptosis (3, 4), cell proliferation (5-7), and secretion (8), as well as in disease states such as ischemic heart disease (9 -12) and stroke (13,14). PKC activation is associated with binding to the negatively charged phospholipids, phosphatidylserine, and different PKC isozymes have varying sensitivities to Ca 2ϩ and lipid-derived second messengers such as diacylglycerol (15). Upon activation, PKC isozymes translocate from the soluble to the particulate cell fraction (16), including cell membrane, nucleus (17), and mitochondria (18).PKC primary sequence can be broadly separated into two domains as follows: the N-terminal regulatory domain and the conserved C-terminal catalytic domain. The regulatory domain of PKC is composed of the C1 and C2 domains that mediate PKC interactions with se...

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Biodistribution of intracellularly acting peptides conjugated reversibly to Tat

Cited by 77 publications

References 38 publications

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K ⁺ channels

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K ⁺ channels

Activation of Nuclear Factor κB (NF-κB) in Prostate Cancer Is Mediated by Protein Kinase C ϵ (PKCϵ)

Peptides Derived from the C2 Domain of Protein Kinase Cϵ (ϵPKC) Modulate ϵPKC Activity and Identify Potential Protein-Protein Interaction Surfaces

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Biodistribution of intracellularly acting peptides conjugated reversibly to Tat

Cited by 77 publications

References 38 publications

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K + channels

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K + channels

Activation of Nuclear Factor κB (NF-κB) in Prostate Cancer Is Mediated by Protein Kinase C ϵ (PKCϵ)

Peptides Derived from the C2 Domain of Protein Kinase Cϵ (ϵPKC) Modulate ϵPKC Activity and Identify Potential Protein-Protein Interaction Surfaces

Contact Info

Product

Resources

About

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K ⁺ channels

RETRACTED: Glycogen synthase kinase 3β transfers cytoprotective signaling through connexin 43 onto mitochondrial ATP-sensitive K ⁺ channels