Aminopeptidase N/CD13 targeting fluorescent probes: Synthesis and application to tumor cell imaging

Zhang, Zhouen; Harada, Hiroshi; Tanabe, Kazuhito; Hatta, Hiroshi; Hiraoka, Masahiro; Nishimoto, S.

doi:10.1016/j.peptides.2005.03.049

Cited by 27 publications

(16 citation statements)

References 25 publications

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“…The specificity of the mouse monoclonal antibody to CD13 (WM15; BD Biosciences) was examined by comparing its staining pattern on cells to that obtained by using independently manufactured rabbit polyclonal antibody to CD13 (a gift from S. Roffler) (29); two patterns were almost indistinguishable. In addition, both antibodies specifically detected exogenously introduced CD13 in MDA-MB231 cells that were known to have very low endogenous CD13 (33). The specificity of the antibody to caveolin-1 was examined by staining cells transfected with caveolin-1 siRNA as demonstrated in Fig.…”

Section: Methodsmentioning

confidence: 99%

The Reversion-inducing Cysteine-rich Protein with Kazal Motifs (RECK) Interacts with Membrane Type 1 Matrix Metalloproteinase and CD13/Aminopeptidase N and Modulates Their Endocytic Pathways

Miki

Takegami

Okawa

et al. 2007

Journal of Biological Chemistry

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The reversion-inducing cysteine-rich protein with Kazal motifs (RECK) is anchored to the cell surface via glycosylphosphatidylinositol. This molecule antagonizes the function of membrane type 1 matrix metalloproteinase (MT1-MMP) to promote proMMP-2 maturation. Here, we attempt to clarify the mechanism underlying RECK functions. First, we found that RECK forms a complex with MT1-MMP and inhibits its proteolytic activity. Notably, RECK increases the amount of MT1-MMP that associates with detergent-resistant membranes during sucrose gradient ultracentrifugation. Furthermore, perturbation of membrane cholesterol significantly affected the function of RECK in suppressing MT1-MMP function. These findings indicate that RECK possibly regulates MT1-MMP function by modulating its behavior on the cell surface as well as by enzymatic action; this prompted us to find another molecule whose behavior in detergent-resistant membranes is influenced by RECK. Subsequently, we found that RECK interacts with CD13/aminopeptidase N. Further, we found that RECK inhibits the proteolytic activity of CD13 in a cholesterol perturbation-sensitive manner. Finally, we examined whether RECK influences the behavior of MT1-MMP and CD13 during their internalization from the cell surface. In the absence of RECK, MT1-MMP and CD13 were internalized along with the markers of clathrin-or caveolae-dependent endocytosis. However, interestingly, in the presence of RECK these molecules were internalized preferentially with an endocytic marker that is neither clathrin-nor caveolae-dependent, indicating that RECK modulates endocytic pathways of MT1-MMP and CD13. This modulation was correlated with the accelerated internalization and decay of MT1-MMP and CD13. This study unveils the novel function and target molecules of RECK.

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Section: Methodsmentioning

confidence: 99%

The Reversion-inducing Cysteine-rich Protein with Kazal Motifs (RECK) Interacts with Membrane Type 1 Matrix Metalloproteinase and CD13/Aminopeptidase N and Modulates Their Endocytic Pathways

Miki

Takegami

Okawa

et al. 2007

Journal of Biological Chemistry

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“…2, Bes-Green has a maximum absorption and emission peak at 450 and 550 nm in Tris-HCl buffer (pH 7.4), respectively. The Stokes shift (115 nm) is much larger than any current affinity-based APN probes [9,[18][19][20], which can substantially diminish the influence of excitation light in detections. Moreover, quantum yield of Bes-Green is 0.22 after careful examination.…”

Section: Resultsmentioning

confidence: 99%

A bestatin-based fluorescent probe for aminopeptidase N cell imaging

Chen

Wang

Qin

et al. 2015

Chinese Chemical Letters

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“…They demonstrated that this conjugate binds CD13 positive human umbilical vein endothelial cells (HUVEC) and that it can induce lysis of HUVECs upon incubation with human serum. Various conjugates of NGR peptides with fluorescent probes, contrast agents, and paramagnetic quantum dot particles have also been developed for imaging purposes [19,26,27,53].…”

Section: Other Ngr-conjugatesmentioning

confidence: 99%

“…For instance, peptides containing cyclic CNGRC and linear GNGRG motives have been used for delivering tumor necrosis factor alpha (TNF) [6][7][8], interferon gamma [9][10][11], and liposomal doxorubicin [12,13] to tumor neovasculature, improving their therapeutic properties. Other investigators have used the NGR motif embedded in similar or different molecular scaffolds for delivering chemotherapeutic drugs, antiangiogenic drugs, tissue factor, viruses and other compounds to tumor vessels [4,[14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Tumor Vasculature Targeting Through NGR Peptide-Based Drug Delivery Systems

Corti

Curnis

2011

CPB

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Various peptide sequences have been discovered by selecting peptide-phage display libraries in vitro against specific receptors or in vivo in tumor-bearing animals. One class of these peptides is characterized by the presence of Asn-Gly-Asp (NGR), a structural motif that can recognize the endothelium and other cells of neoangiogenic vessels. Because of this property these peptides have been used by several investigators to deliver a variety of drugs, cytokines, nanoparticles, viruses and imaging agents to tumor blood vessels. Here we review the reports on these conjugates and discuss the structural, functional and stability properties of NGR embedded into different molecular scaffolds.

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Aminopeptidase N/CD13 targeting fluorescent probes: Synthesis and application to tumor cell imaging

Cited by 27 publications

References 25 publications

The Reversion-inducing Cysteine-rich Protein with Kazal Motifs (RECK) Interacts with Membrane Type 1 Matrix Metalloproteinase and CD13/Aminopeptidase N and Modulates Their Endocytic Pathways

The Reversion-inducing Cysteine-rich Protein with Kazal Motifs (RECK) Interacts with Membrane Type 1 Matrix Metalloproteinase and CD13/Aminopeptidase N and Modulates Their Endocytic Pathways

A bestatin-based fluorescent probe for aminopeptidase N cell imaging

Tumor Vasculature Targeting Through NGR Peptide-Based Drug Delivery Systems

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