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  1. Article ; Online: In vivo bio-imaging using chlorotoxin-based conjugates.

    Stroud, Mark R / Hansen, Stacey J / Olson, James M

    Current pharmaceutical design

    2011  Volume 17, Issue 38, Page(s) 4362–4371

    Abstract: Surgical resection remains the primary component of cancer therapy. The precision required to successfully separate cancer tissue from normal tissue relies heavily on the surgeon's ability to delineate the tumor margins. Despite recent advances in ... ...

    Abstract Surgical resection remains the primary component of cancer therapy. The precision required to successfully separate cancer tissue from normal tissue relies heavily on the surgeon's ability to delineate the tumor margins. Despite recent advances in surgical guidance and monitoring systems, intra-operative identification of these margins remains imprecise and directly influences patient prognosis. If the surgeon had improved tools to distinguish these margins, tumor progression and unacceptable morbidity could be avoided. In this article, we review the history of chlorotoxin and its tumor specificity and discuss the research currently being generated to target optical imaging agents to cancer tissue.
    MeSH term(s) Amino Acid Sequence ; Animals ; Brain Neoplasms/metabolism ; Brain Neoplasms/pathology ; Brain Neoplasms/surgery ; Contrast Media/chemistry ; Contrast Media/pharmacokinetics ; Diagnostic Imaging/instrumentation ; Diagnostic Imaging/methods ; Fluorescent Dyes/chemistry ; Humans ; Intraoperative Care/instrumentation ; Intraoperative Care/methods ; Models, Molecular ; Molecular Sequence Data ; Nanoparticles ; Protein Binding ; Scorpion Venoms/chemistry ; Scorpion Venoms/isolation & purification ; Scorpion Venoms/pharmacokinetics ; Spectrometry, Fluorescence
    Chemical Substances Contrast Media ; Fluorescent Dyes ; Scorpion Venoms ; Chlorotoxin (06UV5RFW57)
    Language English
    Publishing date 2011-12-28
    Publishing country United Arab Emirates
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1304236-1
    ISSN 1873-4286 ; 1381-6128
    ISSN (online) 1873-4286
    ISSN 1381-6128
    DOI 10.2174/138161211798999375
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4714: Show issues Location:
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  2. Article ; Online: Chemical re-engineering of chlorotoxin improves bioconjugation properties for tumor imaging and targeted therapy.

    Akcan, Muharrem / Stroud, Mark R / Hansen, Stacey J / Clark, Richard J / Daly, Norelle L / Craik, David J / Olson, James M

    Journal of medicinal chemistry

    2011  Volume 54, Issue 3, Page(s) 782–787

    Abstract: Bioconjugates composed of chlorotoxin and near-infrared fluorescent (NIRF) moieties are being advanced toward human clinical trials as intraoperative imaging agents that will enable surgeons to visualize small foci of cancer. In previous studies, the ... ...

    Abstract Bioconjugates composed of chlorotoxin and near-infrared fluorescent (NIRF) moieties are being advanced toward human clinical trials as intraoperative imaging agents that will enable surgeons to visualize small foci of cancer. In previous studies, the NIRF molecules were conjugated to chlorotoxin, which results in a mixture of mono-, di-, and trilabeled peptide. Here we report a new chemical entity that bound only a single NIRF molecule. The lysines at positions 15 and 23 were substituted with either alanine or arginine, which resulted in only monolabeled peptide that was functionally equivalent to native chlorotoxin/Cy5.5. We also analyzed the serum stability and serum half-life of cyclized chlorotoxin, which showed an 11 h serum half-life and resulted in a monolabeled product. Based on these data, we propose to advance a monolabeled chlorotoxin to human clinical trials.
    MeSH term(s) Alanine/chemistry ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Arginine/chemistry ; Brain Neoplasms/diagnosis ; Brain Neoplasms/therapy ; Carbocyanines/chemistry ; Fluorescent Dyes/chemistry ; Half-Life ; Lysine/chemistry ; Medulloblastoma/diagnosis ; Medulloblastoma/therapy ; Mice ; Mice, Inbred C57BL ; Models, Molecular ; Molecular Sequence Data ; Peptides/blood ; Peptides/chemistry ; Peptides, Cyclic/blood ; Peptides, Cyclic/chemistry ; Scorpion Venoms/blood ; Scorpion Venoms/chemistry
    Chemical Substances CY5.5 cyanine dye ; Carbocyanines ; Fluorescent Dyes ; Peptides ; Peptides, Cyclic ; Scorpion Venoms ; Chlorotoxin (06UV5RFW57) ; Arginine (94ZLA3W45F) ; Lysine (K3Z4F929H6) ; Alanine (OF5P57N2ZX)
    Language English
    Publishing date 2011-01-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/jm101018r
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Preclinical Validation of the Utility of BLZ-100 in Providing Fluorescence Contrast for Imaging Spontaneous Solid Tumors.

    Fidel, Janean / Kennedy, Katie C / Dernell, William S / Hansen, Stacey / Wiss, Valorie / Stroud, Mark R / Molho, Joshua I / Knoblaugh, Sue E / Meganck, Jeffrey / Olson, James M / Rice, Brad / Parrish-Novak, Julia

    Cancer research

    2014  Volume 75, Issue 20, Page(s) 4283–4291

    Abstract: There is a need in surgical oncology for contrast agents that can enable real-time intraoperative visualization of solid tumors that can enable complete resections while sparing normal surrounding tissues. The Tumor Paint agent BLZ-100 is a peptide- ... ...

    Abstract There is a need in surgical oncology for contrast agents that can enable real-time intraoperative visualization of solid tumors that can enable complete resections while sparing normal surrounding tissues. The Tumor Paint agent BLZ-100 is a peptide-fluorophore conjugate that can specifically bind solid tumors and fluoresce in the near-infrared range, minimizing light scatter and signal attenuation. In this study, we provide a preclinical proof of concept for use of this imaging contrast agent as administered before surgery to dogs with a variety of naturally occurring spontaneous tumors. Imaging was performed on excised tissues as well as intraoperatively in a subset of cases. Actionable contrast was achieved between tumor tissue and surrounding normal tissues in adenocarcinomas, squamous cell carcinomas, mast cell tumors, and soft tissue sarcomas. Subcutaneous soft tissue sarcomas were labeled with the highest fluorescence intensity and greatest tumor-to-background signal ratio. Our results establish a foundation that rationalizes clinical studies in humans with soft tissue sarcoma, an indication with a notably high unmet need.
    MeSH term(s) Adolescent ; Animals ; Child ; Child, Preschool ; Contrast Media/administration & dosage ; Diagnostic Imaging/instrumentation ; Diagnostic Imaging/methods ; Disease Models, Animal ; Dogs ; Female ; Fluorescent Dyes/administration & dosage ; Humans ; Indocyanine Green/administration & dosage ; Indocyanine Green/analogs & derivatives ; Intraoperative Care ; Male ; Neoplasms/diagnosis ; Neoplasms/pathology ; Reproducibility of Results ; Scorpion Venoms/administration & dosage
    Chemical Substances Contrast Media ; Fluorescent Dyes ; Scorpion Venoms ; tozuleristide (835UH424TU) ; Indocyanine Green (IX6J1063HV)
    Language English
    Publishing date 2014-08-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1432-1
    ISSN 1538-7445 ; 0008-5472
    ISSN (online) 1538-7445
    ISSN 0008-5472
    DOI 10.1158/0008-5472.CAN-15-0471
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: A highly conserved His-His motif present in alpha1-->3/4fucosyltransferases is required for optimal activity and functions in acceptor binding.

    Sherwood, Anne L / Upchurch, David A / Stroud, Mark R / Davis, William C / Holmes, Eric H

    Glycobiology

    2002  Volume 12, Issue 10, Page(s) 599–606

    Abstract: Alpha1-->3/4fucosyltransferases (FucTs) from several species contain a highly conserved His-His motif adjacent to an enzyme region correlating with the ability to catalyze fucose transfer to type 1 chain acceptors. Site-directed mutagenesis has been ... ...

    Abstract Alpha1-->3/4fucosyltransferases (FucTs) from several species contain a highly conserved His-His motif adjacent to an enzyme region correlating with the ability to catalyze fucose transfer to type 1 chain acceptors. Site-directed mutagenesis has been employed to analyze structure-function relationships of this His-His motif in human FucT-IV. The results indicate that most changes of His(113) and His(114) and nearby residues of FucT-IV reduced the specific activity of the enzymes. Analysis of acceptor properties demonstrated close similarity of most mutants with wild-type FucT-IV, whereas an apparent preference for the H-type II acceptor was observed for the His(114) mutants. Kinetic studies demonstrated that mutants of His(114) had a substantially increased K(m) for acceptor compared to other enzymes tested. The dramatic increase in acceptor K(m) for the His(114) mutants, particularly for the nonfucosylated acceptor, suggests that this His-His motif is involved in acceptor binding and perhaps interacts with GlcNAc residues of type 2 acceptors. The presence of fucose in acceptor substrates may promote more efficient substrate binding and presumably partially overcomes the weaker interaction with GlcNAc caused by the mutation.
    MeSH term(s) Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Base Sequence ; COS Cells ; DNA Primers ; Fucosyltransferases/chemistry ; Fucosyltransferases/genetics ; Fucosyltransferases/metabolism ; Histidine/metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Sequence Homology, Amino Acid ; Substrate Specificity
    Chemical Substances DNA Primers ; Histidine (4QD397987E) ; Fucosyltransferases (EC 2.4.1.-) ; 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase (EC 2.4.1.65)
    Language English
    Publishing date 2002-10
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwf075
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3150: Show issues Location:
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  5. Article: Universal red blood cells--enzymatic conversion of blood group A and B antigens.

    Olsson, Martin L / Hill, Cheryl A / de la Vega, Humberto / Liu, Qiyong P / Stroud, Mark R / Valdinocci, Jean / Moon, Steven / Clausen, Henrik / Kruskall, Margot S

    Transfusion clinique et biologique : journal de la Societe francaise de transfusion sanguine

    2004  Volume 11, Issue 1, Page(s) 33–39

    Abstract: Accidental transfusion of ABO-incompatible red blood cells (RBCs) is a leading cause of fatal transfusion reactions. To prevent this and to create a universal blood supply, the idea of converting blood group A and B antigens to H using specific exo- ... ...

    Abstract Accidental transfusion of ABO-incompatible red blood cells (RBCs) is a leading cause of fatal transfusion reactions. To prevent this and to create a universal blood supply, the idea of converting blood group A and B antigens to H using specific exo-glycosidases capable of removing the immunodominant sugar residues was pioneered by Goldstein and colleagues at the New York Blood Center in the early 1980s. Conversion of group B RBCs to O was initially carried out with alpha-galactosidase extracted from coffee beans. These enzyme-converted O (ECO) RBCs appeared to survive normally in all recipients independent of blood group. The clinical trials moved from small infusions to single RBC units and finally multiple and repeated transfusions. A successful phase II trial utilizing recombinant enzyme was reported by Kruskall and colleagues in 2000. Enzymatic conversion of group A RBCs has lagged behind due to lack of appropriate glycosidases and the more complex nature of A antigens. Identification of novel bacterial glycosidases with improved kinetic properties and specificities for the A and B antigens has greatly advanced the field. Conversion of group A RBCs can be achieved with improved glycosidases and the conversion conditions for both A and B antigens optimized to use more cost-efficient quantities of enzymes and gentler conditions including neutral pH and short incubation times at room temperature. Of the different strategies envisioned to create a universal blood supply, the ECO concept is the only one, for which human clinical trials have been performed. This paper discusses some biochemical and clinical aspects of this developing technology.
    MeSH term(s) Bacterial Proteins/pharmacology ; Blood Group Incompatibility/prevention & control ; Blood Grouping and Crossmatching ; Clinical Trials as Topic ; Erythrocyte Membrane/drug effects ; Erythrocyte Membrane/immunology ; Forecasting ; Fungal Proteins/pharmacology ; Glycoside Hydrolases/pharmacology ; Humans ; Isoantigens/drug effects ; Isoantigens/metabolism ; Oligosaccharides/metabolism ; Substrate Specificity ; Transfusion Reaction ; Trisaccharides/metabolism
    Chemical Substances Bacterial Proteins ; Fungal Proteins ; Isoantigens ; Oligosaccharides ; Trisaccharides ; blood group A trisaccharide ; blood group B trisaccharide (2P888H42QS) ; Glycoside Hydrolases (EC 3.2.1.-)
    Language English
    Publishing date 2004-02-09
    Publishing country France
    Document type Journal Article ; Review
    ZDB-ID 1204698-x
    ISSN 1953-8022 ; 1246-7820
    ISSN (online) 1953-8022
    ISSN 1246-7820
    DOI 10.1016/j.tracli.2003.12.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4097: Show issues Location:
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    Zs.MO 308: Show issues

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  6. Article: Tumor paint: a chlorotoxin:Cy5.5 bioconjugate for intraoperative visualization of cancer foci.

    Veiseh, Mandana / Gabikian, Patrik / Bahrami, S-Bahram / Veiseh, Omid / Zhang, Miqin / Hackman, Robert C / Ravanpay, Ali C / Stroud, Mark R / Kusuma, Yumiko / Hansen, Stacey J / Kwok, Deborah / Munoz, Nina M / Sze, Raymond W / Grady, William M / Greenberg, Norman M / Ellenbogen, Richard G / Olson, James M

    Cancer research

    2007  Volume 67, Issue 14, Page(s) 6882–6888

    Abstract: Toward the goal of developing an optical imaging contrast agent that will enable surgeons to intraoperatively distinguish cancer foci from adjacent normal tissue, we developed a chlorotoxin:Cy5.5 (CTX:Cy5.5) bioconjugate that emits near-IR fluorescent ... ...

    Abstract Toward the goal of developing an optical imaging contrast agent that will enable surgeons to intraoperatively distinguish cancer foci from adjacent normal tissue, we developed a chlorotoxin:Cy5.5 (CTX:Cy5.5) bioconjugate that emits near-IR fluorescent signal. The probe delineates malignant glioma, medulloblastoma, prostate cancer, intestinal cancer, and sarcoma from adjacent non-neoplastic tissue in mouse models. Metastatic cancer foci as small as a few hundred cells were detected in lymph channels. Specific binding to cancer cells is facilitated by matrix metalloproteinase-2 (MMP-2) as evidenced by reduction of CTX:Cy5.5 binding in vitro and in vivo by a pharmacologic blocker of MMP-2 and induction of CTX:Cy5.5 binding in MCF-7 cells following transfection with a plasmid encoding MMP-2. Mouse studies revealed that CTX:Cy5.5 has favorable biodistribution and toxicity profiles. These studies show that CTX:Cy5.5 has the potential to fundamentally improve intraoperative detection and resection of malignancies.
    MeSH term(s) Animals ; Brain Neoplasms/metabolism ; Carbocyanines/chemistry ; Fluorescent Dyes/chemistry ; Glioma/metabolism ; Humans ; Matrix Metalloproteinase 2/metabolism ; Mice ; Microscopy, Fluorescence/methods ; Neoplasms/metabolism ; Neovascularization, Pathologic ; Photons ; Rats ; Scorpion Venoms/chemistry
    Chemical Substances CY5.5 cyanine dye ; Carbocyanines ; Fluorescent Dyes ; Scorpion Venoms ; Chlorotoxin (06UV5RFW57) ; Matrix Metalloproteinase 2 (EC 3.4.24.24)
    Language English
    Publishing date 2007-07-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1432-1
    ISSN 1538-7445 ; 0008-5472
    ISSN (online) 1538-7445
    ISSN 0008-5472
    DOI 10.1158/0008-5472.CAN-06-3948
    Database MEDical Literature Analysis and Retrieval System OnLINE

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