Shenshen Dou

Eli Lilly (United States)

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Helen Donis-Keller

Franklin W. Olin College of Engineering

Terry C. Lairmore

Louisiana State University Health Sciences Center Shreveport

James R. Howe

University of Iowa

Kent L. Buchanan

Tulane University

David Chi

Washington University Medical Center

Carol F. Webb

University of Oklahoma Health Sciences Center

T. Steinbrueck

Washington University in St. Louis

Rosalie Veile

Sabin Vaccine Institute

Glennda Smithson

Takeda (United States)

Samuel A. Wells

King's College London

Cooperative Institutions

Washington University in St. Louis

Eli Lilly (United States)

Oklahoma Medical Research Foundation

Howard Hughes Medical Institute

Indiana University – Purdue University Indianapolis

University of Oklahoma Health Sciences Center

Indiana University School of Medicine

Indianapolis Zoo

University of Massachusetts Chan Medical School

University of Chicago

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Tumor pretargeting in mice using MORF conjugated CC49 antibody and radiolabeled complimentary cMORF effector.

PubMed (2010)

Guo Liu Shenshen Dou P. Hendrik Pretorius Xueliang Liu Ling Chen

Using the antiCEA antibody MN14, a LS174T mouse tumor model has been successfully targeted with (⁹⁹m)Tc for imaging and ¹⁸⁸Re for radiotherapy by phosphorodiamidate morpholino oligomers (MORF)/complementary MORF (cMORF) pretargeting strategy. This investigation evaluated the antiTAG-72 antibody CC49 as an alternative to MN14 for this application.Both CC49 and MN14 were labeled with ¹¹¹In via SCN-benzyl-DTPA and their biodistributions were compared to that of MN14 labeled via DTPA anhydride. Since the accessibility of the antibody to the effector is required for optimization of pretargeting, the internalization of both MORF-CC49 and MORF-MN14 antibodies in LS174T cells were evaluated in culture. In addition, the accessible concentration of MORF-CC49 antibody in tumor was determined in a series of pretargeting studies with escalating dosages of the [(⁹⁹m)Tc]cMORF effector. Finally, using these results and our semi-empirical model, an imaging study was performed under optimal pretargeting conditions.The biodistribution of ¹¹¹In to trace the MN14 antibody depended significantly on the labeling method. Furthermore, both MORF-CC49 and MORF-MN14 antibodies showed rapid internalization in culture. Fortunately, the accessibility in tumor was found to be less seriously reduced in vivo. In a pretargeting study under optimal conditions, both by imaging and by necropsy, the [(⁹⁹m)Tc]cMORF effector accumulated predominantly in the tumor of pretargeted mice. Normal tissue accumulations were minimal except in kidneys, liver, and a segment of intestines.MORF pretargeting with CC49 was equally successful in the LS174T tumor model to the MORF pretargeting with MN14. The MORF-CC49 antibody may therefore be considered for future investigations toward early clinical trials.

Pretargeting

Biodistribution

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Citations (19)

MicroWorld Butterflies

The Permanente Journal (2018)

Shenshen Dou

10.7812/tpp/18.999

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A new RFLP locus D4S185 maps to human chromosome 4q

Nucleic Acids Research (1991)

Terry C. Lairmore A.Vocero Villeta Shenshen Dou T. Steinbrueck Helen Donis-Keller

Journal Article A new RFLP locus D4S185 maps to human chromosome 4q Get access T.C. Lairmore, T.C. Lairmore 1Departments of Surgery, Washington University Medical SchoolBox 8232, 660 S. Euclid, St Louis, MO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar A.Vocero Villeta, A.Vocero Villeta 2Departments of Genetics, Washington University Medical SchoolBox 8232, 660 S. Euclid, St Louis, MO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar S. Dou, S. Dou 2Departments of Genetics, Washington University Medical SchoolBox 8232, 660 S. Euclid, St Louis, MO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar T. Steinbrueck, T. Steinbrueck 2Departments of Genetics, Washington University Medical SchoolBox 8232, 660 S. Euclid, St Louis, MO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar H. Donis-Keller H. Donis-Keller 2Departments of Genetics, Washington University Medical SchoolBox 8232, 660 S. Euclid, St Louis, MO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar Nucleic Acids Research, Volume 19, Issue 9, 11 May 1991, Page 2518, https://doi.org/10.1093/nar/19.9.2518 Published: 11 May 1991

10.1093/nar/19.9.2518

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Regulation and Expression of Immunoglobulin Heavy Chains

CRC Press eBooks (2000)

Carol F. Webb Kent L. Buchanan Shenshen Dou Elizabeth F. Smith Yoshio Yamashita

Immunoglobulin expression and B lymphocyte differentiation are intimately linked. Immunoglobulin heavy chains are encoded by four groups of gene segments called the DH (diversity), JH (joining), CH (constant), and VH (variable) region segments that undergo rearrangement to allow transcription through one VDJ segment resulting in expression of a full length protein (reviewed in Papavasiliou et al., 1997). Rearrangement occurs in an ordered fashion during differentiation so that D segments first become juxtaposed with J segments (the pro-B cell stage), and then V segments rearrange with the DJ segments to form one contiguous exon (the pre-B cell stage). Rearrangement and expression of the light chain genes defines the next stage in B cell differentiation (the immature B cell stage). Mice that do not produce the proteins required for rearrangement are unable to express immunoglobulin heavy chains or to produce B lymphocytes representative of stages beyond early pro-B cells (Shinkai et al., 1992; Schatz et al., 1989). Later pro-B and pre-B stages in B cell differentiation are at least partially defined on the basis of the rearrangement status of the heavy chain genes. Differentiation beyond the pre-B cell stage also requires rearrangement, but of a light chain locus. Thus, expression of rearranged heavy chains in recombinase deficient mice results in blocks in differentiation at the pre-B cell stage (Young et al., 1994). Signaling through surface receptors containing the heavy chain in conjunction with pseudo-light chains in the pre-B cell, or with light chains in the mature B cell, is critical for progression through B cell differentiation (Burrows and Cooper, 1997; Tarlinton et al., 1997). Therefore, appropriate expression of immunoglobulin heavy chains is also important for late stages in B cell differentiation leading up to the production and secretion of antibody. Although many of the details of the rearrangement process are now understood, this chapter will focus on additional events important for transcription of the heavy chain locus.

Immunoglobulin heavy chain

Heavy chain

Expression (computer science)

10.1201/9781482283693-8

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Mutations in the RET proto-oncogene are associated with MEN 2A and FMTC

Human Molecular Genetics (1993)

Helen Donis-Keller Shenshen Dou David Chi Katrin M. Carlson Koji Toshima

Multiple endocrine neoplasia type 2A (MEN 2A) and familial medullary thyroid carcinoma (FMTC) are dominantly inherited conditions which predispose to the development of endocrine neoplasia. Evidence is presented that sequence changes within the coding region of the RET proto-oncogene, a putative transmembrane tyrosine kinase, may be responsible for the development of neoplasia in these inherited disorders. Single strand conformational variants (SSCVs) in exons 7 and 8 of the RET proto-oncogene were identified in eight MEN 2A and four FMTC families. The variants were observed only in the DNA of individuals who were either affected or who had inherited the MEN2A or FMTC allele as determined by haplotyping experiments. The seven variants identified were sequenced directly. All involved point mutations within codons specifying cysteine residues, resulting in nonconservative amino acid changes. Six of the seven mutations are located in exon 7. A single mutation was found in exon 8. Variants were not detected in four MEN 2B families studied for all exon assays available, nor were they detectable in 16 cases of well documented sporadic medullary thyroid carcinoma or pheochromocytoma that were tested for exon 7 variants. Coinheritance of the mutations with disease and the physical and genetic proximity of the RET proto-oncogene provide evidence that RET is responsible for at least two of the three inherited forms of MEN 2. Neither the normal function, nor the ligand of RET are yet known. However, its apparent involvement in the development of these inherited forms of neoplasia as well as in papillary thyroid carcinoma suggest an important developmental or cell regulatory role for the protein.

RET proto-oncogene

Proto-Oncogene Proteins c-ret

10.1093/hmg/2.7.851

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Citations (1,284)

Family-specific differences in transcription efficiency of Ig heavy chain promoters.

The Journal of Immunology (1997)

Kent L. Buchanan Elizabeth A. Smith Shenshen Dou Lynn M. Corcoran Carol F. Webb

Abstract Murine Ig variable region heavy chain genes (V(H)) are grouped into families based on coding sequence homology. We observed that the accompanying promoter sequences were also conserved in a family-specific manner. Remarkably, no one has directly compared the transcription efficiencies of V(H) genes from different families. Using an in vitro transcription system, we found that transcription efficiencies of different V(H) promoters differed by as much as 70-fold. These differences could be attributed to variation in the octamer-heptamer and TATA sequences, as well as to the presence or absence of initiator elements. The J558 family promoter exhibited the highest level of transcription and specifically interacted with an Oct-1 dimer not bound by other V(H) promoters. These data suggest that differential transcription and regulation of V(H) promoters could occur in vivo. The increased transcription efficiency of the J558 promoter relative to other V(H) promoters also presents a possible explanation for the abundance of J558 sterile transcripts observed before V(H)DJ(H) rearrangement.

Transcription

10.4049/jimmunol.159.3.1247

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Citations (23)

Development of a sequence-tagged site for the centromere of chromosome 10: its use in cytogenetic and physical mapping

Human Genetics (1993)

James R. Howe Terry C. Lairmore Rosalie Veile Shenshen Dou Samuel A. Wells

Yeast artificial chromosome

Bacterial artificial chromosome

Sequence-tagged site

10.1007/bf00218256

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Citations (2)

Strategie für das genetische Screening bei Familien mit MEN 2A und familiärem C-Zell-Karzinom Strategie for genetic screening in MEN 2A and FMTC families

C. Franzi David Chi Shenshen Dou Helen Donis-Keller I Abteilung

Fur die Entstehung der multiplen endokrinen Neoplasie Typ 2A (MEN 2A) und der familiaren Form des C-Zell-Carcinoms sind Mutationen im erst kurzlich identifizierten RET-Protoonkogen (RET) verantwortlich [1, 2]. In den bisher beschriebenen Mutationen wird die Aminosaure Cystein in verschiedenen Codons von Exon 10 und 11 von RET durch unterschiedliche Aminosauren ausgetauscht. Das klassische Screening bei Risikotragem in Familien mit MEN 2A und familiarem C-ZellKarzinom basierte bisher auf der Bestimmung des basalen und stimuliertem Calcitonin im Serum, das als ein hochsensitiver Tumormarker fur das C-ZellKarzinom gilt. Die Identifizierung des verantwortlichen Gens ermoglicht jetzt ein Screening durch die sehr verlasliche direkte DNA-Analyse.

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A new RFLP marker D5S348 maps to 5p14.3-15.2, between D5S60 (CRrR535) and HPRTP2

Nucleic Acids Research (1992)

James R. Howe Terry C. Lairmore Shenshen Dou Rosalie Veile T. Steinbrueck

Journal Article A new RFLP marker D5S348 maps to 5p14.3-15.2, between D5S60 (CRrR535) and HPRTP2 Get access J.R. Howe, J.R. Howe Search for other works by this author on: Oxford Academic PubMed Google Scholar T.C. Lairmore, T.C. Lairmore Search for other works by this author on: Oxford Academic PubMed Google Scholar S. Dou, S. Dou 1Genetics, St. LouisMO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar R. Veile, R. Veile 1Genetics, St. LouisMO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar T. Steinbrueck, T. Steinbrueck 1Genetics, St. LouisMO 63110, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar S.A. Wells, Jr, S.A. Wells, Jr Search for other works by this author on: Oxford Academic PubMed Google Scholar H. Donis-Keller H. Donis-Keller * 1Genetics, St. LouisMO 63110, USA * To whom correspondence should be addressed Search for other works by this author on: Oxford Academic PubMed Google Scholar Nucleic Acids Research, Volume 20, Issue 5, 11 March 1992, Page 1168, https://doi.org/10.1093/nar/20.5.1168 Published: 11 March 1992

10.1093/nar/20.5.1168

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Citations (1)

Decoy receptor 3 (DcR3) is proteolytically processed to a metabolic fragment having differential activities against Fas ligand and LIGHT

Biochemical Pharmacology (2003)

Victor J. Wroblewski Derrick R. Witcher Gerald W. Becker Kelly A Davis Shenshen Dou

Fas ligand

10.1016/s0006-2952(02)01612-x

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Citations (28)