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398 results on '"Flickinger, Charles J."'

55. Genomic Organization, Incidence, and Localization of the SPAN-X Family of Cancer-Testis Antigens in Melanoma Tumors and Cell Lines

Author

Westbrook, V. Anne, primary, Schoppee, Pamela D., additional, Diekman, Alan B., additional, Klotz, Kenneth L., additional, Allietta, Margaretta, additional, Hogan, Kevin T., additional, Slingluff, Craig L., additional, Patterson, James W., additional, Frierson, Henry F., additional, Irvin, William P., additional, Flickinger, Charles J., additional, Coppola, Michael A., additional, and Herr, John C., additional

Published
2004
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57. Splicing in murine CABYR and its genomic structure

Author

Sen, Buer, primary, Mandal, Arabinda, additional, Wolkowicz, Michael J., additional, Kim, Young-Hwan, additional, Reddi, P.Prabhakara, additional, Shetty, Jagathpala, additional, Bush, Leigh Ann, additional, Flickinger, Charles J., additional, and Herr, John C., additional

Published
2003
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58. SLLP1, A Unique, Intra-acrosomal, Non-bacteriolytic, c Lysozyme-Like Protein of Human Spermatozoa1

Author

Mandal, Arabinda, primary, Klotz, Kenneth L., additional, Shetty, Jagathpala, additional, Jayes, Friederike L., additional, Wolkowicz, Michael J., additional, Bolling, Laura C., additional, Coonrod, Scott A., additional, Black, Michael B., additional, Diekman, Alan B., additional, Haystead, Timothy A.J., additional, Flickinger, Charles J., additional, and Herr, John C., additional

Published
2003
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67. Spermatid-Specific Expression of the Novel X-Linked Gene Product SPAN-X Localized to the Nucleus of Human Spermatozoa1

Author

Westbrook, V. Anne, primary, Diekman, Alan B., additional, Klotz, Ken L., additional, Khole, Vrinda V., additional, von Kap-Herr, Chris, additional, Golden, Wendy L., additional, Eddy, Roger L., additional, Shows, Thomas B., additional, Stoler, Mark H., additional, Lee, Chi-Yu G., additional, Flickinger, Charles J., additional, and Herr, John C., additional

Published
2000
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68. FSP95, A Testis-Specific 95-Kilodalton Fibrous Sheath Antigen That Undergoes Tyrosine Phosphorylation in Capacitated Human Spermatozoa1

Author

Mandal, Arabinda, primary, Naaby-Hansen, Søren, additional, Wolkowicz, Michael J., additional, Klotz, Ken, additional, Shetty, Jagathpala, additional, Retief, Jacques D., additional, Coonrod, Scott A., additional, Kinter, Michael, additional, Sherman, Nicholas, additional, Cesar, Fred, additional, Flickinger, Charles J., additional, and Herr, John C., additional

Published
1999
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97. CABYR isoforms expressed in late steps ofspermiogenesis bind with AKAPs and ropporin inmouse sperm fibrous sheath.

Author

Yan-Feng Li, Wei He, Young-Hwan Kim, Mandal, Arabinda, Digilio, Laura, Klotz, Ken, Flickinger, Charles J., and Herr, John C.

Subjects
SPERMIOGENESIS in animals, PROTEIN-tyrosine kinases, AMINO acids, DIMERS, IMMUNOFLUORESCENCE
Abstract

Background: CABYR is a polymorphic calcium-binding protein of the sperm fibrous sheath (FS) which gene contains two coding regions (CR-A and CR-B) and is tyrosine as well as serine/threonine phosphorylated during in vitro sperm capacitation. Thus far, the detailed information on CABYR protein expression in mouse spermatogenesis is lacking. Moreover, because of the complexity of this polymorphic protein, there are no data on how CABYR isoforms associate and assemble into the FS. Methods: The capacity of mouse CABYR isoforms to associate into dimers and oligomers, and the relationships between CABYR and other FS proteins were studied by gel electrophoresis, Western blotting, immunofluorescence, immunoprecipitation and yeast two-hybrid analyses. Results: The predominant form of mouse CABYR in the FS is an 80 kDa variant that contains only CABYR-A encoded by coding region A. CABYR isoforms form dimers by combining the 80 kDa CABYR-A-only variant with the 50 kDa variant that contains both CABYR-A and CABYR-B encoded by full length or truncated coding region A and B. It is proposed that this step is followed by the formation of larger oligomers, which then participate in the formation of the supramolecular structure of the FS in mouse sperm. The initial expression of CABYR occurs in the cytoplasm of spermatids at step 11 of spermiogenesis and increases progressively during steps 12-15. CABYR protein gradually migrates into the sperm flagellum and localizes to the FS of the principal piece during steps 15- 16. Deletion of the CABYR RII domain abolished the interaction between CABYR and AKAP3/AKAP4 but did not abolish the interaction between CABYR and ropporin suggesting that CABYR binds to AKAP3/AKAP4 by its RII domain but binds to ropporin through another as yet undefined region. Conclusions: CABYR expresses at the late stage of spermiogenesis and its isoforms oligomerize and bind with AKAPs and ropporin. These interactions strongly suggest that CABYR participates in the assembly of complexes in the FS, which may be related to calcium signaling. [ABSTRACT FROM AUTHOR]

Published
2010
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100. MEIG1 is essential for spermiogenesis in mice.

Author

Zhanga, Zhibing, Shen, Xuening, Gude, David R., Wilkinson, Bonney M., Justice, Monica J., Flickinger, Charles J., Herr, John C., Eddy, Edward M., and Strauss III, Jerome F.

Subjects
SPERMIOGENESIS in animals, SPERMATOZOA, MEIOSIS, TRANSMISSION electron microscopy, ORGANELLES, LABORATORY mice
Abstract

Spermatogenesis can be divided into three stages: spermatogonial mitosis, meiosis of spermatocytes, and spermiogenesis. During spermiogenesis, spermatids undergo dramatic morphological changes including formation of a flagellum and chromosomal packaging and condensation of the nucleus into the sperm head. The genes regulating the latter processes are largely unknown. We previously discovered that a bi-functional gene, Spagl6, is essential for spermatogenesis. SPAG16S, the 35 kDa, testis-specific isoform derived from the Spa g16 gene, was found to bind to meiosis expressed gene 1 product (MEIG1), a protein originally thought to play a role in meiosis. We inactivated the Meig1 gene and, unexpectedly, found that Meig1 mutant male mice had no obvious defect in meiosis, but were sterile as a result of impaired spermatogenesis at the stage of elongation and condensation. Transmission electron microscopy revealed that the manchette, a microtubular organelle essential for sperm head and flagellar formation was disrupted in spermatids of MEIG1-deficient mice. We also found that MEIG1 associates with the Parkin co-regulated gene (PACRG) protein, and that testicular PACRG protein is reduced in MEIG1-deficient mice. PACRG is thought to play a key role in assembly of the axonemes/flagella and the reproductive phenotype of Pacrg-deficient mice mirrors that of the Meigi mutant mice. Our findings reveal a critical role for the MEIG1/PARCG partnership in manchette structure and function and the control of spermiogenesis. [ABSTRACT FROM AUTHOR]

Published
2009

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