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Biomedical subjects

J T Casey

Publications and source records attributed to J T Casey.

5 recordsLinked to original sources
PubMed1999

Physical and functional interactions between the herpes simplex virus UL15 and UL28 DNA cleavage and packaging proteins.

Herpes simplex virus (HSV) DNA is cleaved from concatemers and packaged into capsids in infected cell nuclei. This process requires seven viral proteins, including UL15 and UL28. UL15 expressed alone displays a nuclear localization, while UL28 remains cytoplasmic. Coexpression with UL15 enables UL28 to enter nuclei, suggesting an interaction between the two proteins. Additionally, UL28 copurified with UL15 from HSV-infected cells after ion-exchange and DNA affinity chromatography, and the complex sedimented as a 1:1 heterodimer upon sucrose gradient centrifugation. These findings are evidence of a physical interaction of UL15 and UL28 and a functional role for UL15 in directing UL28 to the nucleus.

Animals↗
PubMed1998

Prothrombin Greenville, Arg517-->Gln, identified in an individual heterozygous for dysprothrombinemia.

A 64-year-old white male was referred for evaluation of prolonged prothrombin time (PT) and activated partial thromboplastin time (aPTT) obtained before elective surgery with initial PT and PTT results of 14.9 and 38.4 seconds, respectively, which corrected to normal in 1:1 mixes with normal plasma. Functional prothrombin assay indicated a level of 51% with thromboplastin as an activator. The prothrombin antigen was 102%. This discordance in the functional and immunologic prothrombin levels was evidence for dysprothrombinemia. Western blotting showed that thrombin was formed at a normal rate in diluted plasma consistent with a mutation within the thrombin portion of prothrombin. DNA was isolated from leukocytes and the thrombin exons were amplified by polymerase chain reaction, cloned, and sequenced. For exon 13, eight clones were sequenced with four clones showing a point mutation in the codon for Arg517, which would result in substitution by Gln. Arg517 is part of the Arg-Gly-Asp(RGD) sequence in thrombin and contributes to an ion cluster with aspartic acid residues 552 and 554. Mutation at this residue most probably distorts the structure of the Na+ binding site in thrombin. This is the first report indicating the critical role of Arg517 in the normal physiological interaction of thrombin with fibrinogen. This dysprothrombin is designated Prothrombin Greenville.

Arginine↗
PubMed1991

1991 outlook: progress will require partnerships, improved productivity--roundtable discussion.

To address the myriad problems and challenges in the next year, the operative word will be partnership. That's according to members of Modern Healthcare's editorial advisory board in their discussion of the healthcare industry in 1991. The experts see the need for hospitals, physicians and the business community to team up to control costs, solve staffing woes and take initial steps toward healthcare reform.

Efficiency↗
PubMedDate not supplied

The UL6 locus of pseudorabies virus and its homology to oncogenic herpesviruses.

The UL6 locus of pseudorabies virus (PRV) was analyzed to reveal a gene cluster with homology to herpes simplex virus UL5, UL6, UL7 and UL8, Epstein-Barr virus BBRF1 and BBRF2, and Kaposi sarcoma-associated herpes virus ORF43 and ORF42. The noncoding region between PRV UL7 and UL8 contained 16 copies of a 14 bp T + C-rich repeat element. The mRNA start sites for UL6 and UL7 were mapped by primer extension and UL6 was expressed in vitro. The mobility of the in vitro-expressed UL6 protein correlated with the predicted mass of 66 kDa. The relationship and potential significance of the UL6 locus with the corresponding sequences in oncogenic herpesviruses is discussed.

Animals↗