Infrared properties of chemical-vapor deposition polycrystalline diamond windows.

Low-resolution transmittance and reflectance spectra of high-quality chemical-vapor deposition (CVD) diamond windows were measured in the infrared in the 2.5-500-mum wavelength range (20-4000 cm(-1)). High-resolution measurements on a window with nearly parallel surfaces show well defined interference fringes at low frequencies.

Heterogeneous expression of tumor-associated genes in disseminated breast cancer cells.

Background: Gene expression profiles were determined to demonstrate heterogeneity of viable disseminated tumor cells (DTC) in the blood of breast cancer patients.

Patients And Methods: All patients (n = 48) suffered from metastatic disease (M1) and were treated with chemotherapy and/or Herceptin, respectively. Blood samples were analyzed by a DTC detection assay consisting of immunomagnetic tumor cell selection combined with expression profiling of the tumor-associated transcripts GA733-2, MUC-1, HER-2 and Claudin-7.

[Randomized, double-blind crossover study of bioavailability of levothyroxine].

Objective: The synthetic thyroid hormone levothyroxine-sodium (LT4) is still the treatment of choice to replace thyroid hormone deficiency in hypothyroidism, and for adjuvant treatment of euthyroid goiter. A change of LT4 preparations during treatment may lead to major changes of thyroid hormone levels. In this study, we compared the bioavailability of two LT4 preparations, L-Thyroxin Henning 100 and Eferox 100.

Ets1 is a common element in directing transcription of the alpha and beta genes of human protein kinase CK2.

Protein kinase CK2 is a conserved and vital Ser/Thr phosphotransferase with various links to malignant diseases, occurring as a tetramer composed of two catalytically active (CK2alpha and/or CK2alpha') and two regulatory subunits (CK2beta). There is balanced availability of CK2alpha and CK2beta transcripts in proliferating and differentiating cultured cells. Examination of the human CK2beta gene for transcriptionally active regions by systematic deletions and reporter gene assays indicates strong promoter activity at positions -42 to 14 and 12 to 72 containing transcription start sites 1 and 2 of the gene (positions +1 and 33), respectively, an upstream and a downstream enhancer activity at positions -241 to -168 and 123 to 677, respectively, and silencer activity at positions -241 to -261.

Transcription factors ets1, NF-kappa B, and Sp1 are major determinants of the promoter activity of the human protein kinase CK2alpha gene.

CK2alpha is one of two isoforms of protein kinase CK2, a highly conserved, ubiquitous, and vital phosphotransferase whose expression is kept at constant cellular levels and whose dysregulated expression has been linked to malignant diseases. The upstream sequence of the gene coding for human CK2alpha (CSNK1A1, chromosomal location 20p13) has been examined for promoter location and transcription factor interactions using reporter gene assays (luciferase; HeLa cells), site-directed mutagenesis, electrophoretic mobility shift assays, super-shifts, UV cross-linking, Western blotting, and DNA affinity chromatography. Highest promoter activity has been found in a region comprising positions -9 to 46.

Casein kinase 2 binds and phosphorylates the nucleosome assembly protein-1 (NAP1) in Drosophila melanogaster.

The nucleosome assembly protein-1 (NAP1) was originally identified in HeLa cells as a factor facilitating the in vitro assembly of nucleosomes. However, in yeast cells NAP1 is required in the control of mitotic events induced by the Clb2/p34(CDC28). Here, we show that Drosophila NAP1 is a phosphoprotein that is associated with a kinase able to phosphorylate NAP1.

Heterogeneous nuclear ribonucleoprotein A2 interacts with protein kinase CK2.

The catalytic subunit of protein kinase CK2 (CK2alpha) was found associated with heterogeneous nuclear ribonucleoprotein particles (hnRNPs) that contain the core proteins A2 and C1-C2. High levels of CK2 activity were also detected in these complexes. Phosphopeptide patterns of hnRNP A2 phosphorylated in vivo and in vitro by protein kinase CK2 were similar, suggesting that this kinase can phosphorylate hnRNPA2 in vivo.

Multiple forms of protein kinase CK2 present in leukemic cells: in vitro study of its origin by proteolysis.

Human recombinant CK2 subunits were incubated for different times with the two main cytosolic proteases m-calpain and 20 S proteasome. Both, m-calpain in a calcium dependent manner and the 20 S proteasome, were able to degrade CK2 subunits in vitro. In both cases, CK2alpha' was more resistant to these proteases than CK2alpha.

Intermolecular contact sites in protein kinase CK2.

Chemical crosslinking and analysis of CNBr-digested fusion products by immunoblotting with sequence-specific antibodies identifies an interaction between positions 55-70 of subunit beta (beta55-70) and 65-80 of subunit alpha (alpha65-80). This has been supported by crosslinking of subunits with peptides alpha65-80 and beta55-70, by binding of subunits to immobilized peptides, and by the hindrance of coprecipitation with peptide-raised antibodies (anti-alpha65-80; anti-beta55-70). Functionally, beta55-70 is a negative regulatory region for the kinase activity of subunit alpha.

Identification of structural elements of subunit beta of human protein kinase CK2 participating in tight physical alpha-beta intersubunit contacts directly adjacent to a surface-oriented region.

Sites essential for tight physical intersubunit interaction in protein kinase CK2, a tetramer composed of two catalytic (alpha and/or alpha') and two regulatory subunits (beta), have been assigned to the C-terminal part of subunit beta. Mutational analysis suggests region 171-181 of beta to be one of these but this is not consistent with the observation of coprecipitation of catalytic subunits by antibodies directed specifically to this beta segment which indicates that this region is accessible to antibodies even if the beta subunit is associated with the alpha subunit. In an attempt to clarify the apparent contradiction, we have subdivided beta-(155-181)-peptide, which includes the fragment of beta and that both binds to catalytic subunits and stimulates kinase activity, into six more or less overlapping peptides with a length of 9-16 amino acid residues and performed peptide competition and a subunit binding assays.

Interaction sites between catalytic and regulatory subunits in human protein kinase CK2 holoenzymes as indicated by chemical cross-linking and immunological investigations.

Protein kinase CK2, a heterotetramer composed of two catalytic subunits (alpha and/or alpha') and two regulatory subunits (beta), has been examined for intermolecular contact sites by methods that allow investigation of the native, unaltered proteins. Antibodies were raised against a series of 11 subunit peptides, affinity purified, and ensured for site specific binding by peptide competition. Chemical cross-linking of CK2 subunits with a hydrophilic carbodiimide and analysis of fused subunits and of CNBr-digested fusion products by immunoblotting with the sequence specific antibodies identified a tight interaction between positions beta55-70 and alpha65-80 (alpha'66-81) of subunits beta and alpha (alpha'), respectively.

Recombinant human casein kinase II. A study with the complete set of subunits (alpha, alpha' and beta), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme.

Human casein kinase II (CKII) is a ubiquitous and multipotential Ser/Thr kinase involved in the regulation of cell growth and differentiation. Biochemically, two characteristics are particularly notable; first, the tetrameric composition of two catalytic subunits (alpha and/or alpha') and two regulatory subunits (beta); second, the autophosphorylation of the holoenzyme at the N-terminus of CKII beta, suspected to be involved in tuning of the kinase activity. Whether CKII alpha and CKII alpha' reconstitute comparably with CKII beta to form holoenzyme is unclear.