Search PubMed⌕ Search

Biomedical subjects

U Schubert

Publications and source records attributed to U Schubert.

58 records · Page 4Linked to original sources
PubMedDate not supplied

CrossLaps and beta-glucuronidase in peri-implant and gingival crevicular fluid.

Collagen degradation products of the carboxyterminal region possibly reflect bone and attachment loss. In the present study, the Serum CrossLaps One-Step enzyme-linked immunosorbent assay was used to determine a specific part of the carboxyterminal region of type I collagen, the CrossLaps. Samples of peri-implant and gingival crevicular fluid of 111 implants and 53 teeth from 47 partially or completely edentulous patients were examined in reference to levels of CrossLaps and beta-glucuronidase (beta G), an established marker of periodontal disease. Clinical probing pocket depth (PPD), bleeding on probing (BOP), plaque accumulation, mobility, radiographic bone loss, and the occurrence of Actinobacillus actinomycetemcomitans, Porphyromonas gingivalis, and Prevotella intermedia were assessed. The mean values were: for PPD at implants 3.76 +/- 1.41 mm, at teeth 3.44 +/- 0.88 mm; for beta G at implants 0.364 +/- 0.392 pU/min, at teeth 0.314 +/- 0.209 pU/min; for CrossLaps at implants 0.069 +/- 0.059 pmol/min, at teeth 0.082 +/- 0.053 pmol/min. Bleeding on probing was significantly higher on implants than on teeth (McNemar test, P = .004). No significant difference of beta G levels was found between teeth and implants (Wilcoxon test). A negative correlation was found between beta G levels and CrossLaps levels at teeth (Pearson-rank correlation, P = .002). On implants, no significant correlation of these 2 parameters was seen, but significant correlations were found between sulcus fluid flow rate and PPD (P = .012), beta G levels and bone loss (P < 0.0005), and CrossLaps levels and PPD (P = .011). CrossLaps can be detected in both gingival and peri-implant crevicular fluid. While rising levels of beta G may indicate acute peri-implantitis, CrossLaps may not, but could play a role as a marker of ongoing attachment loss.

Adult↗
PubMedDate not supplied

Synthesis and characterization of the hydrophilic C-terminal domain of the human immunodeficiency virus type 1-encoded virus protein U (Vpu).

The HIV-1-specific virus protein U (Vpu) is an amphipathic membrane-associated phosphoprotein that probably possesses an N-terminal hydrophobic membrane anchor and a hydrophilic moiety. Because of an as yet undefined cytotoxic effect and the low concentration of Vpu in host cells, it has not been possible to obtain sufficient quantities of this protein for biochemical and structural investigations. We describe the synthesis, in two forms, of 50-residue peptides representing the polar cytoplasmic domain of Vpu: pVpu, comprising the wild-type Vpu sequence of HIV-1, strain HTLVIIIB, from position Ile32 to Leu81, and a mutant, pVpum2/6, with replacement of Ser52-56 with Asn. This mutation affects the two phosphorylation sites of Vpu for casein kinase-2 (CK-2), the enzyme that phosphorylates Vpu in HIV-1-infected cells. The peptides were purified to homogeneity and characterized by N-terminal sequencing, mass spectrometry and SDS-PAGE. Furthermore, both peptides were immunologically characterized by Western blot and ELISA using Vpu-specific monoclonal and polyclonal antibodies. Recombinant human CK-2 caused in vitro phosphorylation of pVpu, but had no effect on the mutant pVpum2/6. Investigation of the peptides by circular dichroism showed that addition of trifluoroethanol stabilized the alpha-helical secondary structure. Preliminary 1H NMR spectroscopic data indicated that, in the presence of trifluoroethanol, both peptides in solution have stable secondary structures with considerable alpha-helical content.

Acquired Immunodeficiency Syndrome↗