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S Bottega

Publications and source records attributed to S Bottega.

4 recordsLinked to original sources
PubMed2003

Response to a plaque control regimen on different levels of gingival inflammation.

BACKGROUND: The purpose of the present study was to evaluate the effectiveness of an oral hygiene regimen in subjects presenting with substantially different severity of plaque-associated gingivitis. METHODS: The study population was selected from among a large pool of subjects undergoing an experimental gingivitis trial. At completion of the 21-day plaque accumulation period, 2 sub-groups of subjects were identified on the basis of uppermost and lowest quartile for Gingival Index (GI), respectively classified as highly-inflamed (Hinf; n=17; GI: 1.07+/-0.10) and slightly-inflamed (Sinf; n=22; GI: 0.28+/-0.09) groups. An oral hygiene regimen, based on use of amine fluoride/stannous fluoride-containing toothpaste and mouthrinse, was then prescribed for 21 days. RESULTS: Plaque Index (PI), GI, gingival crevicular fluid (GCF) and Angulated Bleeding Index (AngBI) significantly decreased after treatment in both HInf and SInf groups (p<0.001). However, PI (0.77+/-0.41 vs 0.43+/-0.33, p<0.01), GI (0.23+/-0.30 vs 0.08+/-0.11, p<0.05), GCF (15.23 +/-7.11 vs 7.66+/-2.93, p<0.0000) remained significantly greater in the Hinf group compared to the Sinf group. CONCLUSIONS: These results suggest that 1) an oral hygiene regimen based on amine/stannous fluoride-containing toothpaste and mouthrinse is effective in reducing plaque-associated gingivitis, regardless of pre-existing severity of gingival inflammation; 2) the level of improvement in gingival status, however, is dependent on the pre-existing severity of the inflammatory condition.

Adult↗
PubMed1996

Formation of p27-CDK complexes during the human mitotic cell cycle.

In eukaryotic cells, the coordinated activation of different cyclin-dependent kinases regulates entry into S-phase. In vitro and in nonproliferating cells, p27 associates with and inhibits cyclin/cycin-dependent kinase (CDK) holoenzymes containing either CDK4, CDK6, or CDK2. Although many different types of proliferating cells contain p27 protein, neither the interactions of p27 with cyclin/CDK complexes nor the consequences of this interaction during the mitotic cycle have been fully explored. We report that, in MANCA cells, the amount of p27 is constant during the cell cycle. In addition, p27 associates with three different CDKs: CDK2, CDK4, and CDK6. Furthermore, the amount of p27 is significantly lower than the amount of cyclin D3 in these cells. The amount of CDK4 and CDK6 associated with p27 does not change in a cell cycle-dependent fashion; in contrast, the amount of CDK2 associated with p27 is lowest in early G1 cells and increases to a maximum in mid-G1 phase, reaching a steady-state level in late G1-phase cells. After mid-G1 phase, the amount of each p27/CDK complex remains constant through the remainder of the cell cycle. p27-immunoprecipitates contain an Rb-kinase activity. The substrate specificity, the expression pattern of this kinase, and the ability to deplete 50% of this kinase activity with a CDK6-specific antibody suggest that the CDK6 protein mediates, in part, the p27-associated Rb-kinase activity. In contrast, p27 complexes containing CDK2 are incapable of phosphorylating histone H1. These data are consistent with a model wherein cyclin D/CDK complexes sequester the CDK2-dependent kinase inhibitory activity of p27.

Animals↗
PubMed1992

Gas2, a growth arrest-specific protein, is a component of the microfilament network system.

In this report we analyze the protein product of a growth arrest-specific gene, gas2, by means of an affinity-purified antibody raised against the protein produced in bacteria. The regulation of Gas2 biosynthesis reflects the pattern of mRNA expression (Schneider, C., R. King, and L. Philipson. 1988. Cell. 54:787-793): its relative level is tightly associated with growth arrest. Gas2 seems to be regulated also at the posttranslational level via a phosphorylation mechanism. Gas2 is well conserved during the evolution with the same apparent molecular mass (36 kD) between mouse and human. We also demonstrate that Gas2 is a component of the microfilament system. It colocalizes with actin fiber, at the cell border and also along the stress fiber, in growth-arrested NIH 3T3 cells. The pattern of distribution, detected in arrested cells, can also be observed in growing cells when they are microinjected with the purified GST-Gas2 protein. In none of the analyzed oncogene-transformed NIH 3T3 cell lines was Gas2 expression induced under serum starvation.

3T3 Cells↗