Continuing professional development. Setting objectives for the organisation.
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Education, Dental, Continuing↗
Biomedical subjects
M Grace
Publications and source records attributed to M Grace.
Training needs analysis.
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Education, Dental, Continuing↗
A culture for learning.
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Education, Dental, Continuing↗
Macrophage-derived chemokine gene expression in human and macaque cells: mRNA quantification using NASBA technology.
Macrophage-derived chemokine (MDC) is a CC-chemokine that inhibits infection by both macrophage- and T cell-tropic strains of HIV-1. This suppressor activity has led to great interest in fully characterizing the role of MDC in the pathogenesis of HIV-1 infection. Methods for the quantitation of constitutive levels of MDC protein in vivo are lacking. In this report, we describe the development and performance of a NASBA-based assay for the quantification of MDC mRNA expression in human and macaque cells. Although the constitutive in vivo levels of MDC mRNA in macaque and human T lymphocytes were low, in vitro activation of these cells greatly increased MDC transcription. Levels in the human and macaque cells were comparable under all conditions tested. Positive correlations between MDC transcription and protein expression were observed. The results indicate that this assay is extremely sensitive and reproducible over a five log dynamic range, and effectively quantifies MDC mRNA in resting and activated T cells. This assay may therefore permit characterization of the role of MDC in HIV-1/SIV pathogenesis, and in vaccine-induced immune responses.
Animals↗
All change at the GDC?
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General Practice, Dental↗
Biological thermal detection in infrared imaging snakes. 1. Ultramicrostructure of pit receptor organs.
The receptor organs of snakes with "thermal vision" were studied with ultra-high-resolution scanning probe microscopy (SPM) at close to in vivo conditions to elucidate their surface morphology and materials properties critical for prospective biomimetic design of "soft matter"-based infrared (IR) sensors. The surfaces of living tissues were scanned under wet ambient conditions in physiological solution, and the resulting parameters were compared with SPM data obtained for chemically treated (formaldehyde-fixed) tissue in ambient air and TEM studies in high vacuum. We found that the microstructural parameters for the living tissue are similar to ones observed for the formaldehyde-fixed snake tissues. However, previous data obtained from TEM analysis in high vacuum underestimated actual dimensions of surface microstructures. The average spacing of the nanopit array observed within receptor surface areas, which was suggested to play a critical role in selective IR adsorption, was determined to be 520 nm. This value is close to the grating spacing required for efficient reflection of electromagnetic radiation characteristic for sunlight without affecting IR adsorbance.
Animals↗
Structural and biologic characterization of pegylated recombinant IFN-alpha2b.
The type I interferon-alpha (IFN-alpha) family is a family of natural small proteins that have clinically important anti-infective and antitumor activity. We have developed a semisynthetic protein-polymer conjugate of IFN-alpha2b (Intron A) by attaching a 12,000-Da monomethoxypolyethylene glycol (PEG-12000) polymer to the protein. PEG conjugation is thought to increase the serum half-life and thereby prolong patient exposure to IFN-alpha2b without altering the biologic potency to the protein. Matrix-assisted laser desorption ionization/mass spectrometry (MALDI-MS), high-performance size exclusion chromatography (HPSEC), circular dichroism (CD) analysis and tryptic digestion peptide analysis of PEG Intron demonstrated that the IFN-alpha2b protein was approximately 95% monopegylated and that the primary, the secondary, and the tertiary structures were unaltered. Pegylation did not affect the epitope recognition of antibodies used for Intron A quantitation. An extensive analysis of the pegylated positional isomers revealed that approximately 50% of PEG Intron was monopegylated on the His(34) residue of the IFN-alpha2b protein. The highest antiviral activity of the pegylated positional isomers for PEG Intron was associated with the His(34) pegylated isomer. The specific activity for PEG Intron in an antiviral cytopathic protection assay was 28%, relative to Intron A. However, the potency of PEG Intron, defined as bioactivity independent of protein concentration, was comparable to Intron A at both the molecular and cellular levels in a battery of in vitro assays. Equivalent units of PEG Intron and Intron A were indistinguishable for the induction of several key IFN-induced genes, including 2',5'-oligoadenylate synthetase (2',5'-OAS) and protein kinase R (PKR), in Molt 4 cells. The antiviral dose-response curves revealed that there were no significant differences between PEG Intron and Intron A. This demonstrated that the introduction of more IFN-alpha2b protein associated with equivalent unit dosing of PEG Intron did not create any antagonism or agonism in the antiviral assay. In assays for the immune response, PEG Intron and Intron A displayed comparable potency for both natural-killer (NK) and lymphokine-activated killer (LAK) cell cytolytic activity and for the induction of class I major histocompatibility protein. These results demonstrate that PEG Intron maintains an in vitro biologic potency profile for both antiviral and immunotherapeutic activity that is highly comparable to that of Intron A.
Antineoplastic Agents↗
The dental strategy.
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Health Plan Implementation↗
Restrictions on therapists.
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Community Dentistry↗