Search PubMed⌕ Search

Biomedical subjects

P Mahon

Publications and source records attributed to P Mahon.

8 recordsLinked to original sources
PubMed2026

Impact of precision oncology research in pediatric poor prognosis cancer: patient, parent and healthcare provider perspectives.

BACKGROUND: Comprehensive genomic analyses are increasingly accessible to children, adolescents and young adults (AYAs) with poor prognosis cancers. Challenges and successes of pediatric precision oncology studies from the perspectives of AYA patients, parents and healthcare providers (HCPs) are poorly described. METHODS: Between March 2021 and May 2023, we interviewed AYA patients (12-21 years), parents and HCPs who participated in pediatric precision oncology studies for poor prognosis cancers in British Columbia. Interviews followed an investigator-developed semi-structured topic guide. Data were coded inductively and deductively by one qualitative researcher and one trainee, supported by two additional team members. Analytic themes were established using qualitative thematic analysis. RESULTS: We interviewed 9 AYAs, 10 parents, and 17 HCPs. We identified five analytic themes: importance of clear communication of study information between patients, families and multidisciplinary HCPs; a need to support disclosure, understanding and clinical integration of research results; barriers to accessing innovative therapy and mitigation strategies; approaches to managing parent, patient and HCP hopes and expectations; personal challenges and stressors related to participation. CONCLUSIONS: We highlight unmet needs and offer practical considerations for integrating precision oncology into clinical practice. Considerations include educating and supporting oncologists through genomics results disclosure, increasing engagement with multidisciplinary HCPs, streamlining access to study information and results, coordinating efforts to clinically validate results and access therapies, and establishing real-world outcome data to inform clinical decision-making. Implementation of these strategies will optimize care for patients and families who are navigating poor prognosis cancers.

Humans↗
PubMed2001

Quantitative and reproducible two-dimensional gel analysis using Phoretix 2D Full.

Quantitative two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) is used to determine changes in individual protein levels in complex protein mixtures. To provide reliable data, the software used for 2-D gel image analysis must provide a linear response over a wide dynamic range of data output. Here, we show that Phoretix 2D Full analysis of 2-D gels stained with colloidal Coomassie Brilliant Blue G-250 can provide a linear measure of changes in protein quantity. We show using a complex mixture of Arabidopsis thaliana proteins, that this is true for essentially all focused proteins, in a data output range greater than three orders of magnitude. An analysis of the factors that affect errors in the results demonstrated that reproducibility of the data is significantly improved by user seeding, whereas it is reduced by use of the background subtraction algorithms.

Algorithms↗
PubMed2000

A proteomic analysis of organelles from Arabidopsis thaliana.

We introduce the use of Arabidopsis thaliana callus culture as a system for proteomic analysis of plant organelles using liquid-grown callus. This callus is relatively homogeneous, reproducible and cytoplasmically rich, and provides organelles in sufficient quantities for proteomic studies. A database was generated of mitochondrial, endoplasmic reticulum (ER), Golgi/prevacuolar compartment and plasma membrane (PM) markers using two-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (2-D SDS-PAGE) and peptide sequencing or mass spectrometric methods. The major callus membrane-associated proteins were characterised as being integral or peripheral by Triton X-114 phase partitioning. The database was used to define specific proteins at the Arabidopsis callus plasma membrane. This database of organelle proteins provides the basis for future characterisation of the expression and localisation of novel plant proteins.

Amino Acid Sequence↗
PubMed2000

The PA domain: a protease-associated domain.

We have identified a similarity between the apical domain of the human transferrin receptor and several other protein families. This domain is found associated with two different families of peptidases. Therefore, we term it the PA domain for protease-associated domain. The PA domain is found inserted within a loop of the peptidase domain of family M8/M33 zinc peptidases. The PA domain is also found in a vacuolar sorting receptor and a ring finger protein of unknown function that may be a cell surface receptor. The PA domain may mediate substrate determination of peptidases or form protein-protein interactions.

Amino Acid Sequence↗
PubMed1997

The 3' untranslated region plays a role in the targeting of metallothionein-I mRNA to the perinuclear cytoplasm and cytoskeletal-bound polysomes.

The mechanism of localisation of metallothionein-I (MT-I) mRNA was studied in transfected cells by in situ hybridisation and cell fractionation. Hepatoma cells were transfected with the 5'-untranslated region and coding region of the beta-globin gene alone or linked to either the beta-globin 3'-untranslated region (3'-UTR) or the MT-I 3'-UTR. The wild-type beta-globin mRNA and the beta-globin mRNA lacking its native 3'-UTR were present in free and cytoskeletal-bound polysomes to a similar extent and showed no localisation. Chimaeric globin-metallothionein transcripts were significantly enriched in cytoskeletal-bound polysomes and were localised in the perinuclear cytoplasm. Chimaeric globin-metallothionein and wild-type globin transcripts were of similar stability. Chinese Hamster Ovary cells were transfected with constructs in which the MT-I 5'-untranslated region and coding sequences were linked to either the endogenous 3'-UTR or the glutathione peroxidase 3'-UTR. Wild-type MT-I transcripts were localised in the perinuclear cytoplasm but the chimaeric MT-I-glutathione peroxidase transcripts showed no distinct localisation. The results indicate that the 3'-UTR of MT-I mRNA contains a localisation signal which promotes both the association of the mRNA with the cytoskeleton and its perinuclear localisation.

Animals↗
PubMed1995

Localisation of metallothionein isoform mRNAs in rat hepatoma (H4) cells.

The localisation of metallothionein isoform mRNAs in rat hepatoma (H4) cells was investigated using two approaches, namely Northern hybridisation of total RNA extracted from free, cytoskeletal-bound and membrane-bound polysomes isolated by a sequential detergent/salt extraction procedure and in situ hybridisation. The cytoskeletal-bound polysomes were enriched in metallothionein-I (MT-I) and c-myc mRNAs but showed a significantly lower enrichment in MT-II mRNA. These findings indicate that the MT-I mRNA is localised to the cytoskeleton during translation. In situ hybridisation using a biotin-labelled oligonucleotide probe revealed a predominantly perinuclear localisation for the MT-I mRNA.

Actins↗