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1.
ANZ J Surg ; 91(3): 415-419, 2021 03.
Article in English | MEDLINE | ID: mdl-33538101

ABSTRACT

BACKGROUND: In Australia, the COVID-19 pandemic has caused severe social disruptions, including restrictions to the movement of people. Healthcare centres around the world have seen changes in the nature of injuries acquired during the COVID-19 pandemic; we therefore hypothesize that social isolation measures have changed the pattern of plastic and reconstructive surgery presentations. METHODS: A prospective cohort study was designed comparing patient presentations during the enforced COVID-19 lockdown to two previous periods. All emergency referrals requiring operative intervention by the plastic and reconstructive surgery unit of our institution were included. Patient demographics, place and mechanism of injury, drug and alcohol involvement, delays to presentation, length of admission and complication rates were collected. RESULTS: Demographics and complication rates were similar across all groups. A 31.8% reduction in total number of emergency cases was seen during the lockdown period. Increase in do-it-yourself injuries (P = 0.001), bicycle injuries (P = 0.001) and injuries acquired via substance abuse (P = 0.041) was observed. Head and neck injuries, mostly due to animal bites and falls, were also more prevalent compared to the same period the previous year (P = 0.007). As expected, over 80% of plastic surgery operations during the COVID-19 period were due to injuries acquired at home, a significant increase compared to previous periods. CONCLUSION: Despite changes in the pattern of presentations requiring plastic and reconstructive emergency surgery, traumatic injuries continued to occur during the pandemic. Thus, planning will be essential to ensure resource allocation for emergency procedures is sustained as second and third waves of COVID-19 cases emerge worldwide.


Subject(s)
COVID-19/epidemiology , Emergencies , Pandemics , Quarantine , Adult , Comorbidity , Female , Humans , Male , Prospective Studies , Plastic Surgery Procedures , SARS-CoV-2 , Victoria/epidemiology
2.
Front Surg ; 4: 30, 2017.
Article in English | MEDLINE | ID: mdl-28634582

ABSTRACT

AIM: We investigated the expression of the renin-angiotensin system (RAS) by cancer stem cell (CSC) subpopulations we have identified in moderately differentiated lip squamous cell carcinoma (MDLSCC). METHOD: Ten MDLSCC samples underwent 3,3-diaminobenzidine (DAB) and immunofluorescent immunohistochemical (IHC) staining for (pro)renin receptor (PRR), angiotensin-converting enzyme (ACE), angiotensin II receptor 1 (ATIIR1), and receptor 2 (ATIIR2). NanoString analysis and Western blotting (WB) were performed on six MDLSCC samples for gene and protein expression, respectively. RESULTS: IHC staining showed expression of PRR, ATIIR1, and ATIIR2 on cells within the tumor nests (TNs) and the stroma. ACE was localized to the microvessels within the stroma. WB detected PRR, ACE, and ATIIR2. NanoString analysis confirmed gene expression of PRR, ACE, and ATIIR1. CONCLUSION: Components of the RAS: PRR, ATIIR1, and ATIIR2 are expressed on two CSC subpopulations in MDLSCC, one within the TNs and the other within the stroma. The endothelium of the microvessels within the stroma expresses ACE.

3.
Front Surg ; 4: 12, 2017.
Article in English | MEDLINE | ID: mdl-28321397

ABSTRACT

AIM: To identify and characterize cancer stem cells (CSCs) in moderately differentiated lip squamous cell carcinoma (MDLSCC). METHOD: MDLSCC samples underwent 3,3-diaminobenzidine (DAB) immunohistochemical (IHC) staining for squamous cell carcinoma marker EMA, CSC marker CD44 and embryonic stem cell markers NANOG, octamer-binding transcription factor 4 (OCT4), spalt-like transcription factor 4 (SALL4), sex-determining region Y-box 2 (SOX2), and phosphorylated signal transducer and activator of transcription 3 (pSTAT3). Immunofluorescent IHC staining was performed on two MDLSCC samples. Western blotting (WB) was used to confirm the expression of the aforementioned proteins and their transcription activation was investigated using NanoString and RT-qPCR. RESULTS: IHC staining demonstrated the presence of (1) an EMA+/CD44+/SALL4+/NANOG+/pSTAT3+/SOX2+/OCT4- CSC subpopulation within the tumor nests (TNs); (2) a CD44+/SALL4+/NANOG+/pSTAT3+/SOX2+/OCT4- CSC subpopulation; and (3) a CD44+/SALL4+/NANOG+/pSTAT3+/SOX2+/OCT4+ CSC subpopulation within the stroma, between the TNs. NanoString and RT-qPCR confirmed the presence of mRNA for CD44, SALL4, STAT3, SOX2, and OCT4, and WB confirmed the presence of NANOG, pSTAT3, SOX2, and OCT4. CONCLUSION: This study demonstrates three putative CSC subpopulations within MDLSCC.

4.
Int J Breast Cancer ; 2014: 513780, 2014.
Article in English | MEDLINE | ID: mdl-25383226

ABSTRACT

Introduction. There has been recent interest in validity of completion axillary node dissection after a positive sentinel node. This systematic review aims to ascertain if sentinel lymph node dissection alone was noninferior to axillary lymph node dissection for breast cancer patients who have a positive sentinel node. Method. A systematic review of the electronic databases Embase, MEDLINE, and Cochrane Register of Controlled Trials was carried out. Only randomised trials that had patients with positive sentinel node as the study sample were included in the meta-analysis using the reported hazard ratios with a fixed effect model. Results. Three randomised controlled trials and five retrospective studies were identified. The pooled effect for overall survival was HR 0.94, 95% CI [0.79, 1.19], and for disease free survival was HR 0.83, 95% CI [0.60, 1.14]. The reported rates for locoregional recurrence were similar in both groups. The surgical morbidity was found to be significantly more in patients who had underwent axillary dissection. Conclusion. Amongst patients with micrometastasis in the sentinel node, no further axillary dissection is necessary. For patients with macrometastasis in the sentinel node, it is reasonable to consider omitting axillary dissection to avoid the morbidity of the procedure.

5.
Nature ; 446(7135): 537-41, 2007 Mar 29.
Article in English | MEDLINE | ID: mdl-17344860

ABSTRACT

Microbes comprise the majority of extant organisms, yet much remains to be learned about the nature and driving forces of microbial diversification. Our understanding of how microorganisms adapt and evolve can be advanced by genome-wide documentation of the patterns of genetic exchange, particularly if analyses target coexisting members of natural communities. Here we use community genomic data sets to identify, with strain specificity, expressed proteins from the dominant member of a genomically uncharacterized, natural, acidophilic biofilm. Proteomics results reveal a genome shaped by recombination involving chromosomal regions of tens to hundreds of kilobases long that are derived from two closely related bacterial populations. Inter-population genetic exchange was confirmed by multilocus sequence typing of isolates and of uncultivated natural consortia. The findings suggest that exchange of large blocks of gene variants is crucial for the adaptation to specific ecological niches within the very acidic, metal-rich environment. Mass-spectrometry-based discrimination of expressed protein products that differ by as little as a single amino acid enables us to distinguish the behaviour of closely related coexisting organisms. This is important, given that microorganisms grouped together as a single species may have quite distinct roles in natural systems and their interactions might be key to ecosystem optimization. Because proteomic data simultaneously convey information about genome type and activity, strain-resolved community proteomics is an important complement to cultivation-independent genomic (metagenomic) analysis of microorganisms in the natural environment.


Subject(s)
Bacteria/classification , Bacteria/genetics , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Genome, Bacterial/genetics , Proteomics , Recombination, Genetic/genetics , Amino Acid Sequence , Bacteria/chemistry , Bacteria/enzymology , Biofilms/classification , Genomics , Molecular Sequence Data , Peptides/chemistry , Peptides/genetics , Proteome/chemistry , Proteome/genetics , Ribulose-Bisphosphate Carboxylase/chemistry , Ribulose-Bisphosphate Carboxylase/genetics
6.
Science ; 308(5730): 1915-20, 2005 Jun 24.
Article in English | MEDLINE | ID: mdl-15879173

ABSTRACT

Using genomic and mass spectrometry­based proteomic methods, we evaluated gene expression, identified key activities, and examined partitioning of metabolic functions in a natural acid mine drainage (AMD) microbial biofilm community. We detected 2033 proteins from the five most abundant species in the biofilm, including 48% of the predicted proteins from the dominant biofilm organism, Leptospirillum group II. Proteins involved in protein refolding and response to oxidative stress appeared to be highly expressed, which suggests that damage to biomolecules is a key challenge for survival. We validated and estimated the relative abundance and cellular localization of 357 unique and 215 conserved novel proteins and determined that one abundant novel protein is a cytochrome central to iron oxidation and AMD formation.


Subject(s)
Archaeal Proteins/analysis , Bacteria/metabolism , Bacterial Proteins/analysis , Biofilms , Ecosystem , Mining , Proteomics , Thermoplasmales/metabolism , Amino Acids/metabolism , Archaeal Proteins/chemistry , Bacteria/chemistry , Bacteria/genetics , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Bacterial Proteins/physiology , Biofilms/growth & development , Cytochromes/analysis , Cytochromes/chemistry , Gene Expression , Genes, Archaeal , Genes, Bacterial , Genome, Archaeal , Genome, Bacterial , Genomics , Hydrogen-Ion Concentration , Iron/metabolism , Isoelectric Point , Mass Spectrometry , Molecular Sequence Data , Oxidation-Reduction , Protein Biosynthesis , Protein Folding , Proteome , Thermoplasmales/chemistry , Thermoplasmales/genetics
7.
Nature ; 428(6978): 37-43, 2004 Mar 04.
Article in English | MEDLINE | ID: mdl-14961025

ABSTRACT

Microbial communities are vital in the functioning of all ecosystems; however, most microorganisms are uncultivated, and their roles in natural systems are unclear. Here, using random shotgun sequencing of DNA from a natural acidophilic biofilm, we report reconstruction of near-complete genomes of Leptospirillum group II and Ferroplasma type II, and partial recovery of three other genomes. This was possible because the biofilm was dominated by a small number of species populations and the frequency of genomic rearrangements and gene insertions or deletions was relatively low. Because each sequence read came from a different individual, we could determine that single-nucleotide polymorphisms are the predominant form of heterogeneity at the strain level. The Leptospirillum group II genome had remarkably few nucleotide polymorphisms, despite the existence of low-abundance variants. The Ferroplasma type II genome seems to be a composite from three ancestral strains that have undergone homologous recombination to form a large population of mosaic genomes. Analysis of the gene complement for each organism revealed the pathways for carbon and nitrogen fixation and energy generation, and provided insights into survival strategies in an extreme environment.


Subject(s)
Archaea/genetics , Archaea/metabolism , Bacteria/genetics , Bacteria/metabolism , Environmental Microbiology , Genome, Archaeal , Genome, Bacterial , Archaea/classification , Bacteria/classification , Base Composition , Base Sequence , Biofilms/growth & development , Carbon/metabolism , Ecosystem , Genes, Archaeal/genetics , Genes, Bacterial/genetics , Genetic Complementation Test , Genomics , Molecular Sequence Data , Nitrogen Fixation , Open Reading Frames/genetics , Phylogeny , Polymorphism, Single Nucleotide/genetics , RNA, Ribosomal, 16S/genetics , Recombination, Genetic/genetics , Sequence Analysis, DNA , Species Specificity
8.
Mol Biol Cell ; 13(5): 1484-500, 2002 May.
Article in English | MEDLINE | ID: mdl-12006647

ABSTRACT

The Saccharomyces cerevisiae proteins Sec34p and Sec35p are components of a large cytosolic complex involved in protein transport through the secretory pathway. Characterization of a new secretion mutant led us to identify SEC36, which encodes a new component of this complex. Sec36p binds to Sec34p and Sec35p, and mutation of SEC36 disrupts the complex, as determined by gel filtration. Missense mutations of SEC36 are lethal with mutations in COPI subunits, indicating a functional connection between the Sec34p/sec35p complex and the COPI vesicle coat. Affinity purification of proteins that bind to Sec35p-myc allowed identification of two additional proteins in the complex. We call these two conserved proteins Sec37p and Sec38p. Disruption of either SEC37 or SEC38 affects the size of the complex that contains Sec34p and Sec35p. We also examined COD4, COD5, and DOR1, three genes recently reported to encode proteins that bind to Sec35p. Each of the eight genes that encode components of the Sec34p/sec35p complex was tested for its contribution to cell growth, protein transport, and the integrity of the complex. These tests indicate two general types of subunits: Sec34p, Sec35p, Sec36p, and Sec38p seem to form the essential core of a complex to which Sec37p, Cod4p, Cod5p, and Dor1p seem to be peripherally attached.


Subject(s)
Adaptor Proteins, Vesicular Transport , Carrier Proteins/genetics , Membrane Proteins/genetics , Membrane Transport Proteins , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae/genetics , Carrier Proteins/analysis , Coat Protein Complex I/genetics , Conserved Sequence , Fungal Proteins/metabolism , Glycoside Hydrolases/metabolism , Macromolecular Substances , Mass Spectrometry , Membrane Glycoproteins/metabolism , Membrane Proteins/metabolism , Mutation , Open Reading Frames , Precipitin Tests , Saccharomyces cerevisiae/growth & development , Saccharomyces cerevisiae/metabolism , Saccharomyces cerevisiae Proteins/analysis , Saccharomyces cerevisiae Proteins/metabolism , Vesicular Transport Proteins , beta-Fructofuranosidase
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