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1.
Sports Med Arthrosc Rev ; 30(1): 10-16, 2022 Mar 01.
Article in English | MEDLINE | ID: mdl-35113837

ABSTRACT

Expectations following sports medicine and arthroscopic procedures have been elevated because of captivating modern-day media coverage of high-profile athletic injuries, surgery, and rapid return to sports. Unfortunately, this general perception may be misleading, and orthopedic sports medicine physicians must be aware of the harsh reality of the trials and tribulations associated with the subspecialty. The purpose of this review article is to provide an updated brief overview of the complications and failure rates associated with common arthroscopic procedures including rotator cuff repair, biceps tenodesis, Bankart procedure, Latarjet procedure, anterior cruciate ligament reconstruction, anterior cruciate ligament repair, meniscal repair, tibial tubercle osteotomy, and medial patellofemoral ligament reconstruction. Highlighting the complications is the first step toward early recognition, enhancing preventative measures, and successful management.


Subject(s)
Anterior Cruciate Ligament Injuries , Anterior Cruciate Ligament Reconstruction , Arthroplasty, Replacement, Knee , Anterior Cruciate Ligament , Anterior Cruciate Ligament Injuries/surgery , Arthroscopy , Humans , Knee Joint
2.
Environ Microbiol ; 15(5): 1302-17, 2013 May.
Article in English | MEDLINE | ID: mdl-23126454

ABSTRACT

Heterotrophic marine bacteria play key roles in remineralizing organic matter generated from primary production. However, far more is known about which groups are dominant than about the cellular processes they perform in order to become dominant. In the Southern Ocean, eukaryotic phytoplankton are the dominant primary producers. In this study we used metagenomics and metaproteomics to determine how the dominant bacterial and archaeal plankton processed bloom material. We examined the microbial community composition in 14 metagenomes and found that the relative abundance of Flavobacteria (dominated by Polaribacter) was positively correlated with chlorophyll a fluorescence, and the relative abundance of SAR11 was inversely correlated with both fluorescence and Flavobacteria abundance. By performing metaproteomics on the sample with the highest relative abundance of Flavobacteria (Newcomb Bay, East Antarctica) we defined how Flavobacteria attach to and degrade diverse complex organic material, how they make labile compounds available to Alphaproteobacteria (especially SAR11) and Gammaproteobacteria, and how these heterotrophic Proteobacteria target and utilize these nutrients. The presence of methylotrophic proteins for archaea and bacteria also indicated the importance of metabolic specialists. Overall, the study provides functional data for the microbial mechanisms of nutrient cycling at the surface of the coastal Southern Ocean.


Subject(s)
Flavobacteriaceae/genetics , Flavobacteriaceae/metabolism , Metagenomics , Proteomics , Antarctic Regions , Archaea/classification , Archaea/genetics , Archaea/metabolism , Bacteria/classification , Bacteria/genetics , Bacteria/metabolism , Biodiversity , Chlorophyll/analysis , Chlorophyll/metabolism , Chlorophyll A , Eukaryota/metabolism , Flavobacteriaceae/classification , Heterotrophic Processes , Phylogeny , Phytoplankton/metabolism , Plankton/genetics , Plankton/metabolism , Proteobacteria/metabolism , Seawater/microbiology
3.
ISME J ; 6(10): 1883-900, 2012 Oct.
Article in English | MEDLINE | ID: mdl-22534610

ABSTRACT

A metaproteomic survey of surface coastal waters near Palmer Station on the Antarctic Peninsula, West Antarctica, was performed, revealing marked differences in the functional capacity of summer and winter communities of bacterioplankton. Proteins from Flavobacteria were more abundant in the summer metaproteome, whereas winter was characterized by proteins from ammonia-oxidizing Marine Group I Crenarchaeota. Proteins prevalent in both seasons were from SAR11 and Rhodobacterales clades of Alphaproteobacteria, as well as many lineages of Gammaproteobacteria. The metaproteome data were used to elucidate the main metabolic and energy generation pathways and transport processes occurring at the microbial level in each season. In summer, autotrophic carbon assimilation appears to be driven by oxygenic photoautotrophy, consistent with high light availability and intensity. In contrast, during the dark polar winter, the metaproteome supported the occurrence of chemolithoautotrophy via the 3-hydroxypropionate/4-hydroxybutyrate cycle and the reverse tricarboxylic acid cycle of ammonia-oxidizing archaea and nitrite-oxidizing bacteria, respectively. Proteins involved in nitrification were also detected in the metaproteome. Taurine appears to be an important source of carbon and nitrogen for heterotrophs (especially SAR11), with transporters and enzymes for taurine uptake and degradation abundant in the metaproteome. Divergent heterotrophic strategies for Alphaproteobacteria and Flavobacteria were indicated by the metaproteome data, with Alphaproteobacteria capturing (by high-affinity transport) and processing labile solutes, and Flavobacteria expressing outer membrane receptors for particle adhesion to facilitate the exploitation of non-labile substrates. TonB-dependent receptors from Gammaproteobacteria and Flavobacteria (particularly in summer) were abundant, indicating that scavenging of substrates was likely an important strategy for these clades of Southern Ocean bacteria. This study provides the first insight into differences in functional processes occurring between summer and winter microbial communities in coastal Antarctic waters, and particularly highlights the important role that 'dark' carbon fixation has in winter.


Subject(s)
Bacteria/classification , Crenarchaeota/classification , Proteome/analysis , Seasons , Seawater/microbiology , Ammonia/metabolism , Antarctic Regions , Bacteria/metabolism , Crenarchaeota/metabolism , Heterotrophic Processes , Nitrification , Oceans and Seas , Phylogeny , Plankton/classification , Plankton/metabolism , Water/metabolism
4.
Biochem Pharmacol ; 70(7): 1088-95, 2005 Oct 01.
Article in English | MEDLINE | ID: mdl-16099435

ABSTRACT

Multidrug resistance-associated proteins (Mrps) are a group of ATP-dependent efflux transporters for organic anions. Mrp2 and Mrp4 are co-localized to the apical (brush-border) membrane domain of renal proximal tubules, where they may function together in the urinary excretion of organic anions. Previous reports showed that urinary excretion of some organic anions is not impaired in transport-deficient (TR-) rats, which lack Mrp2, suggesting that up-regulation of other transporter(s) may compensate for the loss of Mrp2 function. The purpose of this study was to determine whether Mrp4 expression in kidney is altered in TR- rats. Mrp4 mRNA expression was quantified using the high-throughput branched DNA signal amplification assay. Mrp4 protein expression was determined by Western blot and immunohistochemical analysis. Mrp4 mRNA in kidney of TR- rats was 100% higher than normal Wistar rats. Western blot analysis showed a 200% increase in Mrp4 protein expression in kidney of the mutant rats compared to normal rats. Immunohistochemical analysis of Mrp4 protein demonstrated apical localization of Mrp4 on renal proximal tubules, and that the immunoreactivity was more intense in kidney sections from TR- rats than those from normal rats. In summary, the results of the present study demonstrate that renal Mrp4 expression is up-regulated in TR- rats, which may explain why urinary excretion of some organic anions remains normal in the mutant rats.


Subject(s)
Kidney/metabolism , Mitochondrial Proteins/metabolism , Multidrug Resistance-Associated Proteins/metabolism , Ribosomal Proteins/metabolism , Saccharomyces cerevisiae Proteins/metabolism , Up-Regulation , Animals , Blotting, Western , Glucuronosyltransferase/genetics , Immunohistochemistry , Male , Mitochondrial Proteins/genetics , Multidrug Resistance-Associated Proteins/genetics , RNA, Messenger/genetics , Rats , Rats, Gunn , Rats, Wistar , Ribosomal Proteins/genetics , Saccharomyces cerevisiae Proteins/genetics
5.
J Bacteriol ; 182(12): 3383-93, 2000 Jun.
Article in English | MEDLINE | ID: mdl-10852868

ABSTRACT

Peptidase B (PepB) of Salmonella enterica serovar Typhimurium is one of three broad-specificity aminopeptidases found in this organism. We have sequenced the pepB gene and found that it encodes a 427-amino-acid (46.36-kDa) protein, which can be unambiguously assigned to the leucyl aminopeptidase (LAP) structural family. PepB has been overexpressed and purified. The active enzyme shows many similarities to other members of the LAP family: it is a heat-stable (70 degrees C; 20 min) hexameric ( approximately 270-kDa) metallopeptidase with a pH optimum of 8.5 to 9.5. A detailed study of the substrate specificity of the purified protein shows that it differs from other members of the family in its ability to hydrolyze peptides with N-terminal acidic residues. The preferred substrates for PepB are peptides with N-terminal Asp or Glu residues. Comparison of the amino acid sequence of PepB with those of other LAPs leads to the conclusion that PepB is the prototype of a new LAP subfamily with representatives in several other eubacterial species and to the prediction that the members of this family share the ability to hydrolyze peptides with N-terminal acidic residues. Site-directed mutagenesis has been used to show that this specificity appears to be determined by a single Lys residue present in a sequence motif conserved in all members of the subfamily.


Subject(s)
Amino Acids/metabolism , Aminopeptidases/metabolism , Leucyl Aminopeptidase/metabolism , Salmonella typhimurium/enzymology , Amino Acid Sequence , Aminopeptidases/chemistry , Aminopeptidases/genetics , Aminopeptidases/isolation & purification , Base Sequence , Cloning, Molecular , DNA, Bacterial/genetics , Dipeptidyl-Peptidases and Tripeptidyl-Peptidases , Kinetics , Leucyl Aminopeptidase/chemistry , Leucyl Aminopeptidase/genetics , Molecular Sequence Data , Peptides/metabolism , Phylogeny , Plasmids/genetics , Salmonella typhimurium/genetics , Sequence Alignment , Sequence Analysis, DNA , Substrate Specificity
7.
Int J Zoonoses ; 13(1): 45-8, 1986 Mar.
Article in English | MEDLINE | ID: mdl-3019914

ABSTRACT

An epidemic of buffalo pox infection in buffaloes, white cattle, horses, goats and human beings in the Dhule district of Maharashtra State (India) during December, 1975 to March, 1976 is reported. Buffalo pox virus from this epidemic has been propagated in BHK-21 cell line directly from the skin scab materials collected from those animals in phosphate glycerine buffer. A specific cytopathic effect (CPE) produced in these cell lines was differentiated from the non-specific CPE by the demonstration of the characteristic 'Rosette' or 'Sun flower' like haemadsorption with 0.4% fowl erythrocytes. The CPE started appearing as early as 18 hours and the detachment and peeling off the cells from the glass surface were noted on the 4th day onwards. Eosinophilic inclusion bodies with giant cells (multi-nucleated) formation and fusion of the cells were also observed with a few stellate cells.


Subject(s)
Hemadsorption , Poxviridae/growth & development , Animals , Buffaloes , Cattle , Cell Line , Cytopathogenic Effect, Viral , Goats , Horses , Humans , Poxviridae/isolation & purification , Poxviridae/metabolism , Poxviridae Infections/microbiology , Poxviridae Infections/veterinary , Rosette Formation , Skin/microbiology , Virus Cultivation
9.
Indian Vet J ; 47(3): 251-2, 1970 Mar.
Article in English | MEDLINE | ID: mdl-5462930
11.
Indian Vet J ; 44(3): 257-9, 1967 Mar.
Article in English | MEDLINE | ID: mdl-6068481
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