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2.
Dermatol Surg ; 28(11): 971-8, 2002 Nov.
Article in English | MEDLINE | ID: mdl-12460288

ABSTRACT

BACKGROUND: Liposuction procedures are increasing in frequency and may be performed in hospitals, ambulatory surgery centers, or physician offices. Deaths associated with liposuction and previous surveys of liposuction safety have raised concern about the safety of office-based surgery. OBJECTIVE: To determine the safety of office-based, tumescent liposuction among dermatologic surgeons. METHODS: A survey mailed out to dermatologic surgeons in August 2001 requested retrospective information regarding the number of patients undergoing liposuction, the setting in which the procedures were performed, and the complications that occurred during the 7-year period from 1994 to 2000. A detailed complication record was requested for each serious adverse event or death reported. Surveys were mailed to 517 worldwide members of the American Society for Dermatologic Surgery (ASDS) listed as performing liposuction; 505 had adequate contact information. The main outcome mesure was the rate of serious adverse events (SAEs) or deaths per 1000 liposuction procedures for each service setting and for each level of conscious sedation. RESULTS: The overall response rate was 89% (450/505), and of these, 78% (349/450) perform liposuction. A total of 267 dermatologic surgeons completed the survey; 261 provided data on 66,570 liposuction procedures. No deaths were reported. The overall serious adverse event rate was 0.68 per 1000 cases. The SAE rates were higher for hospitals and ambulatory surgery centers than for nonaccredited office settings. SAE rates were also higher for tumescent liposuction combined with intravenous or intramuscular sedation than combined with oral or no sedation. CONCLUSION: Office-based tumescent liposuction performed by dermatologic surgeons is safe, with a lower complication rate than hospital-based procedures. Future legislation should recognize the proven safety of this procedure as performed by dermatologic surgeons in their offices.


Subject(s)
Ambulatory Surgical Procedures/adverse effects , Lipectomy/adverse effects , Adult , Aged , Ambulatory Surgical Procedures/statistics & numerical data , Data Collection , Dermatology , Female , Humans , Lipectomy/mortality , Lipectomy/statistics & numerical data , Male , Middle Aged , Outpatient Clinics, Hospital/statistics & numerical data , Physicians' Offices/statistics & numerical data , Postoperative Period , Retrospective Studies , Surgicenters/statistics & numerical data , United States
3.
Mol Biol Cell ; 12(2): 309-21, 2001 02.
Article in English | MEDLINE | ID: mdl-11179417

ABSTRACT

Mitochondria are dynamic organelles that undergo frequent division and fusion, but the molecular mechanisms of these two events are not well understood. Dnm1p, a mitochondria-associated, dynamin-related GTPase was previously shown to mediate mitochondrial fission. Recently, a genome-wide yeast two-hybrid screen identified an uncharacterized protein that interacts with Dnm1p. Cells disrupted in this new gene, which we call NET2, contain a single mitochondrion that consists of a network formed by interconnected tubules, similar to the phenotype of dnm1 Delta cells. NET2 encodes a mitochondria-associated protein with a predicted coiled-coil region and six WD-40 repeats. Immunofluorescence microscopy indicates that Net2p is located in distinct, dot-like structures along the mitochondrial surface, many of which colocalize with the Dnm1 protein. Fluorescence and immunoelectron microscopy shows that Dnm1p and Net2p preferentially colocalize at constriction sites along mitochondrial tubules. Our results suggest that Net2p is a new component of the mitochondrial division machinery.


Subject(s)
Carrier Proteins/metabolism , Fungal Proteins/metabolism , Mitochondria/genetics , Mitochondria/metabolism , Saccharomyces cerevisiae Proteins , Yeasts/metabolism , Actins/metabolism , Actins/ultrastructure , Adaptor Proteins, Signal Transducing , Base Sequence , Carrier Proteins/genetics , Cytoskeleton/genetics , Cytoskeleton/ultrastructure , Fungal Proteins/genetics , GTP Phosphohydrolases/genetics , GTP Phosphohydrolases/metabolism , Membrane Proteins/genetics , Membrane Proteins/metabolism , Mitochondria/ultrastructure , Mitochondrial Proteins , Molecular Sequence Data , Mutation , Open Reading Frames , Repetitive Sequences, Amino Acid , Yeasts/genetics
4.
Infect Immun ; 68(2): 732-9, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10639440

ABSTRACT

Porphyromonas gingivalis is a major etiologic agent of periodontitis, a chronic inflammatory disease that ultimately results in the loss of the supporting tissues of the teeth. Previous work has demonstrated the usefulness of avirulent Salmonella enterica serovar Typhimurium strains as antigen delivery systems for protective antigens of pathogens that colonize or cross mucosal surfaces. In this study, we constructed and characterized a recombinant S. enterica serovar Typhimurium avirulent vaccine strain which expresses hemagglutinin A and carries no antibiotic resistance markers. HagA, a major virulence-associated surface protein, is a potentially useful immunogen that contains an antigenic epitope which, in humans, elicits an immune response that is protective against subsequent colonization by P. gingivalis. The hagA gene, including its promoter, was cloned into a balanced-lethal Salmonella vector and transferred to the vaccine strain. Heterologous expression of HagA was demonstrated in both Escherichia coli JM109 and S. enterica serovar Typhimurium vaccine strain chi4072. The HagA epitope was present in its native configuration as determined by immunochemistry and immunoelectron microscopy. Purified recombinant HagA was recognized by sera from mice immunized with the S. enterica serovar Typhimurium vaccine strain. The HagA-specific antigen of the vaccine was also found to be recognized by serum from a periodontal patient. This vaccine strain, which expresses the functional hemagglutinin protein, induces a humoral immune response against HagA and may be useful for developing a protective vaccine against periodontal diseases associated with P. gingivalis.


Subject(s)
Bacterial Proteins , Bacterial Vaccines/immunology , Hemagglutinins/immunology , Porphyromonas gingivalis/immunology , Salmonella typhimurium/immunology , Vaccines, Synthetic/immunology , Amino Acid Sequence , Animals , Female , Humans , Lectins , Mice , Mice, Inbred BALB C , Microscopy, Immunoelectron , Molecular Sequence Data , Plasmids
5.
Microsc Res Tech ; 51(6): 573-83, 2000 Dec 15.
Article in English | MEDLINE | ID: mdl-11169859

ABSTRACT

Mitochondria are essential organelles found in virtually all eukaryotic cells that play key roles in a variety of cellular processes. Mitochondria show a striking heterogeneity in their number, location, and shape in many different cell types. Although the dynamic nature of mitochondria has been known for decades, the molecules and mechanisms that mediate these processes are largely unknown. Recently, several laboratories have isolated and analyzed mutants in the yeast Saccharomyces cerevisiae defective in mitochondrial fusion and division, in the segregation of mitochondria to daughter cells, and in the establishment and maintenance of mitochondrial shape. These studies have identified several proteins that appear to mediate different aspects of mitochondrial morphogenesis. Although it is clear that many additional components have yet to be identified, some of the newly discovered proteins raise intriguing possibilities for how the processes of mitochondrial division, fusion, and segregation occur. Below we summarize our current understanding of the molecules known to be required for yeast mitochondrial dynamics.


Subject(s)
Mitochondria/physiology , Saccharomyces cerevisiae/physiology , Cell Division/physiology , Fungal Proteins/genetics , Fungal Proteins/metabolism , Mitochondria/genetics , Mitochondria/ultrastructure , Saccharomyces cerevisiae/genetics
6.
Lupus ; 8(6): 477-81, 1999.
Article in English | MEDLINE | ID: mdl-10483019

ABSTRACT

SUMMARY: The catastrophic antiphospholipid antibody syndrome (CAPS) is an uncommon disorder characterized by widespread micro- and macrovascular changes due to intravascular thrombosis. This complication of the antiphospholipid antibody syndrome is often fatal and recurrences are very rare. The differential diagnosis of CAPS includes thrombotic thrombocytopenic purpura (TTP) and this distinction may be difficult, but essential, for appropriate therapy. Plasmapheresis is effective in both conditions, but anticoagulation, a mainstay in the treatment of CAPS, could be disastrous in TTP. We present the case of an elderly woman who survived two episodes of CAPS four years apart and whose clinical findings were also suggestive of TTP. The characteristics of TTP and CAPS are compared and the importance of accurate diagnosis is emphasized.


Subject(s)
Antiphospholipid Syndrome , Purpura, Thrombotic Thrombocytopenic , Aged , Antiphospholipid Syndrome/diagnosis , Antiphospholipid Syndrome/immunology , Antiphospholipid Syndrome/physiopathology , Diagnosis, Differential , Female , Humans , Purpura, Thrombotic Thrombocytopenic/diagnosis , Purpura, Thrombotic Thrombocytopenic/immunology , Purpura, Thrombotic Thrombocytopenic/physiopathology , Recurrence
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