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1.
HPB (Oxford) ; 23(4): 595-600, 2021 04.
Artigo em Inglês | MEDLINE | ID: mdl-32988751

RESUMO

BACKGROUND: Discussing the impact of pancreatic surgery on long-term health is poorly understood, but necessary for informed consent. Given the increased number of pancreatic operations being performed annually, further investigation is necessary. METHODS: Patients surviving longer than 5 years after pancreatic surgery were surveyed for postoperative hospitalizations, operations, pain, nutrition and diabetes. Variables were analyzed according to patient and peri-operative variables, and validated using medical records. RESULTS: Eighty individuals completed the survey; median follow-up was 9.5 years (IQR:6.43,12.73). 47.5% underwent a pancreatoduodenectomy, and 25.0% a distal pancreatectomy; 40.0% had adenocarcinoma. 57.1% reported long-term weight loss, of which 65.9% was unintentional. While 1.3% took pancreatic enzymes before surgery, 38.8% utilized after. 12.5% had diabetes before, and 28.6% after surgery; 22 of 30 patients required insulin replacement therapy (73.3%). 41.3% reported hospitalizations, 17.5% required endoscopies and 28.8% additional operations after full recovery. Need for additional interventions were not related to pathology or post-operative complications, but were more common among patients undergoing a Whipple. CONCLUSION: More than half of patients will have a long-term medical complication attributable to pancreatectomy. In comparison to the literature, it may be inferred that consequences occur within the first few years after surgery, and do not compound over time.


Assuntos
Adenocarcinoma , Neoplasias Pancreáticas , Humanos , Pancreatectomia/efeitos adversos , Neoplasias Pancreáticas/cirurgia , Pancreaticoduodenectomia/efeitos adversos , Complicações Pós-Operatórias/etiologia , Resultado do Tratamento
2.
Am J Orthop (Belle Mead NJ) ; 46(1): 10-16, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28235107

RESUMO

In this review, we describe precise methods for evaluating the athlete's hip or groin with an emphasis on recognizing the most common extra-articular and intra-articular pathologies, including adductor strains, athletic pubalgia, osteitis pubis, and femoroacetabular impingement with labral tears.


Assuntos
Atletas , Traumatismos em Atletas/diagnóstico , Impacto Femoroacetabular/diagnóstico , Lesões do Quadril/diagnóstico , Humanos , Exame Físico/métodos
3.
J Phys Chem B ; 119(49): 15235-46, 2015 Dec 10.
Artigo em Inglês | MEDLINE | ID: mdl-26569483

RESUMO

Piscidins were the first antimicrobial peptides discovered in the mast cells of vertebrates. While two family members, piscidin 1 (p1) and piscidin 3 (p3), have highly similar sequences and α-helical structures when bound to model membranes, p1 generally exhibits stronger antimicrobial and hemolytic activity than p3 for reasons that remain elusive. In this study, we combine activity assays and biophysical methods to investigate the mechanisms underlying the cellular function and differing biological potencies of these peptides, and report findings spanning three major facets. First, added to Gram-positive (Bacillus megaterium) and Gram-negative (Escherichia coli) bacteria at sublethal concentrations and imaged by confocal microscopy, both p1 and p3 translocate across cell membranes and colocalize with nucleoids. In E. coli, translocation is accompanied by nonlethal permeabilization that features more pronounced leakage for p1. Second, p1 is also more disruptive than p3 to bacterial model membranes, as quantified by a dye-leakage assay and (2)H solid-state NMR-monitored lipid acyl chain order parameters. Oriented CD studies in the same bilayers show that, beyond a critical peptide concentration, both peptides transition from a surface-bound state to a tilted orientation. Third, gel retardation experiments and CD-monitored titrations on isolated DNA demonstrate that both peptides bind DNA but p3 has stronger condensing effects. Notably, solid-state NMR reveals that the peptides are α-helical when bound to DNA. Overall, these studies identify two polyreactive piscidin isoforms that bind phosphate-containing targets in a poised amphipathic α-helical conformation, disrupt bacterial membranes, and access the intracellular constituents of target cells. Remarkably, the two isoforms have complementary effects; p1 is more membrane active, while p3 has stronger DNA-condensing effects. Subtle differences in their physicochemical properties are highlighted to help explain their contrasting activities.


Assuntos
Peptídeos Catiônicos Antimicrobianos/farmacologia , DNA/efeitos dos fármacos , Proteínas de Peixes/farmacologia , Membranas Artificiais , Peptídeos Catiônicos Antimicrobianos/química , Biofísica , Proteínas de Peixes/química , Espectroscopia de Ressonância Magnética , Conformação Proteica
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