RESUMO
PURPOSE: A paravertebral block (PVB) given via the surgical field can be safer and technically simpler than an epidural block (EP) for postoperative pain control. We conducted this clinical trial to confirm the effectiveness of PVB after thoracotomy. METHODS: In this non-inferiority trial, patients were randomly assigned to receive PVB (n = 35) or EP (n = 35). The primary endpoint was the pain assessed using the visual analog scale (VAS) at rest, 2, 24, and 48 h after thoracotomy, with the non-inferiority margin set at 15 mm. The secondary end points were the pain assessed using the VAS on exercising and on coughing, 2, 24, and 48 h after surgery, respectively, and the complications and need for additional analgesic agents. RESULTS: This trial revealed that PVB was not inferior to EP with respect to the primary end point: The mean VAS scores at rest, 2, 24, and 48 h after thoracotomy were 26.3, 10.8, and 8.3 mm in the PVB group and 23.6, 12.4, and 12.6 mm in the EP group, respectively (P < 0.01 for non-inferiority at all points). There were no significant differences between the groups in the incidence of complications or the need for additional analgesic agents. CONCLUSION: PVB may replace EP for postoperative pain control because of its technical simplicity and safety.
Assuntos
Anestesia Epidural , Bloqueio Nervoso/métodos , Dor Pós-Operatória/prevenção & controle , Toracotomia , Adulto , Idoso , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Dor Pós-Operatória/diagnóstico , Fatores de Tempo , Adulto JovemRESUMO
Full-length cDNA that encodes feline α1-microglobulin (Feα1m)-bikunin was obtained from a feline liver and cloned using an oligo-capping method. The Feα1m-bikunin cDNA was found to contain 1284 nucleotides, and Feα1m was found to include an open reading frame encoding a polypeptide of 201 amino acids. The deduced amino acid sequence of Feα1m showed varying amino acid identity when compared with the published sequences of the related α1-m of other species, ranging from 71.1 to 82.1%. Feα1m mRNA expression was confirmed by reverse transcription polymerase chain reaction (RT-PCR) and real-time PCR analysis in the cerebrum, cerebellum, lung, heart, liver, spleen, pancreas, kidney, adrenal gland, and testicle. The highest Feα1m mRNA level was found in the liver.
Assuntos
alfa-Globulinas/genética , alfa-Globulinas/biossíntese , Sequência de Aminoácidos , Animais , Sequência de Bases , Gatos/genética , Clonagem Molecular , Fígado/metabolismo , Fases de Leitura Aberta/genética , RNA Mensageiro/genética , Reação em Cadeia da Polimerase Via Transcriptase Reversa/veterinária , Alinhamento de SequênciaRESUMO
Cystatin C is a member of the cystatin superfamily of low-molecular-weight proteins that inhibit the activity of cysteine protease. The full-length cDNA that encodes feline cystatin C (FeCysC) has been cloned from feline white blood cells by the oligo-capping method. The cDNA consists of 796 nucleotides and includes an open reading frame encoding a polypeptide of 146 amino acids. Next, we developed several mouse anti-FeCysC monoclonal antibodies (mAbs). The recombinant FeCysC (rFeCysC) was expressed in Escherichia coli (E. coli) BL21 and used as an antigen to immunise mice. The reactivity of the mAbs to native FeCysC was examined by western blot analysis against the urinary protein from cats with chronic kidney disease (CKD). The three anti-rFeCysC mAbs (3-9G, 7-7C, and 9-12F) were able to recognise native FeCysC.
