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1.
Chinese Journal of Practical Surgery ; (12): 810-811, 2019.
Artigo em Chinês | WPRIM | ID: wpr-816466

RESUMO

Female adolescent is in the beginning of sexual maturity period and get into stage of give birth. The key points of management for the inguinal hernia of female adolescent is to cure the hernia, decrease the incidence of recurrence and the complications and protect the round ligament uterus, avoid damage to reproductive function. Tension free hernia repair is the mainly method for inguinal hernia management.Laparoscopic hernia repair is good in decrease the incidence of post operation recurrence and the chronic pain in female adolescent inguinal hernia.

2.
Protein & Cell ; (12): 520-528, 2013.
Artigo em Inglês | WPRIM | ID: wpr-757787

RESUMO

The peptide angiotensin IV (Ang IV) is a derivative of angiotensin II. While insulin regulated amino peptidase (IRAP) has been proposed as a potential receptor for Ang IV, the signalling pathways of Ang IV through IRAP remain elusive. We applied high-resolution mass spectrometry to perform a systemic quantitative phosphoproteome of Neura-2A (N2A) cells treated with and without Ang IV using sta ble-isotope labeling by amino acids in cell culture (SILAC), and identified a reduction in the phosphorylation of a major Ser/Thr protein phosphorylase 1 (PP1) upon Ang IV treatment. In addition, spinophilin (spn), a PP1 regulatory protein that plays important functions in the neural system, was expressed at higher levels. Immunoblotting revealed decreased phosphorylation of p70S6 kinase (p70(S6K)) and the major cell cycle modulator retinoblastoma protein (pRB). These changes are consistent with an observed decrease in cell proliferation. Taken together, our study suggests that Ang IV functions via regulating the activity of PP1.


Assuntos
Animais , Humanos , Camundongos , Ratos , Angiotensina II , Farmacologia , Ciclo Celular , Linhagem Celular Tumoral , Membrana Celular , Metabolismo , Núcleo Celular , Metabolismo , Proliferação de Células , Proteínas dos Microfilamentos , Metabolismo , Proteínas do Tecido Nervoso , Metabolismo , Neurônios , Biologia Celular , Fosforilação , Proteína Fosfatase 1 , Química , Metabolismo , Transporte Proteico , Proteoma , Metabolismo , Treonina , Metabolismo , Regulação para Cima
3.
Chinese Medical Journal ; (24): 316-320, 2012.
Artigo em Inglês | WPRIM | ID: wpr-333495

RESUMO

<p><b>BACKGROUND</b>Neuroblastoma (NB) is one of the most common malignant solid tumors of childhood. It is still not clear whether the apoptosis of tumor cells or the non-tumor cells contributes to the increase of concentration of cytochrome c (Cyt c) in the serum of the cancer patients. The aim of this research was to identify the source of the Cyt c in the serum when the tumor grows up by subcutaneous inoculation of human NB cells into nude mice.</p><p><b>METHODS</b>We subcutaneously inoculated human NB cells (KP-N-NS) into nude mice and collected the sera of tumor-bearing mice (n = 14) and control mice (n = 25) 4 weeks later in order to screen for and identify differentially expressed proteins in the serum. Differentially expressed proteins in the serum were screened by surface-enhanced laser desorption/ionization-time-of-flight (SELDI-TOF) mass spectrometry.</p><p><b>RESULTS</b>The relative intensity of a protein having a mass-to-charge ratio (m/z) of 11 609 was 3338.37 ± 3410.85 in the tumor group and 59.84 ± 40.74 in the control group, indicating that the expression level of this protein in the tumor group was 55.8 times higher than that in the control group. Serum proteins were separated and purified by high-performance liquid chromatography (HPLC). Liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) was performed to produce peptide mass fingerprints (PMFs). Spectrum analysis and a database search revealed that the highly expressed protein (m/z = 11 605.4) from the serum of tumor-bearing mice was the mouse Cyt c.</p><p><b>CONCLUSIONS</b>Increased concentration of Cyt c in the serum of tumor-bearing nude mice might be partially attributed to the secretion of this protein by non-tumor cells.</p>


Assuntos
Animais , Feminino , Humanos , Camundongos , Apoptose , Fisiologia , Linhagem Celular Tumoral , Cromatografia Líquida de Alta Pressão , Citocromos c , Sangue , Camundongos Nus , Neuroblastoma , Sangue , Espectrometria de Massas em Tandem , Ensaios Antitumorais Modelo de Xenoenxerto
4.
Chinese Journal of Oncology ; (12): 265-268, 2009.
Artigo em Chinês | WPRIM | ID: wpr-293135

RESUMO

<p><b>OBJECTIVE</b>To detect and identify the potential specific serum biomarkers for diagnosis of papillary thyroid cancer.</p><p><b>METHODS</b>Samples of 35 patients with papillary thyroid carcinoma, 40 patients with benign thyroid nodule and 34 healthy individuals were analyzed using the SELDI-TOF ProteinChip System and bioinfomation technology to find the differential peaks which were separated by HPLC and then further analyzed by LC-MS/MS. The protein sequences were analyzed by SEQUEST software and searched in Bioworks database.</p><p><b>RESULTS</b>The top six mass-to-charge ratio (M/Z) peaks with the smallest P value were 6651, 6452, 7653, 7932, 15 106 and 15 848 Da, respectively. The 6651 and 6452 Da proteins were weakly expressed in papillary thyroid carcinoma but highly expressed in benign thyroid nodules and healthy individuals. The differences had statistical significance (P < 0.01). The 7653, 7932, 15 106, 15 848 Da proteins were highly expressed in papillary thyroid carcinoma but weakly expressed in benign thyroid nodules and healthy individuals. The differences were statistically significant (P < 0.01). Combination of these six proteins, using the method of leave-one-out to make crossing detection, the specificity of discriminating papillary thyroid carcinoma and non-cancer was 88.0%, and its sensitivity was 92.5%. The 6651 and 6452 Da proteins were identified as apolipoprotein C-I and apolipoprotein C-III, respectively. The 7653 and 15 106 Da proteins were identified as the same protein-alpha-globin, and the 7932 and 15,848 Da proteins were identified as the same protein-beta-globin.</p><p><b>CONCLUSION</b>The detection of differentially expressed apolipoprotein C-I, apolipoprotein C-III, alpha-globin, and beta-globin may have utility for diagnosis of papillary thyroid carcinoma and are worthy of further investigation.</p>


Assuntos
Adulto , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Apolipoproteína C-I , Sangue , Apolipoproteína C-III , Sangue , Biomarcadores Tumorais , Sangue , Carcinoma Papilar , Sangue , Diagnóstico , Análise Serial de Proteínas , Proteômica , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Neoplasias da Glândula Tireoide , Sangue , Diagnóstico , alfa-Globinas , Metabolismo , Globinas beta , Metabolismo
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