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1.
Zhonghua Wai Ke Za Zhi ; 61(9): 807-811, 2023 Sep 01.
Article in Chinese | MEDLINE | ID: mdl-37491175

ABSTRACT

Objective: To compare the clinical effects of endoscopic thyroidectomy using a modified gasless transsubclavian approach and the traditional neck approach for unilateral papillary thyroid carcinoma (cN0). Methods: The clinical data of 135 patients with cN0 papillary thyroid carcinoma who underwent unilateral thyroidectomy in the Department of Thyroid Surgery, the First Hospital of Jilin University from October 2020 to November 2022 were retrospectively analyzed. There were 37 males and 98 females, aging (43.2±8.8) years (range: 21 to 59 years). There were 51 cases using the modified gasless transsubclavian approach (TS group) and 84 cases using the traditional neck approach (TN group). Comparative analyses were performed between the operative results of the 2 groups by t-test, Wilcoxon rank sum test, and χ2 test. Results: All endoscopic operations were successfully completed without conversion to the traditional neck approach. Compared to the TN group, the TS group had a longer operation time (M(IQR)) (73.5 (22.5) minutes vs. 90.0 (30.0) minutes, Z=-5.831, P<0.01), more postoperative drainage (60 (25) ml vs. 95 (45) ml, Z=-6.275, P<0.01), higher hospitalization costs (22 687 (3 488) yuan vs. 26 652 (2 431) yuan, Z=-6.944, P<0.01), and a higher rate of parathyroid autotransplantation (15.5% (13/84) vs. 60.8% (31/51), χ2=29.651, P<0.01). There was no significant difference in the total exposure rate of the central compartment, postoperative hospitalization time, the number of dissected lymph nodes, the number of metastatic lymph nodes, C-reactive protein ratio before and after operation, and preoperative and postoperative parathyroid hormone (all P>0.05). Conclusion: Endoscopic thyroidectomy using the modified gasless transsubclavian approach is safe for cN0 papillary thyroid carcinoma, with longer operating time, more postoperative drainage, higher hospitalization costs, and more difficulty in preserving the inferior parathyroid gland in situ compared to traditional open surgery.


Subject(s)
Carcinoma, Papillary , Thyroid Neoplasms , Male , Female , Humans , Thyroid Cancer, Papillary/surgery , Thyroidectomy/methods , Thyroid Neoplasms/surgery , Thyroid Neoplasms/pathology , Retrospective Studies , Neck Dissection/methods , Carcinoma, Papillary/surgery , Endoscopy
2.
Zhonghua Yi Xue Za Zhi ; 99(7): 481-483, 2019 Feb 19.
Article in Chinese | MEDLINE | ID: mdl-30786343
3.
Plant J ; 26(6): 561-71, 2001 Jun.
Article in English | MEDLINE | ID: mdl-11489170

ABSTRACT

We have cloned a phosphatidylinositol-4-phosphate 5-kinase (PIP5K) cDNA (AtP5K1) from Arabidopsis thaliana. By the application of cell permeabilization and short-term nonequilibrium labelling we show that expression of AtP5K1 in Baculovirus-infected insect (Spodoptera frugiperda) cells directs synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3. The same phosphoinositides were produced by isolated whole-cell membrane fractions of AtP5K1-expressing insect cells. Their synthesis was not affected by adding defined precursor lipids, that is PtdIns(3)P, PtdIns(4)P, PtdIns(3,4)P2, or PtdIns(4,5)P2, in excess, indicating that substrates for the plant enzyme were not limiting in vivo. Enzymatic dissection of lipid headgroups revealed that AtP5K1-directed synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 proceeds via 5-phosphorylation of precursors. Analysis of promoter-reporter gene (beta-glucuronidase) fusions in transgenic plants revealed that expression of the AtP5K1 gene is strongest in vascular tissues of leaves, flowers, and roots, namely in cells of the lateral meristem, that is the procambium. Single-cell sampling of sap from flower stem meristem tissue and neighbouring phloem cells, when coupled to reverse transcriptase--polymerase chain reaction, confirmed preferential expression of AtP5K1 in procambial tissue. We hypothesize that AtP5K1, like animal and yeast PIP5K, may be involved in the control of cell proliferation.


Subject(s)
Arabidopsis/enzymology , Phosphatidylinositol 4,5-Diphosphate/biosynthesis , Phosphatidylinositol Phosphates/biosynthesis , Phosphotransferases (Alcohol Group Acceptor)/metabolism , Animals , Arabidopsis/cytology , Base Sequence , Cloning, Molecular , DNA Primers , Molecular Sequence Data , Phosphorylation , Phosphotransferases (Alcohol Group Acceptor)/genetics , Promoter Regions, Genetic , Spodoptera
4.
Plant Mol Biol ; 42(5): 757-64, 2000 Mar.
Article in English | MEDLINE | ID: mdl-10809447

ABSTRACT

It is believed that phosphatidylinositol (PI) metabolism plays a central role in signalling pathways in both animals and higher plants. PI is synthesized from CDP-diacylglycerol (CDP-DG) and myo-inositol by phosphatidylinositol synthase (PI synthase, EC 2.7.8.11). Here we report the identification of a plant cDNA (AtPIS1) encoding a 26 kDa PI synthase from Arabidopsis thaliana. The plant enzyme as deduced from its cDNA sequence shares 35-41% identical amino acids with PI synthases from Saccharomyces cerevisiae and mammals. AtPIS1 functionally complements a mutant of S. cerevisiae with a lesion in PI synthase, and recombinant AtPIS1 protein present in yeast membranes strongly depends on the two principal substrates, myo-inositol and CDP-DG, and requires Mg2+ ions for full activity.


Subject(s)
Arabidopsis/genetics , Saccharomyces cerevisiae/genetics , Transferases (Other Substituted Phosphate Groups)/genetics , Amino Acid Sequence , Arabidopsis/enzymology , Arabidopsis Proteins , Blotting, Northern , CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase , Cloning, Molecular , DNA, Complementary/chemistry , DNA, Complementary/genetics , Gene Expression Regulation, Enzymologic , Gene Expression Regulation, Plant , Genetic Complementation Test , Membrane Proteins , Molecular Sequence Data , Mutation , RNA, Plant/genetics , RNA, Plant/metabolism , Saccharomyces cerevisiae/enzymology , Sequence Alignment , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Tissue Distribution
5.
J Int Med Res ; 28(6): 313-7, 2000.
Article in English | MEDLINE | ID: mdl-11191725

ABSTRACT

Blood fibrinogen concentrations and glutamic-pyruvic transaminase activities of 66 adult cancer inpatients (aged 22 - 70 years) were determined both before and after one or two chemotherapy regimens. The percentage of hepatoma patients with abnormal blood fibrinogen levels (< 1.5 or > 6.0 g/l) was higher (64.3% of 14 patients) than that in other cancer categories (19.2% of 52 patients). The mean blood fibrinogen concentrations of male (3.5 g/l) and female (4.5 g/l) cancer patients were higher than those previously reported for healthy humans (2.8 and 2.9 g/l, respectively). After chemotherapy, blood fibrinogen concentrations decreased in patients whose primary tumours were surgically removed (from 4.8 to 3.2 g/l) but increased (from 3.0 to 4.8 g/l) in those who did not undergo surgery. Glutamic-pyruvic transaminase activities did not appear to be related to blood fibrinogen levels. We conclude that the increase in mean blood fibrinogen levels of cancer patients is probably related to tumour growth. Different mechanisms may operate in patients with hepatoma.


Subject(s)
Antineoplastic Agents/therapeutic use , Fibrinogen/metabolism , Neoplasms/blood , Neoplasms/drug therapy , Adolescent , Adult , Case-Control Studies , Female , Humans , Male , Middle Aged , Neoplasms/surgery
6.
J Biol Chem ; 274(9): 5738-45, 1999 Feb 26.
Article in English | MEDLINE | ID: mdl-10026194

ABSTRACT

Phosphatidylinositol metabolism plays a central role in signaling pathways in animals and is also believed to be of importance in signal transduction in higher plants. We report here the molecular cloning of a cDNA encoding a previously unidentified 126-kDa phosphatidylinositol (PI) 4-kinase (AtPI4Kbeta) from the higher plant Arabidopsis thaliana. The novel protein possesses the conserved domains present in animal and yeast PI 4-kinases, namely a lipid kinase unique domain and a catalytic domain. An additional domain, approximately 300 amino acids long, containing a high percentage (46%) of charged amino acids is specific to this plant enzyme. Recombinant AtPI4Kbeta expressed in baculovirus-infected insect (Spodoptera frugiperda) cells phosphorylated phosphatidylinositol exclusively at the D4 position of the inositol ring. Recombinant protein was maximally activated by 0.6% Triton X-100 but was inhibited by adenosine with an IC50 of approximately 200 microM. Wortmannin at a concentration of 10 microM inhibited AtPI4Kbeta activity by approximately 90%. AtPI4Kbeta transcript levels were similar in all tissues analyzed. Light or treatment with hormones or salts did not change AtPI4Kbeta transcript levels to a great extent, indicating constitutive expression of the AtPI4Kbeta gene.


Subject(s)
1-Phosphatidylinositol 4-Kinase/genetics , Arabidopsis/enzymology , 1-Phosphatidylinositol 4-Kinase/metabolism , Amino Acid Sequence , Animals , Baculoviridae/genetics , Base Sequence , Blotting, Northern , Cloning, Molecular , DNA, Complementary , Molecular Sequence Data , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sequence Homology, Amino Acid , Spodoptera
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