Thesis (M. Phil.)--University of Hong Kong, 2010. / Includes bibliographical references (leaves 157-161). Also available in print.

Thesis (M.Sc.)--York University, 2005. Graduate Programme in Biology. / Typescript. Includes bibliographical references (leaves 56-62). Also available on the Internet. MODE OF ACCESS via web browser by entering the following URL: http://gateway.proquest.com/openurl?url%5Fver=Z39.88-2004&res%5Fdat=xri:pqdiss &rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:MR11827

Submitted in part fulfillment for the Degree of Master of Technology: Biotechnology, Durban Institute of Technology, 2003. / Evidence suggests that the induction of tissue kallikrein, and the subsequently formed kinins, enhances proliferation of tumour cells because of their mitogenic property. Additionally, the kinin peptides are believed to promote the invasion of normal tissue by tumour cells. TGF-l is a potent inhibitor of the growth of renal epithelial cells, and is a classical anti-mitogen, which is central to many of its antiproliferative effects. No studies thus far have been performed, as to whether the proposed anti-mitogenesis ofTGF-1 has a regulatory effect on the cell proliferative action of kinins on renal epithelial and carcinoma cells. / M

No description available.

The human pancreatic cancer cell line T3M4, is known to produce transforming growth factor-alpha (TGF-alpha); as well as overexpress the receptor for this ligand, epidermal growth factor (EGF) receptor. TGF-alpha messenger RNA (mRNA) levels were assayed using northern blot, after addition of epidermal growth factor or TGF-alpha. The level of TGF-alpha mRNA was found to increase 2-fold at 2 hours and then return to near basal levels at 10 hours, after treatment with either ligand. Both ligands were also equipotent in a 2 hour dose response assay, with half maximal stimulation seen at 1 nM and maximal stimulation reached at 4 nM. Furthermore, there appeared to be a 2-fold increase in TGF-alpha transcription as determined by nuclear runoff experiments. Induction of TGF-alpha mRNA coupled with the overexpression of the EGF receptor, may result in a potent autocrine cycle; which may be found in other cancers.

published_or_final_version / abstract / Obstetrics and Gynaecology / Master / Master of Philosophy

published_or_final_version / Paediatrics and Adolescent Medicine / Doctoral / Doctor of Philosophy

published_or_final_version / Medicine / Doctoral / Doctor of Philosophy

The purpose of these studies was to determine whether lactogen-dependent Nb2-11c cells and lactogen-independent Nb2-SP cells differ with respect to morphology and autocrine growth control. To this end, the ultrastructural and surface morphology of both Nb2 cell lines was analyzed and the autocrine growth modulatory activity of Nb2 cell conditioned medium (Nb2-CM) was determined. The autocrine growth inhibitory activity of Nb2-CM was biologically characterized and attempts were made to biochemically characterize and purify the Nb2 cell autocrine growth inhibitor as well as to determine its mechanism of action. Quantitative analysis of transmission electron micrographs reveals that the ultrastructural morphology of lactogen-dependent Nb2-11c cells differs from that of lactogen-independent Nb2-SP cells. Nb2-11c cells exhibit a greater incidence and volume density of nuclear pockets, whereas the incidence and volume density of lipid droplets is greater in the Nb2-SP cell line. Surface feature of Nb2-11c and Nb2-SP cells, as examined with scanning electron microscopy, and indistinguishable. Nb2-11c and Nb2-SP cells share a common mode of growth control in the form of constitutive secretion of an autocrine inhibitory factor. Medium conditioned by either Nb2-11c or Nb2-SP cells inhibits the growth of both cell lines. Nb2-CM-mediated growth inhibition is dose-dependent and reversible. Nb2-CM does not induce quiescence or cell death, but rather, causes a delay in the progression of cells through all phases of the cell cycle. Nb2 cell proliferation stimulated by a variety of mitogens is inhibited by Nb2-CM. Nb2-CM also has the ability to inhibit the growth of normal rat splenocytes as well as MCF-7 human breast cancer cells. Biochemical analysis of Nb2-CM was equivocal; however, indirect evidence suggests that the autocrine growth inhibitory factor produced by Nb2 cells may be a prostaglandin or another arachadonic acid metabolite since the growth inhibitory activity of Nb2-CM is reduced when CM is prepared in the presence of indomethacin. Interestingly, levels of prostaglandin F₁(α) are elevated in CM-treated culture supernatants. Examination of other signal transduction systems in Nb2 cells suggests that neither cAMP activation, polyamine biosynthesis, nor protein kinase C activation mediate or influence the inhibitory effect of Nb2-CM.

Zhang, Chaoxiong. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2010. / Includes bibliographical references (leaves 115-132). / Abstracts in English and Chinese. / Chapter I --- Title page --- p.i / Chapter II --- Thesis committee --- p.ii / Chapter III --- Abstract --- p.iii / Chapter IV --- Abstract (Chinese version) --- p.v / Chapter V --- Acknowledgement --- p.vii / Chapter VI --- Table of content --- p.viii / Chapter VII --- List of figure --- p.xiii / Chapter Chapter 1 --- General introduction --- p.1 / Chapter Chapter 2 --- Literature review --- p.7 / Chapter 2.1 --- An introduction to myostatin --- p.8 / Chapter 2.1.1 --- A general introduction --- p.8 / Chapter 2.1.2 --- Myostatin identification --- p.9 / Chapter 2.1.3 --- Structural studies of myostatin --- p.10 / Chapter 2.1.4 --- Phenotype of myostatin-null animals or transgenic animal --- p.10 / Chapter 2.2 --- Regulation of myostatin --- p.12 / Chapter 2.2.1 --- Biosynthesis of myostatin --- p.12 / Chapter 2.2.2 --- Regulation of myostatin expression --- p.13 / Chapter 2.2.3 --- Regulation of myostatin protein --- p.16 / Chapter 2.3 --- Myostatin effect --- p.20 / Chapter 2.3.1 --- Myostatin Signaling Pathway --- p.20 / Chapter 2.3.2 --- Cellular Responses to Myostatin Signaling --- p.23 / Chapter 2.4 --- Possible functions in tissues other than muscle --- p.26 / Chapter 2.5 --- Myostatin in fishes --- p.27 / Chapter 2.5.1 --- Introduction of silver sea bream --- p.27 / Chapter 2.5.2 --- Studies carried out in fishes --- p.27 / Chapter 2.5.3 --- Possible novel functions of myostatin in fishes --- p.30 / Chapter Chapter 3 --- Characterization of myostatin gene in the silver seabream (Sparus sarba) --- p.31 / Chapter 3.1 --- Abstract --- p.32 / Chapter 3.2 --- Introduction --- p.33 / Chapter 3.3 --- Materials and methods --- p.35 / Chapter 3.3.1 --- Experimental fish --- p.35 / Chapter 3.3.2 --- Total RNA extraction and cDNA cloning of myostatin-1 and myostatin-2 in silver sea bream --- p.35 / Chapter 3.3.3 --- Multiple sequence alignment --- p.38 / Chapter 3.3.4 --- Real-time PCR for quantification of myostatin-1 and myostatin-2 mRNA expression --- p.38 / Chapter 3.3.5 --- 1 --- p.39 / Chapter 3.3.6 --- Data processing and statistical analysis --- p.40 / Chapter 3.4 --- Results --- p.40 / Chapter 3.4.1 --- Cloning of myostatin-l and myostatin-2 cDNA --- p.40 / Chapter 3.4.2 --- Myostatin tissue distribution and seasonal pattern --- p.42 / Chapter 3.5 --- Discussion --- p.55 / Chapter Chapter 4 --- "Effects of growth hormone, 11-ketotestosterone and cortisol on myostatin mRNA expression in silver sea bream (Sparus sarba)" --- p.61 / Chapter 4.1 --- Abstract --- p.62 / Chapter 4.2 --- Introduction --- p.63 / Chapter 4.3 --- Materials and methods --- p.65 / Chapter 4.3.1 --- Experimental fish --- p.65 / Chapter 4.3.2 --- Growth hormone injection --- p.65 / Chapter 4.3.3 --- 11-ketotestosterone and cortisol injection --- p.66 / Chapter 4.3.4 --- Muscle explants culture and hormone exposure --- p.67 / Chapter 4.3.5 --- Primary pituitary cell culture and cortisol exposure --- p.68 / Chapter 4.3.6 --- Measurement of growth hormone secretion by ELISA --- p.69 / Chapter 4.3.7 --- Data processing and statistical analysis --- p.70 / Chapter 4.4 --- Results --- p.71 / Chapter 4.4.1 --- Growth hormone injection --- p.71 / Chapter 4.4.2 --- 11-ketotestosterone injection --- p.71 / Chapter 4.4.3 --- Cortisol injection --- p.71 / Chapter 4.4.4 --- "In vitro hormone treatment-growth hormone, 11-ketotestosterone and cortisol" --- p.72 / Chapter 4.4.5 --- Pituitary cell growth hormone secretion under cortisol treatment --- p.72 / Chapter 4.5 --- Discussion --- p.81 / Chapter Chapter 5 --- Expression of myostatin mRNA in silver sea bream in different salinity --- p.87 / Chapter 5.1 --- Abstract --- p.88 / Chapter 5.2 --- Introduction --- p.89 / Chapter 5.3 --- Materials and Methods --- p.91 / Chapter 5.3.1 --- Experimental fish --- p.92 / Chapter 5.3.2 --- Long term salinity adaptation --- p.92 / Chapter 5.3.3 --- Abrupt transfer form seawater to freshwater --- p.92 / Chapter 5.3.4 --- Data processing and statistical analysis --- p.93 / Chapter 5.4 --- Results --- p.93 / Chapter 5.4.1 --- Long term adaptation to different salinities --- p.93 / Chapter 5.4.2 --- Abrupt transfer from 33ppt to 6ppt - 24 h --- p.93 / Chapter 5.4.3 --- Abrupt transfer from 33ppt to 6ppt - 72 h --- p.94 / Chapter 5.5 --- Discussion --- p.104 / Chapter Chapter 6 --- General discussion and conclusion --- p.108 / References --- p.115