The purpose of this study was to establish an exercise protocol that demonstrated a relationship between rest-interval duration and the exercise induced human growth hormone (hGH) response. Ten recreationally trained male subjects (23 ± 0.9 yrs) performed three leg extension trials on an Eagle — Cybex leg extension machine that consisted of 4 sets of 10 repetitions. The workload and volume was kept constant, but each trial had different rest-interval durations. Rest-interval durations between sets were at: 30 sec intervals (T-30), 60 sec intervals (T-60), or 120 sec intervals (T-120). Blood samples were obtained pre- and 0 — 30 minutes post-exercise and analyzed for lactate and hGH. All blood lactates rose significantly above baseline after exercise, with no differences in time of occurrence between trials. Blood lactates were significantly greater after the T-30 trials, compared to that of the T-60 and T-120 trials. There was no significant difference in hGH concentrations between trials. However, the data did suggest a relationship between rest-interval duration and the variability of hGH responses. The T-30 trials yielded significantly greater variation in hGH concentrations than the T-120 trials, and the T-120 trials showed significantly less variation than both the T-30 and T-60 trials. Although significant differences were found in these variations between trials, they did not prevent any significant differences in concentrations between trials from being found. In summary, the results of this study demonstrated an exercise related increase in lactic acid that had an inverse relationship to the length of the rest-intervals. hGH data on the other hand, did not show a relationship between rest-interval duration and the hGH concentrations. The connection between rest-interval duration and variability of hGH responses could possibly suggest that hGH values may have been significantly different if an exercise protocol higher in volume were utilized. Additionally, the results indicate that there is no direct relationship between blood lactate and hGH concentrations, as others have suggested. / School of Physical Education, Sport, and Exercise Science

Finally, the isolation and cloning of black sea bream SL receptor using PCR cloning and protein pull down assay were also attempted. Based on the PCR cloning results, the phylogenetic analysis of nonsalmonids fish GHR1 and SLR protein sequence, the GHR1 data of tissue distribution and effects of environmental salinity and fasting in tilapia, along with the results of far western blot, black sea bream GHR1 is probably a receptor for SL, however there is also a SL specific receptor in black sea bream. / In hormone treated primary cell culture of nonspawning black sea bream pituitary, 10-8 M E2 significantly increases SL mRNA level but 10-10 M, 10-9 M, 10-8 M of E2 inhibit GH mRNA level in female black seabream; 10-8 M E2 also inhibits SL and GH mRNA expression in bisexual black sea bream; 10-8 M MT inhibits SL mRNA expression in male black sea bream but any concentration of MT detected shows no significant effect on GH mRNA level. / Key words. somatolactin (SL), monthly changes, SL promoter, pit-1 and SL receptor / Somatolactin, SL, is a novel member of GH family of pituitary hormone only found in fish. It is considered to be a member of the GH gene family after gene duplication. Two types of SL, SL alpha and SL beta were identified, and SL 13 seems only in fresh water fish, such as goldfish, catfish, rainbow trout, eel and zebrafish. Black sea bream is a marine fish, and there is only SL alpha found from sequencing of over 100 SL cDNA clones. / The cDNAs encoding for transcription factor pit-1 variants were cloned and the transactivation of these Pit-1 isoforms on SL gene promoter were studied. Three variants of Pit-1 are first identified in fish. Pit-1b and Pit-1c can enhance SL promoter activity in Hepa-T1 cells respectively to about 2 fold and 12 fold, but pit-1a failed to activate the SL gene it in the same cells. All the three pit-1s of black sea bream couldn't reverse the inhibition of SL promoter in GH3 cells. The data suggest that N terminal 60 amino acid residues are critical in transactiation on SL promoter and SL promoter activity is possibly limited to fish SL secreting cells. / The SL gene promoter was obtained for gene regulation studies aiming to search for possible regulatory elements controlling the transcription of SL gene in black seabream. SL gene promoter is active in HepaT1 cells, but is inhibited in GH3 cells. Seven putative pit-1 response elements were confirmed with EMSA and super shift assay. / To study the physiological function of SL in black seabream, we initiated a study of monthly expressions of SL mRNA and gonadal somatic index (GSI) to determine whether SL is related to reproduction in black seabream, with GH mRNA levels were also detected for comparison. The results imply that function of SL is possibly related to early development of testis, while GH probably plays some roles in testis and ovary maturation. / by Tian, Jing. / "October 2007." / Source: Dissertation Abstracts International, Volume: 69-08, Section: B, page: 4574. / Thesis (Ph.D.)--Chinese University of Hong Kong, 2007. / Includes bibliographical references (p. 156-170). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Electronic reproduction. [Ann Arbor, MI] : ProQuest Information and Learning, [200-] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Abstracts in English and Chinese. / School code: 1307.

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Hui Fong Fong Liza. / Thesis submitted in: December 2002. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2003. / Includes bibliographical references (leaves 130-182). / Abstracts in English and Chinese. / Chapter I --- Title page --- p.I / Chapter II --- Thesis committee --- p.II / Chapter III --- Acknowledgements --- p.III / Chapter IV --- Abstract (Chinese version) --- p.IV / Chapter V --- Abstract (English version) --- p.VII / Chapter VI --- Table of contents --- p.X / Chapter VII --- List of figures --- p.XIV / Chapter VIII --- List of table --- p.XVIII / Chapter Chapter 1: --- General introduction --- p.1 / Chapter Chapter 2: --- Literature review --- p.5 / Chapter 2.1. --- Gill --- p.5 / Chapter 2.2. --- Chloride cells (Mitochondria-rich cells) --- p.6 / Chapter 2.2.1. --- Ion extrusion by fish in seawater --- p.9 / Chapter 2.2.2. --- Ion uptake by fish in hypo-osmotic condition --- p.12 / Chapter 2.3. --- Sparus sarba (Silver seabream) --- p.14 / Chapter 2.4. --- Sodium-potassium adenosinetriphosphatase (Na+-K+-ATPase) --- p.15 / Chapter 2.4.1. --- Na+-K+-ATPase α-subunit --- p.17 / Chapter 2.4.2. --- Na+-K+-ATPase β-subunit --- p.18 / Chapter 2.4.3. --- Regulation of Na+-K+-ATPase --- p.20 / Chapter 2.5. --- Hormones --- p.21 / Chapter 2.5.1. --- Growth hormone-prolactin family --- p.21 / Chapter 2.5.2. --- Structure of hormones --- p.22 / Chapter 2.5.2.1. --- Structure of growth hormone and prolactin in fish --- p.22 / Chapter 2.5.2.2. --- Structure of insulin-like growth factors in fish --- p.26 / Chapter 2.5.2.3. --- Structure of Cortisol in fish --- p.27 / Chapter 2.5.3. --- Regulation of hormones --- p.28 / Chapter 2.5.3.1. --- Regulation of growth hormone in fish --- p.28 / Chapter 2.5.3.2. --- Regulation of prolactin in fish --- p.32 / Chapter 2.5.3.3. --- Regulation of insulin-like growth factor-I in fish --- p.33 / Chapter 2.5.3.4. --- Regulation of Cortisol in fish --- p.33 / Chapter 2.5.4. --- Functions of hormones --- p.33 / Chapter 2.5.4.1. --- Functions of growth hormone in fish --- p.33 / Chapter 2.5.4.2. --- Functions of prolactin in fish --- p.39 / Chapter 2.5.4.3. --- Functions of insulin-like growth factor-I in fish --- p.44 / Chapter 2.5.4.4. --- Functions of Cortisol in fish --- p.45 / Chapter 2.5.4.5. --- "Combined effects of GH, IGF-I, PRL and Cortisol" --- p.49 / Chapter 2.6. --- Salinity effects on Na+-K+-ATPase expression --- p.52 / Chapter Chapter 3: --- In vitro effect of hormones on branchial Na+-K+- ATPase expression in marine teleost Sparus sarba --- p.58 / Chapter 3.1. --- Abstract --- p.58 / Chapter 3.2. --- Introduction --- p.60 / Chapter 3.3. --- Materials and methods --- p.62 / Chapter 3.3.1. --- Overall experimental design --- p.62 / Chapter 3.3.2. --- Fish preparation --- p.62 / Chapter 3.3.3. --- Tissue sampling --- p.62 / Chapter 3.3.4. --- RNA extraction and dot blot analysis --- p.63 / Chapter 3.3.5. --- Protein extraction --- p.65 / Chapter 3.3.6. --- Protein quantification --- p.65 / Chapter 3.3.7. --- Na+-K+-ATPase activity --- p.65 / Chapter 3.3.8. --- Protein gel electrophoresis and immunoblotting (Western blotting) --- p.66 / Chapter 3.3.9. --- Statistical analysis --- p.67 / Chapter 3.4. --- Results --- p.69 / Chapter 3.4.1. --- Dot blot analysis of Na+-K+-ATPase mRNA subunits --- p.69 / Chapter 3.4.2. --- Analysis of Na+-K+-ATPase protein α-subunit --- p.81 / Chapter 3.4.3. --- Analysis of Na+-K+-ATPase activity --- p.87 / Chapter 3.5. --- Discussion --- p.92 / Chapter 3.5.1. --- Effects of rbGH and rbIGF-I on Na+-K+-ATPase expression --- p.92 / Chapter 3.5.2. --- Effects of oPRL on Na+-K+-ATPase expression --- p.102 / Chapter 3.5.3 --- Effects of Cortisol on Na+-K+-ATPase expression --- p.104 / Chapter 3.6. --- Conclusion --- p.108 / Chapter Chapter 4: --- In vivo effect of salinity on branchial Na+-K+-ATPase expression in marine teleost Sparus sarba --- p.109 / Chapter 4.1. --- Abstract --- p.109 / Chapter 4.2. --- Introduction --- p.110 / Chapter 4.3. --- Materials and methods --- p.112 / Chapter 4.3.1. --- Overall experimental design --- p.112 / Chapter 4.3.2. --- Fish preparation --- p.112 / Chapter 4.3.3. --- Tissue sampling --- p.113 / Chapter 4.3.4. --- "RNA extraction, dot blot analysis, protein extraction, quantification, Na+-K+-ATPase activity, protein gel electrophoresis and immunoblotting (Western blotting)" --- p.113 / Chapter 4.3.5. --- Statistical analysis --- p.114 / Chapter 4.4. --- Results --- p.114 / Chapter 4.4.1. --- Dot blot analysis of Na+-K+-ATPase mRNA subunits --- p.114 / Chapter 4.4.2. --- Analysis of Na+-K+-ATPase protein a-subunit --- p.114 / Chapter 4.4.3. --- Analysis of Na+-K+-ATPase activity --- p.115 / Chapter 4.5. --- Discussion --- p.120 / Chapter 4.6. --- Conclusion --- p.125 / Chapter Chapter 5: --- General discussion and conclusion --- p.126 / References --- p.130

Fung Chun Kit. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2005. / Includes bibliographical references (leaves 117-139). / Abstracts in English and Chinese. / Declaration of Originality --- p.i / Acknowledgements --- p.ii / Abstract --- p.iii / 摘要 --- p.v / List of figures --- p.vi / List of tables --- p.viii / List of abbreviations --- p.ix / Chapter Chapter I --- General introduction --- p.1 / Chapter 1.1 --- Different fish habitats with various salinities --- p.1 / Chapter 1.2 --- Osmotic challenges faced by teleosts --- p.2 / Chapter 1.3 --- High ionic strength results in DNA damage and excess water gain --- p.3 / Chapter 1.4 --- Osmoregulatory organs and mechanisms for osmotic balance --- p.4 / Chapter 1.5 --- Different tolerance to salinity changes --- p.8 / Chapter 1.6 --- Effective communication among osmoregulatory organs --- p.9 / Chapter 1.7 --- Introduction to GH and PRL --- p.9 / Chapter 1.8 --- Structure of the GHR and PRLR --- p.10 / Chapter 1.9 --- Hypoosmoregulatory action of GH/IGF-I axis in teleosts --- p.11 / Chapter 1.10 --- Hyperosmoregulatory action of PRL in teleosts --- p.11 / Chapter Chapter II --- Research rationale --- p.13 / Chapter 2.1 --- Physiological importance of osmoregulation in fish --- p.13 / Chapter 2.1.1 --- Energy metabolism --- p.13 / Chapter 2.1.2 --- Growth --- p.14 / Chapter 2.1.3 --- Immunity --- p.14 / Chapter 2.1.4 --- Reproduction --- p.15 / Chapter 2.2 --- Aquaculture importance --- p.15 / Chapter 2.3 --- Unknown molecular regulatory mechanism of hormones during salinity changes in fish --- p.16 / Chapter 2.4 --- Animal model --- p.17 / Chapter Chapter III --- In vivo studies of sbGHR and sbPRLR expression in osmoregulatory organs in response to salinity changes --- p.18 / Chapter 3.1 --- Introduction --- p.18 / Chapter 3.1.1 --- Dynamic change of GH level during salinity changes --- p.18 / Chapter 3.1.2 --- Dynamic change of PRL level during salinity changes --- p.19 / Chapter 3.1.3 --- In vitro studies of GH and PRL release from teleost pituitary in response to extracellular osmolality changes --- p.20 / Chapter 3.1.4 --- Biological actions of GH and PRL through the GHR and PRLR --- p.21 / Chapter 3.2 --- Materials and methods --- p.23 / Chapter 3.3 --- Results --- p.28 / Chapter 3.4 --- Discussion --- p.36 / Chapter 3.4.1 --- Plasma osmolality change during salinity changes --- p.36 / Chapter 3.4.2 --- Gene expression after HSW exposure --- p.38 / Chapter 3.4.3 --- Ionic mediators of the gene expression --- p.43 / Chapter 3.4.4 --- Gene expression after BW exposure --- p.44 / Chapter 3.4.5 --- Dynamic changes of the GHR and PRLR in response to salinity changes --- p.45 / Chapter 3.4.6 --- Regulation of the gene expression in response to salinity changes --- p.46 / Chapter Chapter IV --- Gene expression of sbGHR in liver during salinity changes --- p.49 / Chapter 4.1 --- Introduction --- p.49 / Chapter 4.1.1 --- Responses of the somatotropic axis to salinity changes in fish --- p.49 / Chapter 4.2 --- Materials and methods --- p.52 / Chapter 4.3 --- Results --- p.56 / Chapter 4.4 --- Discussion --- p.60 / Chapter 4.4.1 --- Inhibition of GHR and IGF-I gene expression in liver during HSW exposure --- p.60 / Chapter 4.4.2 --- Downregulation of GHR gene expression by hyperosmotic stress --- p.62 / Chapter 4.4.3 --- Growth retardation of fish during hyperosmotic environment --- p.64 / Chapter Chapter V --- Gene expression studies of sbPRLR in gill organ culture --- p.68 / Chapter 5.1 --- Introduction --- p.68 / Chapter 5.1.1 --- Functions of gill in fish osmoregulation --- p.68 / Chapter 5.1.2 --- Gill culture as a model for osmoregulation studies --- p.69 / Chapter 5.2 --- Materials and methods --- p.70 / Chapter 5.3 --- Results --- p.71 / Chapter 5.4 --- Discussion --- p.73 / Chapter Chapter VI --- Regulation of gene expression of sbGHR in liver during hyperosmotic stress: promoter studies --- p.75 / Chapter 6.1 --- Introduction --- p.75 / Chapter 6.1.1 --- What is a promoter? --- p.75 / Chapter 6.1.2 --- Promoter studies of GHR gene --- p.76 / Chapter 6.2 --- Materials and methods --- p.78 / Chapter 6.3 --- Results --- p.85 / Chapter 6.4 --- Discussion --- p.104 / Chapter Chapter VII --- General discussion and future perspectives --- p.111 / References --- p.117

Ng Ho Yuen Andus. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2001. / Includes bibliographical references (leaves 105-131). / Abstracts in English and Chinese. / Chapter I --- Title page --- p.i / Chapter II --- Thesis committee --- p.ii / Chapter III --- Acknowledgement --- p.iii / Chapter IV --- Abstract --- p.v / Chapter V --- Abstract (Chinese version) --- p.vii / Chapter V --- Table of contents --- p.ix / Chapter VI --- List of abbreviations --- p.xv / Chapter VII --- List of figures --- p.xviii / General introduction --- p.1 / Chapter Chapter 1: --- Literature review --- p.5 / Chapter 1.1. --- Heat shock proteins (HSPs) --- p.6 / Chapter 1.1.1. --- Introduction --- p.6 / Chapter 1.1.2. --- The various heat shock proteins --- p.8 / Chapter 1.1.2.1. --- HSP100s --- p.8 / Chapter 1.1.2.2. --- HSP90s --- p.9 / Chapter 1.1.2.3. --- HSP70s --- p.12 / Chapter 1.1.2.3.1. --- ATPase reaction cycle of HSP70 and protein folding --- p.13 / Chapter 1.1.2.3.2. --- Protein translocation --- p.14 / Chapter 1.1.2.3.3. --- Selective lysosomal proteolysis --- p.16 / Chapter 1.1.2.4. --- HSP60s --- p.16 / Chapter 1.1.2.5. --- Small HSPs --- p.17 / Chapter 1.1.2.6. --- Ubiquitin --- p.19 / Chapter 1.1.3. --- HSP studies in fish --- p.21 / Chapter 1.1.3.1. --- In vivo works --- p.21 / Chapter 1.1.3.2. --- In vitro works --- p.23 / Chapter 1.2. --- Growth hormone / prolactin family in teleostean fishes --- p.26 / Chapter 1.2.1. --- Introduction --- p.26 / Chapter 1.2.2. --- Growth hormone (GH; somatotropin) --- p.29 / Chapter 1.2.2.1. --- Structure --- p.29 / Chapter 1.2.2.2. --- Actions --- p.29 / Chapter 1.2.2.3. --- Insulin-like Growth Factors (IGFs; somatomedins) --- p.31 / Chapter 1.2.3. --- Prolactin (PRL) --- p.34 / Chapter 1.2.3.1. --- Structure --- p.34 / Chapter 1.2.3.2. --- Actions --- p.35 / Chapter 1.2.4. --- Somatolactin (SL) --- p.37 / Chapter 1.2.4.1. --- Structure --- p.37 / Chapter 1.2.4.2. --- Actions --- p.38 / Chapter 1.2.5. --- Growth hormone receptor (GH-R) and prolactin receptor (PRL-R) --- p.39 / Chapter 1.3. --- Cortisol in teleostean fishes --- p.41 / Chapter 1.4. --- Salinity adaptation in teleosts --- p.44 / Chapter Chapter 2: --- Effect of in vitro thermal shock on HSP70 expression in whole blood of Sparus sarba --- p.46 / Chapter 2.1. --- Introduction --- p.47 / Chapter 2.2. --- Materials and methods --- p.49 / Chapter 2.2.1. --- Overall experimental design --- p.49 / Chapter 2.2.2. --- Experimental fish --- p.49 / Chapter 2.2.3. --- Blood sampling and preparation --- p.49 / Chapter 2.2.4. --- Thermal stress regimes --- p.50 / Chapter 2.2.5. --- Protein extraction --- p.51 / Chapter 2.2.6. --- Protein quantification --- p.51 / Chapter 2.2.7. --- Indirect enzyme-linked immunosorbent assay (ELISA) --- p.52 / Chapter 2.2.8. --- Protein gel electrophoresis and immunoblotting (Western blotting) --- p.54 / Chapter 2.2.9. --- Statistical analysis --- p.55 / Chapter 2.3. --- Results --- p.56 / Chapter 2.3.1. --- Validation of indirect ELISA --- p.56 / Chapter 2.3.2. --- Effect of in vitro thermal shock on HSP70 expression in whole blood of Sparus sarba --- p.56 / Chapter 2.4. --- Discussion --- p.60 / Chapter 2.5. --- Conclusion --- p.64 / Chapter Chapter 3: --- Effects of hormones on HSP70 expression in whole blood of Sparus sarba in vitro --- p.65 / Chapter 3.1. --- Introduction --- p.66 / Chapter 3.2. --- Materials and methods --- p.68 / Chapter 3.2.1. --- Overall experimental design and experimental fish --- p.68 / Chapter 3.2.2. --- Hormone treatments --- p.59 / Chapter 3.2.3. --- "Protein extraction and quantification, indirect ELISA，gel electrophoresis, and immunoblotting (Western blotting)" --- p.70 / Chapter 3.2.4. --- Statistical analysis --- p.70 / Chapter 3.3. --- Results --- p.71 / Chapter 3.3.1. --- Effect of Cortisol on HSP70 levels in whole Blood --- p.71 / Chapter 3.3.2. --- Effect of recombinant bream growth hormone on HSP70 levels in whole blood --- p.71 / Chapter 3.3.3. --- Effect of recombinant bream insulin-like growth factor-I on HSP70 levels in whole blood --- p.71 / Chapter 3.3.4. --- Effect of ovine prolactin on HSP70 levels in whole blood --- p.72 / Chapter 3.4. --- Discussion --- p.81 / Chapter 3.4.1. --- Effect of Cortisol on HSP70 levels in whole Blood --- p.81 / Chapter 3.4.2. --- Effect of recombinant bream growth hormone on HSP70 levels in whole blood --- p.83 / Chapter 3.4.3. --- Effect of recombinant bream insulin-like growth factor-I on HSP70 levels in whole blood --- p.85 / Chapter 3.4.4. --- Effect of ovine prolactin on HSP70 levels in whole blood --- p.86 / Chapter 3.5. --- Conclusion --- p.88 / Chapter Chapter 4: --- Effect on HSP70 expression in whole blood of Sparus sarba acclimated to various salinities --- p.89 / Chapter 4.1. --- Introduction --- p.90 / Chapter 4.2. --- Materials and methods --- p.92 / Chapter 4.2.1. --- Overall experimental design and experimental fish --- p.92 / Chapter 4.2.2. --- "Protein extraction and quantification, indirect ELISA, gel electrophoresis, and immunoblotting (Western blotting)" --- p.92 / Chapter 4.2.3. --- Statistical analysis --- p.93 / Chapter 4.3. --- Results --- p.94 / Chapter 4.4. --- Discussion --- p.97 / Chapter 4.5. --- Conclusion --- p.100 / Chapter Chapter 5: --- General discussion and conclusion --- p.101 / References --- p.105