Resistance exercise stress: theoretical mechanisms for growth hormone processing and release from the anterior pituitary somatotroph.

Heavy resistance exercise (HRE) is the most effective method for inducing muscular hypertrophy and stimulating anabolic hormones, including growth hormone, into the blood. In this review, we explore possible mechanisms within the GH secretory pathway of the pituitary somatotroph, which are likely to modulate the flow of hormone synthesis and packaging as it is processed prior to exocytosis. Special emphasis is placed on the secretory granule and its possible role as a signaling hub. We also review data that summarize how HRE affects the quality and quantity of the secreted hormone. Finally, these pathway mechanisms are considered in the context of heterogeneity of the somatotroph population in the anterior pituitary.

Hormonal stress responses of growth hormone and insulin-like growth factor-I in highly resistance trained women and men.

The purpose of this study was to examine the responses of growth hormone (GH) and insulin-like growth factor-I (IGFI) to intense heavy resistance exercise in highly trained men and women to determine what sex-dependent responses may exist. Subjects were highly resistance trained men (N = 8, Mean ± SD; age, yrs., 21 ± 1, height, cm, 175.3 ± 6.7, body mass, kg, 87.0 ± 18.5, % body fat, 15.2 ± 5.4, squat X body mass, 2.1 ± 0.4; and women (N = 7; Mean ± SD, age, yrs. 24 ± 5, height, cm 164.6 ± 6.7, body mass, kg 76.4 ± 8.8, % body fat, 26.9 ± 5.3, squat X body mass, 1.7 ± 0.6). An acute resistance exercise test protocol (ARET) consisted of 6 sets of 10 repetitions at 80% of the 1 RM with 2 min rest between sets was used as the stressor. Blood samples were obtained pre-exercise, after 3 sets, and then immediately after exercise (IP), 5, 15, 30, and 70 min post-exercise for determination of blood lactate (HLa), and plasma glucose, insulin, cortisol, and GH. Determination of plasma concentrations of IGFI, IGF binding proteins 1, 2, and 3 along with molecular weight isoform factions were determined at pre, IP and 70 min. GH significantly (P ≤ 0.05) increased at all time points with resting concentrations significantly higher in women. Significant increases were observed for HLa, glucose, insulin, and cortisol with exercise and into recovery with no sex-dependent observations. Women showed IGF-I values that were higher than men at all times points with both seeing exercise increases. IGFBP-1 and 2 showed increase with exercise with no sex-dependent differences. IGFBP-3 concentrations were higher in women at all-time points with no exercise induced changes. Both women and men saw an exercise induced increase with significantly higher values in GH in only the mid-range (30-60 kD) isoform.  Only women saw an exercise induced increase with significantly higher values for IGF fractions only in the mid-range (30-60 kD) isoform, which were significantly greater than the men at the IP and 70 min post-exercise time points. In conclusion, the salient findings of this investigation were that in highly resistance trained men and women, sexual dimorphisms exist but appear different from our prior work in untrained men and women and appear to support a sexual dimorphism related to compensatory aspects in women for anabolic mediating mechanisms in cellular interactions.

Recovery using "float" from high intensity stress on growth hormone-like molecules in resistance trained men.

OBJECTIVE: The purpose of this study was to examine the influence of a novel "floatation-restricted environmental stimulation therapy" (floatation-REST) on growth hormone responses to an intense resistance exercise stress. DESIGN: Nine resistance trained men (age: 23.4 ±â€¯2.5 yrs.; height: 175.3 ±â€¯5.4 cm; body mass: 85.3 ±â€¯7.9 kg) completed a balanced, crossover-controlled study design with two identical exercise trials, differing only in post-exercise recovery intervention (i.e., control or floatation-REST). A two-week washout period was used between experimental conditions. Plasma lactate was measured pre-exercise, immediately post-exercise and after the 1 h. recovery interventions. Plasma iGH was measured pre-exercise, immediately-post exercise, and after the recovery intervention, as well as 24 h and 48 h after the exercise test. The bGH-L was measured only at pre-exercise and following each recovery intervention. RESULTS: For both experimental conditions, a significant (P ≤ 0.05) increase in lactate concentrations were observed immediately post-exercise (~14 mmol • L-1) and remained slightly elevated after the recovery condition. The same pattern of responses was observed for iGH with no differences from resting values at 24 and 48 h of recovery. The bGH-L showed no exercise-induced changes following recovery with either treatment condition, however concentration values were dramatically lower than ever reported. CONCLUSION: The use of floatation-REST therapy immediately following intense resistance exercise does not appear to influence anterior pituitary function in highly resistance trained men. However, the lower values of bGH suggest dramatically different molecular processing mechanisms at work in this highly trained population.

Growth Hormone and Insulin-like Growth Factor-I Molecular Weight Isoform Responses to Resistance Exercise Are Sex-Dependent.

Purpose: To determine if acute resistance exercise-induced increases in growth hormone (GH) and insulin-like growth factor-I (IGF-I) were differentially responsive for one or more molecular weight (MW) isoforms and if these responses were sex-dependent. Methods: College-aged men (n = 10) and women (n = 10) performed an acute resistance exercise test (ARET; 6 sets, 10 repetition maximum (10-RM) squat, 2-min inter-set rest). Serum aliquots from blood drawn Pre-, Mid-, and Post-ARET (0, +15, and +30-min post) were processed using High Performance Liquid Chromatography (HPLC) fractionation and pooled into 3 MW fractions (Fr.A: >60; Fr.B: 30-60; Fr.C: <30 kDa). Results: We observed a hierarchy of serum protein collected among GH fractions across all time points independent of sex (Fr.C > Fr.A > Fr.B, p ≤ 0.03). Sex × time interactions indicated that women experienced earlier and augmented increases in all serum GH MW isoform fraction pools (p < 0.05); however, men demonstrated delayed and sustained GH elevations (p < 0.01) in all fractions through +30-min of recovery. Similarly, we observed a sex-independent hierarchy among IGF-I MW fraction pools (Fr.A > Fr.B > Fr.C, p ≤ 0.01). Furthermore, we observed increases in IGF-I Fr. A (ternary complexes) in men only (p ≤ 0.05), and increases in Fr.C (free/unbound IGF-I) in women only (p ≤ 0.05) vs. baseline, respectively. Conclusions: These data indicate that the processing of GH and IGF-I isoforms from the somatotrophs and hepatocytes are differential in their response to strenuous resistance exercise and reflect both temporal and sex-related differences.

Growth Hormone(s), Testosterone, Insulin-Like Growth Factors, and Cortisol: Roles and Integration for Cellular Development and Growth With Exercise.

Hormones are largely responsible for the integrated communication of several physiological systems responsible for modulating cellular growth and development. Although the specific hormonal influence must be considered within the context of the entire endocrine system and its relationship with other physiological systems, three key hormones are considered the "anabolic giants" in cellular growth and repair: testosterone, the growth hormone superfamily, and the insulin-like growth factor (IGF) superfamily. In addition to these anabolic hormones, glucocorticoids, mainly cortisol must also be considered because of their profound opposing influence on human skeletal muscle anabolism in many instances. This review presents emerging research on: (1) Testosterone signaling pathways, responses, and adaptations to resistance training; (2) Growth hormone: presents new complexity with exercise stress; (3) Current perspectives on IGF-I and physiological adaptations and complexity these hormones as related to training; and (4) Glucocorticoid roles in integrated communication for anabolic/catabolic signaling. Specifically, the review describes (1) Testosterone as the primary anabolic hormone, with an anabolic influence largely dictated primarily by genomic and possible non-genomic signaling, satellite cell activation, interaction with other anabolic signaling pathways, upregulation or downregulation of the androgen receptor, and potential roles in co-activators and transcriptional activity; (2) Differential influences of growth hormones depending on the "type" of the hormone being assayed and the magnitude of the physiological stress; (3) The exquisite regulation of IGF-1 by a family of binding proteins (IGFBPs 1-6), which can either stimulate or inhibit biological action depending on binding; and (4) Circadian patterning and newly discovered variants of glucocorticoid isoforms largely dictating glucocorticoid sensitivity and catabolic, muscle sparing, or pathological influence. The downstream integrated anabolic and catabolic mechanisms of these hormones not only affect the ability of skeletal muscle to generate force; they also have implications for pharmaceutical treatments, aging, and prevalent chronic conditions such as metabolic syndrome, insulin resistance, and hypertension. Thus, advances in our understanding of hormones that impact anabolic: catabolic processes have relevance for athletes and the general population, alike.

Bioactive growth hormone in humans: Controversies, complexities and concepts.

OBJECTIVE: To revisit a finding, first described in 1978, which documented existence of a pituitary growth factor that escaped detection by immunoassay, but which was active in the established rat tibia GH bioassay. METHODS: We present a narrative review of the evolution of growth hormone complexity, and its bio-detectability, from a historical perspective. RESULTS: In humans under the age of 60, physical training (i.e. aerobic endurance and resistance training) are stressors which preferentially stimulate release of bioactive GH (bGH) into the blood. Neuroanatomical studies indicate a) that nerve fibers directly innervate the human anterior pituitary and b) that hind limb muscle afferents, in both humans and rats, also modulate plasma bGH. In the pituitary gland itself, molecular variants of GH, somatotroph heterogeneity and cell plasticity all appear to play a role in regulation of this growth factor. CONCLUSION: This review considers more recent findings on this often forgotten/neglected subject. Comparison testing of a) human plasma samples, b) sub-populations of separated rat pituitary somatotrophs or c) purified human pituitary peptides by GH bioassay vs immunoassay consistently yield conflicting results.

Two types of rat pituitary somatotrophs secrete growth hormone with different biological and immunological profiles.

OBJECTIVE: Two stable subpopulations of somatotrophs reside in the rat pituitary gland. We tested the hypothesis that one produced growth hormone (GH) with greater activity when tested in the tibial line bioassay (BGH) than the other, while differences in the activities between the two groups would be less dramatic when measured by immunoassay (IGH). DESIGN: A series of studies using hypophysectomized rats, hollow fibers, treatments and culture models were used to differentiate differences in Type I and Type II anterior pituitary somatotrophs in both function and production of immunoactive and bioactive growth hormone. RESULTS: We found that dense, Type II somatotrophs (>1.070g·cm-3) differed markedly in their secretion patterns of IGH vs BGH in different In vitro and in vivo tests. In culture, Type II cells secreted five times as much BGH, and three fourths as much IGH as the less dense Type I cells. Production (storage and secretion) of BGH was 7-fold greater by Type II cells whereas IGH production was identical for the two cell types. Implantation of Type II cells into hypophysectomized rats significantly increased body weight, epiphyseal cartilage thickness, and muscle weight of the recipients; in contrast, Type I cells elicited only a small increase in body weight. Type I somatotrophs isolated from rats which had been previously fasted or insulin-treated subsequently showed only small, inconsistent changes in release relative to that from cells in the unfractionated cell population. However, release of BGH from the Type II cells was markedly decreased. CONCLUSION: Both IGH and BGH should be considered in the elucidation of GH physiology.

Bioactive growth hormone in older men and women: It's relationship to immune markers and healthspan.

OBJECTIVE: The consequences of age-related decline in the somatotropic axis of humans are complex and remain largely unresolved. We tested the hypothesis that hGH measurements of plasma by bioassay vs immunoassay from samples obtained from free-living, elderly individuals would reveal a dichotomy in GH activities that are correlated with the functional status of the donors, i.e. their healthspan. DESIGN: Forty-one men and women of advanced age (men: N=16, age, 80.5±6.5years; height, 173.1±6.9cm; body mass, 81.8±13.0kg) and (women: N=25, age, 80.7±7.2years; height, 157.7±6.0cm; body mass, 68.8±17kg), were recruited for a cross-sectional study. Participants filled out PROMIS (Patient-Reported Outcomes Measurement Information System, U. S. Department of Health and Human Services) scales, undertook physical performance tests and had fasted blood samples obtained at rest for measurement of hormonal and immunology biomarkers. RESULTS: When measured by the well-established rat tibial line GH bioassay, one half of the plasma samples (n=20) contained bioassayable GH (bGH), but the other half (n=21) failed to mount increases in tibial plate width above saline injected controls. This difference did not correlate with the age, sex or physical functionality of the plasma donor. It also did not correlate with hGH concentrations measured by immunoassay. In those cases in which bGH was detected, various hierarchical regression models predicted that GHRH, c-peptide, VEGF, NPY, IL-4 and T-regulatory lymphocytes were associated with the difference and predicted bGH. CONCLUSION: Results from this study suggest that the actions of bGH at the cellular level may be modified by other factors and that this may explain the lack of correlations observed in this study.

Acute resistance exercise stimulates sex-specific dimeric immunoreactive growth hormone responses.

PURPOSE: We sought to determine if an acute heavy resistance exercise test (AHRET) would elicit sex-specific responses in circulating growth hormone (GH), with untreated serum and serum treated with a reducing agent to break disulfide-bindings between GH dimers. METHODS: 19 untrained participants (nine men and ten women) participated in an acute heavy resistance exercise test using the back squat. Blood samples were drawn before exercise (Pre), immediate post (IP), +15 min (+15), and +30 min (+30) afterwards. Serum samples were chemically reduced using glutathione (GSH). ELISAs were then used to compare immunoreactive GH concentrations in reduced (+GSH) and non-reduced (-GSH) samples. Data were analyzed using a three-way (2 sex × 2 treatment × 4 time) mixed methods ANOVA, with significance set at p ≤ 0.05. RESULTS: GSH reduction resulted in increased immunoreactive GH concentrations when compared to non-reduced samples at Pre (1.68 ± 0.33 µg/L vs 1.25 ± 0.25 µg/L), IP (7.69 ± 1.08 µg/L vs 5.76 ± 0.80 µg/L), +15 min (4.39 ± 0.58 µg/L vs 3.24 ± 0.43 µg/L), and +30 min (2.35 ± 0.49 µg/L vs 1.45 ± 0.23 µg/L). Also, women demonstrated greater GH responses compared to men, and this was not affected by reduction. CONCLUSIONS: Heavy resistance exercise increases immunoreactive GH dimer concentrations in men and women, with larger increases in women and more sustained response in men. The physiological significance of a sexually dimorphic GH response adds to the growing literature on aggregate GH and may be explained by differences in sex hormones and the structure of the GH cell network.

The influence of age and exercise modality on growth hormone bioactivity in women.

OBJECTIVE: Prior research has indicated that the loss of skeletal muscle mass and bone mineral density observed with aging is related to the prominent age-related decline in the concentration of serum growth hormone (GH). However, there is limited data on the effects of aging on GH responses to acute bouts of heavy resistance exercise (HRE) and aerobic exercise (AE). DESIGN: The present investigation examined the effects of a HRE protocol and an AE protocol on immunoreactive GH (IGH) and bioactive GH (BGH) in active young and old women. RESULTS: Older women had a diminished serum IGH response to both the HRE and AE protocols compared to the younger women, however a similar response was not observed in serum BGH. Additionally, the HRE protocol elicited a greater BGH response than the AE protocol exclusively in the younger group. CONCLUSIONS: Regardless of exercise mode, aging induces an increase in growth hormone polymerization that specifically results in a loss of serum growth hormone immunoreactivity without a concurrent loss of serum growth hormone bioactivity. The greater BGH response to the HRE protocol found in the younger group can be attributed to an unknown serum factor of molecular weight between 30 and 55kD that either potentiated growth hormone bioactivity in response to HRE or inhibited growth hormone bioactivity in response to AE.

Resistance exercise induces region-specific adaptations in anterior pituitary gland structure and function in rats.

The anterior pituitary gland (AP) increases growth hormone (GH) secretion in response to resistance exercise (RE), but the nature of AP adaptations to RE is unknown. To that end, we examined the effects of RE on regional AP somatotroph GH release, structure, and relative quantity. Thirty-six Sprague-Dawley rats were assigned to one of four groups: 1) no training or acute exercise (NT-NEX); 2) no training with acute exercise (NT-EX); 3) resistance training without acute exercise (RT-NEX); 4) resistance training with acute exercise (RT-EX). RE incorporated 10, 1 m-weighted ladder climbs at an 85° angle. RT groups trained 3 days/wk for 7 wk, progressively. After death, trunk blood was collected, and each AP was divided into quadrants (ventral-dorsal and left-right). We measured: 1) trunk plasma GH; 2) somatotroph GH release; 3) somatotroph size; 4) somatotroph secretory content; and 5) percent of AP cells identified as somatotrophs. Trunk GH differed by group (NT-NEX, 8.9 ± 2.4 µg/l; RT-NEX, 9.2 ± 3.5 µg/l; NT-EX, 15.6 ± 3.4 µg/l; RT-EX, 23.4 ± 4.6 µg/l). RT-EX demonstrated greater somatotroph GH release than all other groups, predominantly in ventral regions (P < 0.05-0.10). Ventral somatotrophs were larger in NT-EX and RT-NEX compared with RT-EX (P < 0.05-0.10). RT-NEX exhibited significantly greater secretory granule content than all other groups but in the ventral-right region only (P < 0.05-0.10). Our findings indicate reproducible patterns of spatially distinct, functionally different somatotroph subpopulations in the rat pituitary gland. RE training appears to induce dynamic adaptations in somatotroph structure and function.

Immunoreactive and bioactive growth hormone responses to resistance exercise in men who are lean or obese.

It has been suggested that obese individuals have a blunted growth hormone (GH) response to spontaneous and stimulated GH secretion. The present study was designed to examine the effects of a high-volume, whole body acute resistance exercise (RE) protocol on immunoreactive GH (iGH), bioactive GH (bGH), and GH-binding protein (GHBP) in sedentary lean and obese men. Nine obese (mean ± SD: 20.8 ± 2.1 yr old, 177.0 ± 4.1 cm height, 108.7 ± 15.9 kg body mass, 37.6 ± 5.29% body fat) and nine lean (20.1 ± 2.1 yr old, 177.8 ± 8.7 cm height, 71.7 ± 5.8 kg body mass, 14.7 ± 3.54% body fat) men completed an acute RE protocol (6 exercises, 3 sets of 10 repetitions at 85-95% of 10 repetitions maximum with 120- and 90-s rest periods), and blood samples were collected before, at the midpoint, and immediately after exercise and during recovery (+50, +70, and +110). In contrast to prior studies, which examined acute responses to cardiovascular exercise protocols, groups did not differ in iGH response to the exercise stimulus. However, bGH concentrations overall were significantly lower in the obese than the lean participants (P < 0.001). Additionally, obese individuals had significantly higher GHBP concentrations (P < 0.001). Results suggest that obese and lean sedentary men performing a high-volume, whole body acute RE protocol demonstrate similar increases in iGH. Blunted bGH and elevated GHBP concentrations are indicative of altered GH activity associated with obesity. Prior research findings of blunted iGH response may be attributable to RE protocols not equated on relative intensity or volume. These results underscore the complexity of pituitary biology and its related mechanisms and may have implications for exercise prescription in the treatment of obesity.

Effects of 14 days of microgravity on fast hindlimb and diaphragm muscles of the rat.

The purpose of the present study was to determine the effects of 14 days of microgravity on specific rat fast-twitch muscles, and to compare these data with previous data from rat fast-twitch muscles exposed to microgravity for 10 days (Kraemer et al. 2000). Hindlimb muscles containing predominately fast fibers [extensor digitorum longus (EDL), superficial "white" (GSW) and deep "red" (GDR) gastrocnemius] and the diaphragm (DIA) were removed from flight and ground-based control animals and analyzed for: muscle mass, fiber type distribution, cross-sectional area, and myosin heavy chain (MHC) isoform content. Gravitational unloading for 14 days caused significant decreases in muscle mass (8-9%) and cross-sectional area of almost all fiber types (10-35%) from both EDL and gastrocnemius muscles. However, microgravity had little effect on fiber type composition in these muscles with significant changes occurring only in the EDL type IID fiber population (9.5% decrease). Similarly, relative MHC isoform content was only slightly altered by exposure to microgravity (increased content of MHCIIa in flight EDL). No changes in area, fiber type percentages, or MHC isoform content were detected in the DIA following the 14-day spaceflight. Similar to data gathered following a 10-day spaceflight (Kraemer et al. 2000), the 14-day flight did not appear to cause significant slow-to-fast (I --> IIA) or fast-to-faster (IIA --> IID --> IIB) transformations in hindlimb muscles containing predominantly fast-twitch fibers. However, the longer period of gravitational unloading did result in additional loss in muscle fiber cross-sectional area with involvement of more major fiber types.

Influence of oral contraceptive use on growth hormone in vivo bioactivity following resistance exercise: responses of molecular mass variants.

The purpose was to examine effects of oral contraceptive (OC) use on plasma growth hormone (GH) responses to heavy resistance exercise. Sixty untrained women were placed into one of two groups: currently using OC (Ortho Tri-Cyclen) (n=25; mean+/-SD: 24.5+/-4.2y, 160.4+/-7.1cm, 64.1+/-11.3kg) or not currently using OC (NOC) (n=35; 23.6+/-4.6y, 165.9+/-6.0cm, 65.7+/-10.3kg). Participants performed an acute heavy resistance exercise test (AHRET; six sets of 10 repetition squats; 2min rest between sets) during days 2-4 of the follicular phase (NOC group) or of inactive oral contraceptive intake (OC group). Plasma was obtained before and immediately after AHRET and subsequently fractionated based on apparent molecular weight (>60kD, 30-60kD, and <30kD). GH was determined in unfractionated plasma and each plasma fraction using 4 methods: (1) Nichols Institute Diagnostics immunoradiometric assay (Nichols), (2) National Institute of Diabetes and Digestive Kidney Diseases (NIDDK) competitive radioimmunoassay, (3) DSL immunofunctional enzyme-linked immunoabsorbent assay (IFA) and (4) rat tibial line bioassay. GH increased (P<0.05) in all fractions post-AHRET for the Nichols, NIDDK, and IFA. The OC group displayed higher resting GH for the NIDDK, and higher exercise-induced GH for the IFA, Nichols, and NIDDK in unfractionated plasma and >60kD subfraction compared to NOC group. No differences were observed for the tibial line bioassay. OC use augmented immunological GH response to AHRET in unfractionated plasma and >60kD molecular weight subfraction. However, OC use only increased biological activity of GH in one of two bioassays. These data demonstrated that GH concentrations at rest and following exercise are assay-dependent.

Chronic resistance training in women potentiates growth hormone in vivo bioactivity: characterization of molecular mass variants.

This investigation determined the influence of acute and chronic resistance exercise on responses of growth hormone (GH) molecular variants in women. Seventy-four healthy young women (23 +/- 3 yr, 167 +/- 7 cm, 63.8 +/- 9.3 kg, 26.3 +/- 4.0% body fat) performed an acute bout of resistance exercise (6 sets of 10 repetition maximum squat). Blood samples were obtained pre- and postexercise. Resulting plasma was fractionated by molecular mass (fraction A, >60 kDa; fraction B, 30-60 kDa; and fraction C, <30 kDa) using chromatography. Fractionated and unfractionated (UF) plasma was then assayed for GH using three different detection systems (monoclonal immunoassay, polyclonal immunoassay, and rat tibial line in vivo bioassay). Subjects were then matched and randomly placed into one of four resistance exercise training groups or a control group for 24 wk. All experimental procedures were repeated on completion of the 24-wk resistance training programs. After acute exercise, immunoassays showed consistent increases in UF GH samples and fractions B and C; increases in fraction A using immunoassay were seen only in the monoclonal assay. No consistent changes in bioactive GH were found following acute exercise. Conversely, chronic exercise induced no consistent changes in immunoassayable GH of various molecular masses, whereas, in general, bioassayable GH increased. In summary, although acute exercise increased only immunoactive GH, chronic physical training increased the biological activity of circulating GH molecular variants. Increased bioactive GH was observed across all fractions and training regimens, suggesting that chronic resistance exercise increased a spectrum of GH molecules that may be necessary for the multitude of somatogenic and metabolic actions of GH.

Nocturnal growth hormone secretory dynamics are altered after resistance exercise: deconvolution analysis of 12-hour immunofunctional and immunoreactive isoforms.

To characterize the effects of daytime exercise on subsequent overnight growth hormone (GH) secretion and elimination dynamics, serum was sampled, and GH was measured every 10 min for 12 h (1800 to 0600) in a control (CON) condition and after a 50-set resistance exercise protocol (EX) from 1500 to 1700. GH was measured with a conventional immunoreactive (IR) and an immunofunctional (IF) assay, and values were analyzed via a multi-parameter deconvolution analysis. EX resulted in a higher overnight secretory burst frequency [CON: 7.6 (SD 2.4) < EX: 9.4 (2.2) bursts per 12 h, P = 0.005] but lower mean burst mass [CON: 9.2 (4.7) > EX: 6.0 (2.9) microg/l, P = 0.019] and secretory rate [CON: 0.68 (0.29) > EX: 0.48 (0.23) microg/l/min; P = 0.015; ANOVA main effect means presented]. Approximate entropy (ApEn) was greater after EX, indicating a less orderly GH release process than CON. The estimated half-life of IF GH was significantly lower than IR GH [IF: 15.3 (1.1) < IR 19.8 (1.6) min, P < 0.001] but similar between the CON and EX conditions (approximately 17 min). Despite the changes in secretory dynamics, 12-h mean and integrated GH concentrations were similar between conditions. The results suggest that although quantitatively similar total amounts of GH are secreted overnight in CON and EX conditions, resistance exercise alters the dynamics of secretion by attenuating burst mass and amplitude yet increasing burst frequency.

High-affinity growth hormone binding protein and acute heavy resistance exercise.

PURPOSE: The purpose of this investigation was to examine the influence of resistance training on circulating concentrations of growth hormone binding protein (GHBP) in response to acute heavy resistance exercise. METHODS: Using a cross-sectional experimental design, a group of resistance-trained men (RT, N=9, 7.9+/-1.3 yr resistance training experience) and a group of untrained men (UT, N=10) performed an acute heavy resistance exercise protocol (AHREP) consisting of 6 sets of 10 repetition maximum parallel squats. Blood samples were obtained 72 h before exercise, immediately before exercise, and 0, 15, 30, 45, and 60 min after exercise. RESULTS: Significant increases (P<0.05) in GHBP, immunoreactive growth hormone (iGH), and IGF-1 were observed in both subject groups after AHREP. There were no differences (P>0.05) between groups in GHBP at rest or after AHREP. However, RT exhibited a significantly greater iGH response to AHREP than UT subjects, and significantly higher IGF-1 values at rest and after exercise. Significant positive correlations were found between GHBP and BMI, body fat, and leptin in both groups. A significant positive correlation also was observed between resting leptin and GHBP values in UT but not RT subjects. CONCLUSIONS: In summary, these data indicate that resistance training does not increase blood GHBP. Nevertheless, the increases observed with IGF-1 concentrations in the resistance-trained subjects do suggest an apparent adaptation with the regulation of this hormone. If there was in fact an increase in GH sensitivity and GH receptor expression at the liver that was not detected by blood GHBP in this study, it may be possible that factors contributing to the circulating concentration of GHBP other than hepatocytes (e.g., leptin and adipocytes) may serve to mask training-induced increases in circulating GHBP of a hepatic origin, thus masking any detectable increase in GH receptor expression.

Responses of plasma proenkephalin peptide F in rats following 14 days of spaceflight.

INTRODUCTION: . Proenkephalin peptide F [107-140] is related to the enhancement of immune function, while microgravity has been shown to cause immuno-suppression. We investigated the physiological response of proenkephalin peptide F to microgravity. METHODS: There were 12 Fischer 344 female rats, ovariectomized at 10.5 wk of age, used to determine plasma concentrations of peptide F in response to a 14-d flight aboard the Columbia Space Shuttle mission STS-62. There were 36 other such rats that served as ground-based controls to separate the effects of microgravity from those of thermal stress, flight stress, and crowded habitats. Control groups of 12 rats each were kept under the following conditions: 1) 22 degrees C vivarium, 2) 28 degrees C vivarium, and 3) variable (Var) to mimic flight. The flight and control groups were housed in animal enclosure modules 21 d prior to flight and for the duration of the study. The rats were sacrificed within 4-5 h after landing, at which time blood samples were obtained. RESULTS: Body weights were obtained prior to sacrifice; mean values were flight, 199 g; 22 degrees C, 193 g; 28 degrees C, 192 g; and Var, 194 g. The flight group produced a significantly greater (p < or = 0.05) level of plasma peptide F (0.056 pmol x ml(-1)) compared with the controls (0.016, 0.022, and 0.016 pmol x ml(-1) for 22 degrees C, 28 degrees C, and Var, respectively). Flight animals demonstrated higher corticosterone concentrations and reduced T and B cell splenocyte counts than controls. CONCLUSIONS: These data indicate that the increases in proenkephalin peptide F observed with exposure to microgravity may present an adrenal-medullary response to cope with the decreased immune function and increased stress experienced during spaceflight and landing.

Growth hormone molecular heterogeneity and exercise.

There are more than 100 molecular isoforms of circulating growth hormone (GH), but the traditional measurement approach in the exercise literature has only focused on the main isoform (i.e., 22 kDa). New assay methodologies now can assess various GH isoforms. The current data suggest that exercise results in the preferential release of GH isoforms with extended half-lives, thereby sustaining biological actions.