Bi-Arrhenius Diffusion and Surface Trapping of

We report measurements of the diffusion rate of isolated ion-implanted ^{8}Li^{+} within ∼120 nm of the surface of oriented single-crystal rutile TiO_{2} using a radiotracer technique. The α particles from the ^{8}Li decay provide a sensitive monitor of the distance from the surface and how the depth profile of ^{8}Li evolves with time. The main findings are that the implanted Li^{+} diffuses and traps at the (001) surface. The T dependence of the diffusivity is described by a bi-Arrhenius expression with activation energies of 0.3341(21) eV above 200 K, whereas at lower temperatures it has a much smaller barrier of 0.0313(15) eV. We consider possible origins for the surface trapping, as well the nature of the low-T barrier.

Growth hormone: independent release of big and small forms from rat pituitary in vitro.

Sequential release of big and small forms of growth hormone by perifused rat pituitaries has been demonstrated by immunoprecipitation. The results suggest that either the two forms are independently synthesized and released, or that a newly synthesized molecule of big growth hormone follows one of two paths: direct release or intracellular processing through the storage compartment with conversion to small growth hormone.

Partial purification and characterization of a peptide with growth hormone-releasing activity from extrapituitary tumors in patients with acromegaly.

Growth hormone (GH)-releasing activity has been detected in extracts of carcinoid and pancreatic islet tumors from three patients with GH-secreting pituitary tumors and acromegaly. Bioactivity was demonstrated in 2 N acetic acid extracts of the tumors using dispersed rat adenohypophyseal cells in primary monolayer culture and a rat anterior pituitary perifusion system. The GH-releasing effect was dose responsive and the greatest activity was present in the pancreatic islet tumor. Small amounts of activity were also found in two other tumors (carcinoid and small cell carcinoma of lung) unassociated with GH hypersecretion. Each of the tumors contained somatostatin-like immunoreactivity but the levels did not correlate with the net biologic expression of the tumor. Sephadex G-75 gel filtration indicated the GH-releasing activity to have an apparent molecular size of slightly greater than 6,000 daltons. The GH-releasing activity was adsorbed onto DEAE-cellulose at neutral pH and low ionic strength, from which it could be eluted by increasing ionic strength. The GH-releasing activity was further purified by high pressure liquid chromatography using an acetonitrile gradient on a cyanopropyl column to yield a preparation that was active at 40 ng protein/ml. Partially purified GH-releasing activity, from which most of the bioactive somatostatin had been removed, increased GH release by pituitary monolayer cultures to five times base line. Enzymatic hydrolysis studies revealed that the GH-releasing activity was resistant to carboxypeptidase, leucine-aminopeptidase, and pyroglutamate-amino-peptidase but was destroyed by trypsin and chymotrypsin, indicating that internal lysine and/or arginine and aromatic amino acid residues are required for biologic activity and that the NH2-terminus and CO9H-terminus are either blocked or not essential. The results provide an explanation for the presence of GH-secreting tumors in some patients with the multiple endocrine neoplasia syndrome, type I, and warrant the addition of GH-releasing activity to the growing list of hormones secreted by tumors of amine precursor uptake and decarboxylation cell types.

Basal and dibutyryl cyclic AMP-stimulated release of newly synthesized and stored growth hormone from perifused rat pituitaries.

The basal rate of pre-labeled stored 14C-labeled rat growth hormone ([14C]rGH) release from perifused rat pituitary explants is a constant fraction of pituitary GH content, suggesting random release from the storage pool. Basal release of newly synthesized [3H]rGH occurs in two phases: 1) immediate and associated with [3H]rGH synthesis, and 2) late (delayed by 60 min) and independent of concurrent [3H]rGH synthesis. Dibutyryl cyclic AMP (10(-2)M)-stimulated release of stored [14C]rGH is characterized by an initial acute rise followed by a second phase of continuous rapid release. Immediate and late release of new [3H]rGH is increased by dibutyryl cyclic AMP, and the late phase of [3H]rGH is less delayed. Simultaneous exposure of pituitary explants to [3H]alanine and [14C]leucine resulted in the release of immunoprecipitable rGH whose ratio of incorporated 3H and 14C varied with time. The observed changes suggest that after it is synthesized, a GH molecule may either be released directly or be processed into the somatotroph's storage compartment. In addition, stored GH is composed of two pools, one of which is immediately releasable. The differential incorporation of [3H]alanine and [14C]leucine into "big" and "small" rGH, together with the ability to differentially displace 3H-labeled "big" and 14C-labeled "small" rGH from the GH antibody suggest that "big" rGH is a heterogenous molecule including "small" rGH and another peptide rather than simply a dimer of "small" rGH.

Influence of synthetic somatostatin upon growth hormone release from perifused rat pituitaries.

Basal release of pre-labeled, stored tritiated rat growth hormone ([3H]rGH) from perfused rat pituitary explants is a constant fraction of pituitary [LH]rGH content. Synthetic somatostatin (SRIF) inhibits the release of pre-labeled, stored [3H]rGH in a dose-dependent fashion. Prolonged exposure to SRIF results in an immediate and continuous inhibition of [3H]rGH release. In the in vitro perifusion system, the maximal inhibition, which is achieved with 25 nM SRIF, results in a rate of [3H]rGH release which is 30 to 40 per cent of basal release. Pulses of SRIF produce inhibition of [3H]rGH release followed by rebound release after withdrawal of SRIF. When the time of exposure to SRIF is held constant, both the SRIF-induced inhibition and the rebound release of [3H]rGH are dose-dependent. A similar progressive response is seen when a constant SRIF concentration is pulsed for variable periods of time. There is no net inhibition of [3H]rGH release by pulses of SRIF.

Functional substructure of the rat somatotroph immediate release pool: definition by responses to N6,2'-O-dibutyryl cyclic adenosine 3',5'-monophosphate, potassium ion, and/or prostaglandin E1.

Previous results from our laboratory suggest that stored rat GH (rGH) in the pituitary is divisible into at least two functional compartments. An immediate release pool (IRP) responds quickly and can be exhausted. A larger and less labile pool responds continuously to long term stimulation. We previously demonstrated that the sum of IRP rGH discharged by (Bu)2cAMP and potassium ion (K+) in separate experiments exceeds by one third the amount released by the two agents administered simultaneously. This overlap suggested an IRP substructure. We used prelabeled rat pituitary fragments in an in vitro perifusion-immunoprecipitation system to define intracellular hormone storage and to track release of stored rGH and rat PRL (rPRL). We tested three secretagogues: K+ to induce release without altering pituitary cAMP levels, (Bu)2cAMP to introduce cAMP into cells without activating adenylate cyclase, and prostaglandin E1 (PGE1) to produce a temporary, localized cAMP increase through adenylate cyclase activation. Prelabeled tissue in basal perifusion was first exposed to one secretagogue for 90 min. Then, while the first secretagogue was continued, a second secretagogue was added for a second 90-min period. Demonstrable alterations in tissue responses to secretagogues included: K+ diminished PGE1-induced rGH release from the IRP by 69% but had a mixed effect on the response to (Bu)2cAMP; (Bu)2cAMP enhanced K+-induced rGH release from the IRP by 71% but reduced PGE1-induced rGH release by 72%; PGE1 diminished K+-induced rGH release by 13% and (Bu)2cAMP-induced rGH release by 23%; combined K+ and (Bu)2cAMP reduced the rGH response to PGE1 stimulation by 81% whereas prior PGE1 enhanced the response to subsequent combined K+ and (Bu)2cAMP by 16%. We conclude that the somatotroph IRP consists of a K+-sensitive portion which overlaps with, but is not identical to, a (Bu)2cAMP-sensitive portion. The PGE1-sensitive portion of the IRP appears to be roughly equivalent to the shared fraction of the K+- and (Bu)2cAMP-sensitive portions of the IRP. These agents define a similar rPRL compartmentalization. However, the K+-sensitive portions of the somatotroph and lactotroph IRP differ in that the former is larger and expandable, whereas the latter is smaller and appears to be of limited capacity.

Growth hormone-releasing factor-44 specificity for components of somatotroph and lactotroph immediate release pool substructures.

Rat somatotroph and lactotroph hormone storage is divisible into at least two functional compartments: an immediate release pool (IRP) and a pool that responds to prolonged stimulation. An IRP substructure has been defined by release in response to potassium ion (K+), prostaglandin E1 (PGE1), and Bu2cAMP. The somatotroph IRP is expandable; the lactotroph IRP is fixed in size. The present experiments examined which IRP components contribute to the rapid release of stored GH in response to GH-releasing factor-44 (GRF). Release of stored PRL was monitored for comparison. In vitro prelabeling defined stored rat (r) GH and rPRL. Release in response to 21 mM K+, 3 microM PGE1, 1 mM Bu2cAMP, and/or 3 nM GRF was monitored with a perifusion-immunoprecipitation system. After 120 min of basal perifusion, tissue was exposed to one of the four secretagogues for 90 min. During a second 90-min period a second secretagogue was added while exposure to the first secretagogue continued. We demonstrated that 21 mM K+ reduces peak rGH release in response to 3 nM GRF by 52%, whereas GRF does not reduce rGH release in response to K+; 3 microM PGE1 reduces rGH release in response to GRF by only 19% although GRF reduces rGH release in response to PGE1 by 88%; 1 mM Bu2cAMP reduces rGH release in response to GRF by 87%, and GRF eliminates rGH release in response to Bu2cAMP (1.2% of control value); combined K+ plus Bu2cAMP reduce rGH release in response to GRF to 2.5% of the control value, whereas after GRF pretreatment rGH release in response to combined K+ plus Bu2cAMP is 93% of the control value; and combined PGE1 and Bu2cAMP reduce the response to GRF to 17% of the control value. Effects on rPRL release are qualitatively similar. We conclude that immediate GRF-stimulated release of stored rGH originates in the somatotroph IRP components defined by responses to PGE1 and Bu2cAMP; it derives only slightly, if at all, from the IRP component defined by the response to K+. The smaller GRF-stimulated release of IRP rPRL is similarly derived.

Combined effects of human growth hormone (GH)-releasing factor-44 (GRF) and somatostatin (SRIF) on post-SRIF rebound release of GH and prolactin: a model for GRF-SRIF modulation of secretion.

Somatostatin (SRIF) and GRFs play key roles in regulating GH secretion. We previously presented a model of SRIF-cAMP interaction; SRIF blocks rat (r) GH release without preventing its accumulation in a potentially releasable pool. This phenomenon may represent a mechanism whereby tonic SRIF inhibition and its subsequent reduction or withdrawal can modulate the magnitude if not the initiation of rGH pulses. Herein we test that model using human GRF-44 (hGRF-44). Tritium-prelabeled rat anterior pituitary fragments were perifused until stored [3H]rGH and [3H]rPRL release rates were stable. SRIF (10 or 25 nM), with and without hGRF-44 (3 or 10 nM), was added in short (1-h hGRF-44) and long (3-h hGRF-44) protocols; SRIF was then withdrawn while hGRF-44 was continued. Release of stored prelabeled [3H]rGH and [3H]rPRL was assessed by immunoprecipitation. Effects on PRL release were followed for comparison. SRIF-induced inhibition of release was only partially reversed by hGRF-44. At these concentrations and so long as SRIF was present, hGRF-44 could not stimulate the rate of hormone release to values above pre-SRIF basal rates. On the other hand, the amplitude of post-SRIF rebound release was increased by prolonging exposure to SRIF alone, by including hGRF-44 with SRIF, by increasing the amount of hGRF-44 included with SRIF, by prolonging exposure to hGRF-44 plus SRIF, and by using a smaller concentration of SRIF during exposure to hGRF-44. Interaction of hGRF-44-SRIF effects generated peak rates of hormone release after SRIF withdrawal which exceeded the maximum rates achieved using hGRF-44 alone in this system. Lactotroph responses were much smaller, but qualitatively resembled somatotroph responses. We conclude that the interplay of simultaneous hGRF-44 and SRIF effects can regulate the amplitude of rGH pulses. Although GRF can initiate physiological GH release, and GRF antisera can block GH pulses, we suggest that the surge of release that follows reduction of SRIF-induced inhibitory tone in vitro represents a potential mechanism that could contribute to the initiation of some pulses of release. Finally, we also present a theoretical model of secretagogue interactions at the cellular level to explain our results. The model is compatible with either a homogeneous cell population in which each secretory cell has multiple capabilities or a heterogeneous cell population composed of cell subgroups with complementary secretory abilities.

Pituitary immediate release pools of growth hormone and prolactin are preferentially refilled by new rather than stored hormone.

Pituitary stores of rat GH (rGH) and PRL (rPRL) are divisible into immediately releasable and more stable compartments representing either compartmentalized hormone within individual cells of a homogeneous population or responses of specialized cell subsets in a functionally heterogeneous population. In addition, newly synthesized rGH and rPRL can be processed either into intracellular storage or toward direct release. Fractional assignment of new hormone to these two paths can be influenced in the somatotroph by GHRH and may also represent either intracellular processes or functional heterogeneity of cells. We investigated the source, newly synthesized or stored, of hormone refilling the somatotroph and lactotroph immediately releasable pools (IRP) after their discharge by 21 mM potassium ion, 1 mM (Bu)2cAMP, 3 nM human GHRH-44, or 3 microM prostaglandin E1. Experiments were performed using perifused pituitary fragments exposed sequentially to [14C]- and [3H]leucine in association with stimulation by two 30-min pulses of the same secretagogue. Therefore, only [14C]hormone was available for release by the first stimulus, whereas both [14C]- and [3H]hormone were available for release by the second stimulus. Analysis was by specific immunoprecipitation. The first episode of stored [14C]rGH release exceeded the second episode of stored [14C]rGH release in response to each secretagogue. However, release of newly synthesized [3H]rGH in response to the second episode of stimulation exceeded the simultaneous release of stored [14C]rGH while matching or exceeding the [14C]rGH release that had occurred in the same experiment in response to the first episode of stimulation. Refilling both GH and PRL IRP stores drew primarily upon newly synthesized hormone, but with different secretagogue-specific patterns. These data confirm differential handling of new and stored rGH and rPRL within the pituitary. They are consistent with either (1) the enhanced shunting of newly synthesized hormone to IRPs within cells that are capable of compartmentalized intracellular hormone storage, or (2) the relatively complete discharge of a subset of somatotrophs and lactotrophs that are specialized to deliver pulsed hormone release, after which they are refilled by newly synthesized hormone.

Human pancreatic growth hormone-releasing factor-44 differentially stimulates release of stored and newly synthesized rat growth hormone in vitro.

Effects of synthetic human pancreatic GH-releasing factor-44 (hpGRF-44) on synthesis and release of rat pituitary GH and PRL were examined in vitro in a static incubation system. A double label, specific immunoprecipitation protocol permitted simultaneous study of hormone synthesis as well as release of both stored and newly synthesized hormone. Synthetic hpGRF-44 (0.3 and 3.0 nM) stimulated the release of stored GH 240% beyond the basal level, while simultaneously stimulating the release of newly synthesized GH by 610%. Despite the stimulation of release, hpGRF-44 did not alter GH synthesis (102% of control value). A small but statistically significant increase in release of stored PRL occurred in response to hpGRF-44, while release of newly synthesized PRL and PRL synthesis were unaffected. In contrast, 1 mM (Bu)2cAMP stimulated the release of both newly synthesized and stored GH and PRL. We conclude that hpGRF-44 differentially stimulates GH release from separate intracellular compartments and that the lactotroph may also, under certain conditions, respond to this secretagogue.

Effect of growth hormone-releasing factor-44 upon release of concurrently synthesized hormone by perifused rat pituitary tissue.

We previously reported the differential stimulation of stored and newly synthesized rat (r)GH release by human GH-releasing factor-44 (hGRF-44). Those studies were performed over a 3-h period in a static in vitro incubation system. The present experiments focus on hGRF-44 effects upon release of new hormone (synthesized during tissue stimulation by the secretagogue) and were performed in in vitro perifusion to study the time course of the response. A double label ([14C], [3H]), immunoprecipitation protocol defined hormone release in relation to time of synthesis: intracellular stores of hormone were prelabeled with [14C]; subsequent exposure of prelabeled tissue to continuous concurrent [3H]leucine and 3 nM hGRF-44 defined newly synthesized hormone and associated it with the secretagogue. In a parallel set of experiments, 1 mM (Bu)2cAMP was substituted for hGRF-44. Prolonged exposure to hGRF-44 in perifusion stimulated an initial surge of stored [14C]rGH release which was followed by a rate of [14C]rGH release which declined rapidly but remained suprabasal. [14C]rGH release in response to (Bu)2cAMP was also biphasic, but the initial surge was delayed and the later stimulatory period was better sustained in comparison to responses to hGRF-44. Stimulation of stored [14C] rPRL release by hGRF-44 was observed in perifusion, confirming our observation in the static system. Release of newly synthesized, 3H-labeled rGH was immediately stimulated by either hGRF-44 or (Bu)2cAMP, and that stimulation was maintained throughout exposure to either secretagogue. In contrast, whereas newly synthesized [3H]rPRL release was stimulated by (Bu)2cAMP, its release in response to hGRF-44 resembled that in control experiments. No effect upon hormone synthesis was observed during the 3h of exposure to hGRF-44. In conclusion, these experiments confirm that hGRF-44 differentially stimulates release of both newly synthesized and stored rGH, and demonstrate differential dynamics in the response as well. Specifically, hGRF-44 stimulation of new rGH release is sustained while its effect on stored hormone simultaneously wanes. Further, when expressed as a percent of intracellular hormone available for release, new hormone is released more than 10 times faster than stored hormone. These observations argue for the existence of separate intracellular paths along which newly synthesized and stored hormone are released by the somatotroph. Finally, these data confirm that hGRF-44 stimulates release of stored rPRL without altering release of newly synthesized rPRL.

Thyrotropin-releasing hormone stimulates growth hormone release from the anterior pituitary of hypothyroid rats in vitro.

We have examined the interaction of thyroid hormone and TRH on GH release from rat pituitary monolayer cultures and perifused rat pituitary fragments. TRH (10(-9) and 10(-8)M) consistently stimulated the release of TSH and PRL, but not GH, in pituitary cell cultures of euthyroid male rats. Basal and TRH-stimulated TSH secretion were significantly increased in cells from thyroidectomized rats cultured in medium supplemented with hypothyroid serum, and a dose-related stimulation of GH release by 10(-9)-10(-8) M TRH was observed. The minimum duration of hypothyroidism required to demonstrate the onset of this GH stimulatory effect of TRH was 4 weeks, a period significantly longer than that required to cause intracellular GH depletion, decreased basal secretion of GH, elevated serum TSH, or increased basal secretion of TSH by cultured cells. In vivo T4 replacement of hypothyroid rats (20 micrograms/kg, ip, daily for 4 days) restored serum TSH, intracellular GH, and basal secretion of GH and TSH to normal levels, but suppressed only slightly the stimulatory effect of TRH on GH release. The GH response to TRH was maintained for up to 10 days of T4 replacement. In vitro addition of T3 (10(-6) M) during the 4-day primary culture period significantly stimulated basal GH release, but did not affect the GH response to TRH. A GH stimulatory effect of TRH was also demonstrated in cultured adenohypophyseal cells from rats rendered hypothyroid by oral administration of methimazole for 6 weeks. TRH stimulated GH secretion in perifused [3H]leucine-prelabeled anterior pituitary fragments from euthyroid rats. A 15-min pulse of 10(-8) M TRH stimulated the release of both immunoprecipitable [3H]rat GH and [3H]rat PRL. The GH release response was markedly enhanced in pituitary fragments from hypothyroid rats, and this enhanced response was significantly suppressed by T4 replacement for 4 days. The PRL response to TRH was enhanced to a lesser extent by thyroidectomy and was not affected by T4 replacement. These data suggest the existence of TRH receptors on somatotrophs which are suppressed by normal amounts of thyroid hormones and may provide an explanation for the TRH-stimulated GH secretion observed clinically in primary hypothyroidism.

Big growth hormone (GH): conversion to small GH without peptide bond cleavage.

Mercaptoethanol treatment of big growth hormone (GH) obtained from human pituitary resulted in a 60% conversion to small GH. Further dissociation was obtained by combined treatment with the reducing agent plus urea. The results indicate that the existence of big GH is dependent upon the formation of inter-polypeptide chain disulfide bonds.

Use of telemedicine for children with special health care needs.

OBJECTIVE: In 1995, the Children's Medical Services (CMS) of the State of Georgia contracted with the Department of Pediatrics of the Medical College of Georgia (MCG) and the MCG Telemedicine Center to develop telemedicine programs to provide subspecialty care for children with special health care needs. This article presents project statistics and results of client evaluation of services, as well as physician faculty attitudes toward telemedicine. DESIGN: A demonstration project using telemedicine between a tertiary center and a rural clinic serving children with special health care needs was established. Data were collected and analyzed for December 12, 1995 to May 31, 1997, during which 333 CMS telemedicine consultations were performed. RESULTS: Most CMS telemedicine consultations (35%) involved pediatric allergy/immunology. Other subspecialties included pulmonology (29%), neurology (19%), and genetics (16%). Overall, patients were satisfied with the services received. Initially, physician faculty members were generally positive but conservative in their attitudes toward using telemedicine for delivering clinical consultation. After a year's exposure and/or experience with telemedicine, 28% were more positive, 66% were the same, and only 4% were more negative about telemedicine. The more physicians used telemedicine, the more positive they were about it (r =.30). CONCLUSIONS: In terms of family attitudes and individual care, telemedicine is an acceptable means of delivering specific pediatric subspecialty consultation services to children with special health care needs, living in rural areas distant to tertiary centers. Telemedicine is more likely to be successful as part of an integrated health services delivery than when it is the sole mode used for delivery of care.

Significance of extrathyroidal uptake of Tc-99m and I-123 in the thyroid scan: concise communication.

Areas of extrathyroidal uptake were noted on thyroid scans obtained with Tc-99m and I-123 in five subjects. Four of them had palpable lymph nodes corresponding to the extrathyroidal uptake. All the palpable nodes that showed radionuclide uptake contained metastatic thyroid carcinoma, with predominantly well-differentiated follicular cells. Extrathyroidal areas of uptake on a routine thyroid scan with pertechnetate and/or radioiodine most probably indicate thyroid carcinoma with regional metastases.

SRIF-sensitive compartmentalization of stored rGH is abolished by hypothyroidism.

Rat adenohypophyses lose immuno- and bioassayable growth hormone in hypothyroidism. We examined whether the somatotroph also loses mechanisms for intracellular hormone compartmentalization during hypothyroidism. A series of identical perifusions was performed using pituitary tissue from thyroidectomized rats before and after thyroxine replacement. Somatostatin (SRIF), (Bu)2cAMP and potassium ion were employed to produce a wide range of hormone release responses. Growth hormone synthesis diminished with hypothyroidism and increased with thyroid hormone replacement. Growth hormone release was therefore expressed as a percent of pituitary content to circumvent effects of variable content. Post-somatostatin rebound release was lost in hypothyroidism: it fell progressively after thyroidectomy (day 7 = 45% of control; day 14 = 11%; day 71 = 3%) and was restored by thyroxine replacement (day 2 = 24%; day 5 = 50%; day 9 = 102%). In conclusion, hypothyroid somatotrophs lose the ability to sequester stored hormone in a SRIF-sensitive compartment. Thyroxine replacement restores that capability. Thus, SRIF-sensitive rGH compartmentalization is thyroid hormone dependent.

Monensin influences basal and human growth hormone-releasing hormone 44-induced release of stored and new rat growth hormone and prolactin.

When previous data suggested a growth hormone-releasing factor (GRF)-sensitive branch in intracellular hormone processing, the monensin-sensitive Golgi apparatus seemed a likely candidate. We examined monensin's effect on basal and GRF-stimulated release of newly synthesized and stored rat growth hormone (rGH) and rat prolactin (rPRL). 14C-Pre-labeled, perifused rat pituitary fragments were exposed to [3H]leucine in 0-10 microM monensin; a pulse of 3 nM GRF assessed subsequent secretory responsivity. Monensin dose-dependently reduced basal release of stored [14C]rGH and [14C]rPRL. GRF-stimulated release of stored [14C]hormone was doubled after 0.03 microM and 0.1 microM monensin; higher concentrations diminished stored hormone release. Low concentrations of monensin accelerated basal (0.03 microM and 0.1 microM) and GRF-stimulated (0.03 microM) [3H]rGH and [3H]rPRL release without altering recovery; higher monensin concentrations (greater than or equal to 1 microM) reduced basal, and abolished GRF-stimulated, new hormone release and reduced total [3H]rGH and [3H]rPRL recovery. These data are consistent with a GRF-sensitive and monensin-influenced branch in intracellular hormone processing that regulates the fraction of new hormone exiting the cell without prior immersion in storage compartments.

Physical training, lifestyle education, and coronary risk factors in obese girls.

The effects of supervised physical training (PT) and lifestyle education (LSE) on risk factors for coronary artery disease and non-insulin-dependent diabetes mellitus were compared in obese 7- to 11-yr-old black girls. The subjects were divided into two groups. The PT group (N = 12) completed a 5-d.wk-1, 10-wk, aerobic training program; and the LSE group participated in weekly lifestyle discussions to improve exercise and eating habits. The PT group showed a significant increase in aerobic fitness (P < 0.05) and decrease in percent body fat (P < 0.05), while the LSE group declined significantly more in dietary energy and percent of energy from fat (P < 0.05). Fasting insulin did not change significantly. The LSE group declined significantly more than the PT group in glucose (P < 0.05), and glycohemoglobin declined from baseline in both groups (P < 0.05). Lipid changes were similar in the two groups: total cholesterol/high density lipoprotein cholesterol (P < 0.01) and triglycerides (P < 0.05) declined, the low density lipoprotein (LDL)/apoproteinB ratio increased (which indicates a decrease in small dense LDL) (P < 0.05) and lipoprotein(a) increased (P < 0.05). Thus, the interventions were similarly effective in improving some diabetogenic and atherogenic factors, perhaps through different pathways; i.e., the PT improved fitness and fatness, while the LSE improved diet. Exercise and diet-induced changes in lipoprotein(a) require further investigation.

Practice of otolaryngology via telemedicine.

Teleotolaryngology is becoming a reality as a result of improvements in technology and telecommunications. This prospective, clinical trial was designed to demonstrate the utility of three telemedicine systems in an otolaryngology practice. Optel is a desktop system used in the office. Picasso is a mobile system used from various locations throughout the hospital. The Georgia Statewide Telemedicine Program (GSTP) is a large, sophisticated system used from a fixed site within a rural hospital. Patients with a wide variety of ear, nose, and throat problems were presented to consultants at two medical teaching centers in Georgia. Fifty-four consults were completed over a 24-month period. In addition, three teleconsultations demonstrated enhanced capabilities for continuing medical education (CME) and health care networks. Nine different specialty fields were accessed by the otolaryngologist. Five consults were completed via the Optel system; 13 via the Picasso system; and 36 via GSTP. Overall, teleotolaryngology provided quality audio and visual communication between the physicians that significantly improved diagnostic capabilities and treatment options for the patient.

Ileal carcinoid tumor complicated by retroperitoneal fibrosis and a prolactinoma.

A patient with mid-gut carcinoid tumor and the unusual complication of retroperitoneal fibrosis was also found to have a prolactinoma. This case brings the number of reported mid-gut carcinoid tumors complicated by a second endocrine neoplasm to five. Three of the second tumors were parathyroid in origin, and the fourth was an insulinoma. In view of the rarity of second tumors and in the absence of documented familial occurrence, it is inappropriate to exhaustively study each person with mid-gut carcinoid tumor, or their families, for a second endocrine neoplasm; however, physicians caring for patients with mid-gut carcinoid should be aware that second tumors are possible. Retroperitoneal fibrosis is also a rare complication of carcinoid, but can be associated with renal failure that can be prevented by surgical intervention. Thus, physicians caring for patients with the carcinoid syndrome should also be aware of this complication.