PubMed Health⌕ Search

Biomedical subjects

H G Friesen

Publications and source records attributed to H G Friesen.

At least 19 recordsLinked to original sources
PubMed1992

Comparison of Nb2 lymphoma cell bioassay with immunoassay for human prolactin: the role of estrogen.

The Nb2 lymphoma cell bioassay (BA-PRL) is a sensitive measure of serum prolactin under physiologic conditions. Since estrogens prime the lactotroph, prolactin heterogeneity and hence bioassayable prolactin may be influenced. A study was performed to observe the effect on BA-PRL of changing estradiol (E2) concentrations. In 13 normal subjects clomiphene citrate was administered to stimulate ovarian activity and blood samples were obtained before and after stimulation. Estradiol, BA-PRL and immunoassayable prolactin (RIA-PRL) were measured. While there was a substantial increase in E2 post-stimulation (p less than 0.001), there was no significant change in BA-PRL, RIA-PRL or BA/RIA-PRL ratios. Despite the lack of change in the mean BA/RIA-PRL ratio over a wide range of E2 concentrations that include and exceed those normally seen in spontaneous menstrual cycles, it is difficult to drawn conclusions regarding an association between E2 and BA/RIA-PRL ratios as there was no discernible change in the concentration of prolactin (possibly due to the antiestrogenic effect of clomiphene citrate).

Adolescent↗
PubMed1992

Prolactin bioassay in schizophrenia before and after neuroleptics.

Fifteen drug-free schizophrenic male inpatients and 14 normal control subjects were studied. The schizophrenic subjects had a significantly lower ratio of bioassay prolactin to radioimmunoassay prolactin before neuroleptic treatment than they did after treatment. The ratio was lower in the drug-free patients as compared with normal controls. These findings suggest that neuroleptic medications may alter the molecular forms of serum prolactin. The results also suggest that drug-free schizophrenic patients may have a different pattern of prolactin variants than normal subjects and that this difference could be secondary to a disordered tuberoinfundibular dopamine system or long-term effects of neuroleptic drugs.

Adult↗
PubMed1992

Molecular cloning and cDNA sequence analysis of coho salmon stanniocalcin.

Stanniocalcin (STC) (formerly known as both teleocalcin and hypocalcin) is an anti-hypercalcemic, glycoprotein hormone that is produced by the corpuscles of Stannius (CS), endocrine glands that are confined to bony fishes. The hormone has a unique amino acid sequence and exists as a disulfide-linked homodimer in the native state. In previous studies, we have described the purification and characterization of two salmon STCs, and examined the regulation of hormone secretion in response to calcium using both in vitro and in vivo model systems. This report describes the molecular cloning and cDNA sequence analysis of a coho salmon STC messenger RNA (mRNA) from a salmon CS lambda gt10 cDNA library. The STC mRNA in salmon is approximately 2 kilobases in length and encodes a primary translation product of 256 amino acids. The first 33 residues comprise the prepro region of the hormone, whereas the remaining 223 residues make up the mature form of the hormone. One N-linked, glycosylation consensus sequence was identified in the protein coding region as well as an odd number of half cysteine residues, the latter of which would allow for interchain bonding or dimerization of monomeric subunits. In addition, three sites were identified in the mature protein core of STC (two dibasic, one tribasic) that may be acted upon by endopeptidases to produce truncated forms of the hormone. In support of this latter possibility, Western blot analysis revealed multiple molecular weight forms of sTC within salmon glands.

Adaptation, Physiological↗
PubMed1992

Characterization of big, big prolactin in patients with hyperprolactinaemia.

OBJECTIVE: The present study was designed to characterize the clinical findings of patients with macroprolactinaemia (sustained hyperprolactinaemia where the predominant form of prolactin is of large molecular size) and to further assess the bioactivity and structure of big, big prolactin (BB-PRL). DESIGN: The patients with macroprolactinaemia were identified by the domperidone test and by gel filtration of their serum samples. The bioactivity of sera and fractions containing BB-PRL was evaluated and the fractions analysed by affinity chromatography and electrophoresis. PATIENTS: Eleven patients with hyperprolactinaemia in whom BB-PRL was the predominant form (group 1) were studied. Sera were also examined from eight patients with prolactinomas (group 2). Thirty-one first-degree relatives from patients in group 1 were screened for macroprolactinaemia. MEASUREMENTS: Prolactin in the sera and fractions was measured by radioimmunoassay (RIA), immunoradiometric assay (IRMA) and Nb2 cell bioassay (Nb2 BA). The distribution of BB-PRL was also investigated after protein A Sepharose chromatography, immunoprecipitation, SDS-PAGE and Western blotting. RESULTS: (1) Seven out of 11 patients in group 1 had galactorrhoea, menstrual disturbances or both; (2) the ratio Nb2 BA/RIA in whole serum was similar to the ratio found in group 2 patients; (3) the ratios Nb2 BA/RIA and Nb2 BA/IRMA in the BB-PRL fractions obtained after gel filtration were significantly lower than in whole serum (P < 0.003); (4) in group 1 patients, RIA estimates of PRL did not correlate either with Nb2 BA or with IRMA, while Nb2 BA and IRMA were correlated. In group 2 patients, RIA and Nb2 BA were correlated (r = 0.881; P = 0.02); (5) 24-86% of BB-PRL reacted as immunoglobulin-bound PRL as demonstrated by protein A Sepharose and by SDS-PAGE; (6) a high percentage of BB-PRL (54, 49 and 43%), was found in three of the serum samples obtained from 31 first-degree relatives of patients in group 1. CONCLUSIONS: Macroprolactinaemia must be suspected not only in patients with asymptomatic hyperprolactinaemia but also in women with galactorrhoea and/or menstrual disturbances who have normal responses to PRL stimulating tests. Our results also suggest that the absence of symptoms in these women is not explained by a lower bioactivity of BB-PRL. Instead, we postulate that due to the high molecular weight, BB-PRL does not easily cross the capillary walls. During gel chromatography either a change in the structure of BB-PRL and/or a removal of substances which potentiate the bioactivity of PRL occurs, explaining the lower bioactivity of fractions containing BB-PRL in comparison with the serum. In this study we demonstrated that at least half (range 24-86%) of BB-PRL behaves as an immunoglobulin-bound PRL. Finally, we found that macroprolactinaemia was not genetically transmitted to first-degree relatives in the majority of the cases studied.

Adult↗
PubMed1992

Distribution of a novel peptide in the anterior pituitary, gastric pyloric gland, and pancreatic islets of rat.

We used Western blot and immunohistochemical methods to investigate the biochemical characteristics and cellular distribution of a novel peptide (peptide 23) that was previously shown to be released from anterior pituitary cells of rat in response to growth hormone-releasing hormone. In the pituitary, peptide 23 isolated from intact cells had an Mr of 31,000, whereas that released into culture medium had an Mr of 16,000. Pancreatic islets contained a 19 KD form of the peptide. Immunohistochemically, peptide 23 in the rat pituitary gland was localized in a subpopulation of somatotropes. In pancreatic islets, the peptide was found by triple immunofluorescence labeling to be present in both insulin- and somatostatin-containing cells. In the gastrointestinal tract, peptide 23 was found only in a subpopulation of endocrine cells in the pyloric glands. This subpopulation of cells was found to be entirely separate from those containing either serotonin or somatostatin, and may represent one of the other known or as yet biochemically uncharacterized cell types in this gland. The results suggest that in response to secretagogues in vitro, an altered form of the peptide is secreted from pituitary cells and that an intracellular form of peptide 23 is expressed in some but not all somatotropes, a large proportion of islet cells, and a distinct population of pyloric cells.

Animals↗
PubMed1992

Expression and secretion of galanin during pregnancy in the rat.

The expression of galanin messenger RNA (mRNA) in the pituitary and conceptus of pregnant rats has been studied at various stages of gestation. Using Northern blot analysis and in situ hybridization we have found that high levels of mRNA coding for galanin were detected in the conceptus during early pregnancy. The level of expression in conceptuses increased until day 11-12 after which the levels decreased rapidly. In contrast, in the pituitary galanin mRNA continued to increase throughout pregnancy, especially in the latter half of pregnancy as serum estradiol levels has been reported to be increased. The size of the galanin transcript was the same in the conceptus and pituitary (0.9 kilobase). Expression of this mRNA was confined to the decidua and was first seen at day 5 of pregnancy at a time when implantation swellings were first observed. Galanin antisense probe hybridized strongly to the decidual cells that surround the implantation site. At day 11 of pregnancy the galanin mRNA was found in both the antimesometrial and the mesometrial tissue with the highest concentration in the region lateral to the antimesometrial cells and continued toward the mesometrial cells. Serum galanin levels measured by an RIA using synthetic rat galanin as standard and antisera raised against porcine galanin, exhibited a temporal pattern similar to the pattern of mRNA expression in decidua, with a 7.1-fold increase at day 12 of pregnancy followed by a decline. In summary, decidual cells may differentiate into an endocrine cell during pregnancy. The galanin secreted by these cells, in addition to acting locally in a paracrine/autocrine fashion, may function as a placental hormone with systemic effects on distal target tissues.

Animals↗
PubMed1992

Tissue-specific regulation of vasoactive intestinal peptide messenger ribonucleic acid levels by estrogen in the rat.

The early and chronic effects of 17 beta-estradiol on vasoactive intestinal peptide (VIP) gene expression in rats were examined. Total RNA of four VIP-producing tissues were subjected to Northern blot analysis 15 and 30 min, and 1, 3, 6, and 24 h after a single injection of 17 beta-estradiol (100 micrograms/kg ip). Pituitary, hypothalamus, brain, and ileum VIP messenger RNA (mRNA) levels rose in a time-dependent manner after estrogen treatment. In the pituitary, the increase was maximal at 30-60 min, whereas in the hypothalamus, the increase reached significance only at 3 h but then persisted until at least 24 h. In the brain, a transient increase in VIP mRNA was observed at 30 min, whereas VIP mRNA levels in the ileum responded in a biphasic pattern; the initial early increase was followed by a second elevation occurring at 6 h. A smaller 1-kilobase VIP-related transcript particularly abundant in the pituitary was regulated in parallel with the 1.7-kilobase mature VIP mRNA species. Continuous estrogen stimulation for 7 weeks dramatically increased both mRNA species in the pituitary but did not affect VIP mRNA levels in the other tissues. These data suggest that the regulation of VIP gene expression by transient increases in estrogen levels is rapid and that the pattern of induction is tissue specific.

Animals↗
PubMed1992

Steroids and tissue-specific modulation of galanin gene expression in the male rat reproductive system.

Galanin is a neuropeptide widely distributed throughout the vertebrate neural and endocrine system. Galanin can influence pituitary hormone secretion, intestinal motility, and other biological activities. The precise physiological role of galanin is unknown. We studied the control of galanin gene expression in peripheral organs in the male rat using Northern blot and in situ hybridization techniques. In the adrenals and prostate, galanin mRNA was undetectable in the controls and did not change after the administration of dexamethasone (0.0001-10.0 mg/kg, ip) and diethylstilbestrol (0.1 mg/kg, ip). In the testis, thymus, seminal vesicles, medial basal hypothalamus, and colon, galanin message was detectable, but was not influenced by steroids. On the other hand, dexamethasone (0.5-10.0 mg/kg) was very effective in enhancing galanin expression in the vas deferens and epididymis (4- to 7-fold in the vas deferens), with a peak 6-9 h after the treatment. Diethylstilbestrol (0.1 mg/kg) stimulated galanin mRNA transcription only in the vas deferens (2- to 3-fold), with a peak 1-3 h after the treatment. Dihydrotestosterone treatment (0.2-0.4 mg/kg) was ineffective in all tissues examined. In the vas deferens and seminal vesicles, galanin mRNA has been localized at a cellular level by in situ hybridization. In these tissues only fibroblast-like cells contained the message. These data demonstrate that galanin is expressed in the male rat reproductive system and that steroid hormones participate in the control of galanin gene expression in a tissue- and hormone-specific fashion.

Adrenal Glands↗
PubMed1991

Galanin.

Explore the source record for details and available documents.

Animals↗
PubMed1991

Studies on the regulation and characterization of plasma stanniocalcin in rainbow trout.

Stanniocalcin (STC) is a hormone that is synthesized and secreted by the corpuscles of stannius (CS), endocrine glands that are unique to the bony fishes. The hormone inhibits Ca2+ transport from the aquatic environment into the bloodstream by way of the gills. Previous in vitro studies by our laboratory have shown that STC secretion is positively regulated by Ca2+ in a time- and dose-dependent fashion. In this report, we have examined circulating levels of STC in free-swimming, cannulated rainbow trout and how hormone levels are affected by surgical stress and intra-arterial infusions of mono and divalent cations. In addition, the plasma hormone has been concentrated by immunoaffinity chromatography and characterized by Western blot analysis. The results suggest that the in vivo response of the CS is extremely rapid and Ca(2+)-specific and that STC circulates in multiple molecular weight forms.

Animals↗
PubMed1991

Molecular cloning and expression of rat placental lactogen-Iv, a variant of rPL-I present in late pregnant rat placenta.

Late pregnant rat placenta was found to contain a messenger RNA (mRNA) that encodes an additional member of the prolactin-growth hormone family. This polypeptide was detected by hybridization of complementary DNA (cDNA) for rPL-I to a 1 kilobase mRNA transcript in late pregnant rat placenta. A cDNA clone for the new polypeptide was isolated from a phage lambda-gt10 library containing cDNA synthesized from day 18 rat placental mRNA. Sequencing of the day 18 cDNA clone revealed that it was most closely related structurally to rPL-I and at the amino acid terminal was identical to the rPL-I variant (rPL-Iv). The sequence of rPL-Iv (223 amino acids) is 85% homologous to rPL-I (230 amino acid). There are 71 base pair changes (85% nucleotide homology) between rPL-Iv and rPL-I which are not confined to any specific region of the molecule and which result in 36 amino acid changes. In vitro translation of rPL-Iv mRNA produced by transcription of the cDNA template yielded a 26 kilodalton polypeptide, the size of the expected precursor protein. In situ hybridization studies indicated that mRNA for rPL-Iv was present primarily in cytotrophoblasts of the basal zone as early as day 15 of gestation with some hybridization in a few giant cells as well.

Amino Acid Sequence↗
PubMed1991

Galanin immunoreactivity in neuroendocrine tumors.

We investigated immunoreactivity for galanin, a 29-amino acid peptide, in formalin-fixed, paraffin-embedded sections of 123 neuroendocrine tumors. Galanin-immunoreactive cells were found in one of 12 hypothalamic gangliocytomas, nine of 18 adrenal pheochromocytomas, nine of 14 pituitary corticotroph adenomas, and one of two thymic endocrine tumors. In pheochromocytomas, galanin-immunoreactive cells were seen either singly or in clusters. In corticotroph adenomas, many tumor cells were positive for galanin, indicating colocalization of corticotropin and galanin in the same tumor cells. No galanin-immunoreactive cells were noted in four extra-adrenal paragangliomas; 10 medullary carcinomas of the thyroid; 35 endocrine tumors arising in the lung, pancreas, and gastrointestinal tract; and 28 pituitary adenomas composed of cells other than corticotrophs. In nontumorous counterparts of these neuroendocrine tumors, galanin immunoreactivity was observed in nerve cells of the hypothalamus, nerve fibers of the duodenum, and adenohypophyseal cells corresponding to corticotrophs. These findings indicate that galanin expression in neuroendocrine tumors is uncommon and restricted to some tumor types.

Endocrine Gland Neoplasms↗
PubMed1991

Prolactin deficiency in rheumatoid arthritis.

Prolactin and growth hormone were determined from the sera of 48 patients with rheumatoid arthritis (RA) and 23 controls by radioimmunoassay and by the Nb2 lymphoma proliferation bioassay. A highly significant deficiency was found in the bioactivity of circulating prolactin (PRL) in patients with RA, whereas immunoactive PRL was near normal. Only age matched male patients showed significantly lower serum PRL levels by radioimmunoassay. Patients with RA with anemia and high reticulocyte counts had bioactivity of PRL elevated and those with anemia and low reticulocyte counts had a decreased bioactivity of PRL when compared to patients without anemia. Prolactin isolated from the sera of 5 patients with RA showed decreased bioactivity in comparison with PRL separated from 5 sex matched controls. Serum factors capable of enhancing or inhibiting the response of Nb2 cells to ovine PRL were also discovered. Our results indicate that RA is associated with PRL deficiency.

Anemia↗
PubMed1990

Human prolactin gene expression. The use of an alternative noncoding exon in decidua and the IM-9-P3 lymphoblast cell line.

The prolactin (PRL) gene is normally expressed in the anterior pituitary lactotrope and the decidualized stromal cell of the human endometrium. We have recently described the ectopic expression of the human PRL gene in a B-lymphoblastoid cell line, IM-9-P. The IM-9-P and decidual PRL mRNAs are approximately 150 nucleotides longer than the pituitary transcript. The protein coding sequence of the IM-9-P and decidual PRL cDNAs is identical to the pituitary PRL message, and the 3'-untranslated region (UTR) exhibited a 7-14-nucleotide elongation. The 5'-UTR of IM-9-P and decidual PRL cDNAs revealed an extension of 41 base pairs upstream of the normal transcription start site for the human pituitary PRL gene. This is preceded by an additional sequence that is not homologous to the DNA found 5' to the pituitary PRL cap site. Decidual and IM-9-P PRL mRNAs possess identical 5' ends having 5'-UTRs of 83-263 nucleotides longer than that of the pituitary mRNA. The decidual/IM-9-P-specific segment of the 5'-UTR is located as a new 5'-noncoding exon 5-7 kilobase pairs upstream of the human pituitary PRL gene, exon 1. The clonal IM-9-P3 cell line provides a unique and easily manageable resource with which to study decidual specific PRL gene transcription.

Base Sequence↗
PubMed1990

Expression of insulin-like growth factor-I and insulin-like growth factor-binding protein-1 in the rat uterus during decidualization.

Decidualization of the uterus involves proliferation and differentiation of uterine cells. The effects of decidualization on uterine expression of insulin-like growth factor-I (IGF-I) and IGF-binding protein-1 (IGFBP-1) have been examined in the hypophysectomized-ovariectomized (hypox-ovx) rat and the pituitary-intact (ovx) rat. Decidualization was induced by uterine stimulation of animals treated with a combination of 17 beta-estradiol and progesterone. The patterns of change in uterine IGF-I mRNA and IGFBP-1 mRNA abundance were similar to hypox-ovx rats, hypox-ovx rats replaced with GH and T4, and ovx rats. The changes in IGF-I mRNA abundance were temporally related to 17 beta-estradiol injections. IGFBP-1 mRNA was undetectable early in the decidualization process and reached maximal levels on day 6. Mechanical separation of the deciduoma tissue from the underlying myometrium revealed that the deciduoma tissue was depleted in IGF-I mRNA, while the majority of the IGFBP-1 was located in the deciduoma tissue. The in situ hybridization technique was used to localize IGF-I and IGFBP-1 mRNA in the decidualized uterus. The majority of the IGF-I expression was localized to the outer stroma and smooth muscle cell layer, whereas IGFBP-1 mRNA was detected in uterine epithelial cells and stromal glands. These experiments demonstrated that uterine IGF-I and IGFBP-1 expression during the process of decidualization are pituitary independent. Furthermore, our observations support the hypothesis that the expression of IGFBP-1, a protein capable of inhibiting the mitogenic activity of IGF-I, in deciduoma tissue may inhibit paracrine IGF-1 actin and allow for the differentiation of stromal tissue.

Animals↗
PubMed1990

Expression of rat prolactin-like protein B in deciduoma of pseudopregnant rat and in decidua during early pregnancy.

The rat PRL-like protein-B (rPLP-B) complementary DNA (cDNA), originally cloned from a late term placental library, hybridizes to transcripts in the deciduoma tissue artificially produced in pseudopregnant rats. The expression of rPLP-B in deciduoma is first observed 48 h (pseudopregnancy day 7) after the deciduogenic stimulus and increases to a maximum by 96-120 h (pseudopregnancy day 9-10). In situ hybridization studies show that rPLP-B hybridizes specifically to the antimesometrial cells of deciduoma tissue in day 9 pseudopregnant rats and to the homologous cells of the decidua that surround the embryo-trophoblastic structure at day 9 of pregnancy. A temporal study on the expression of rPLP-B during pregnancy shows that rPLP-B is concomitantly expressed by the decidual cells of maternal origin and the cytotrophoblast of fetal origin around day 13 of pregnancy.

Animals↗