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PubMed1987

Extrahypothalamic brain prolactin: characterization and evidence for independence from pituitary prolactin.

Prompted by reports of immunohistochemical localization of a prolactin-like immunoreactivity (PLI) within the rat brain, a study was undertaken to define the immunologic and biologic characteristics of this material in extrahypothalamic regions of the rat brain. Ninety-seven percent recovery of rat prolactin standard, added to homogenates of brain parts, insured that neuronal tissue did not interfere with the radioimmunoassay for rat prolactin. PLI was consistently found in the cerebellum, thalamus, brainstem (pons-medulla), hippocampus, cerebral cortex and caudate. Examination of the elution profile of each of the extrahypothalamic brain parts from Sephadex G-75 columns showed that, although a small amount of brain PLI elutes in the vicinity of the anterior pituitary prolactin marker, the bulk of brain-based PLI migrates with the void volume and as late eluting, low molecular weight material. While increasing amounts of brain extracts progressively displaced more 125I-prolactin from antibody binding, the displacement curve was not parallel to that produced by the addition of increasing amounts of anterior pituitary prolactin standards of rat origin. Extracts of various brain parts from hypophysectomized animals, analyzed for biologic activity in the Nb2 lymphoma cell assay, revealed prolactin-like bioactivity, but the bioactivity/immunoreactivity ratio for some of the brain parts was significantly lower than that for pituitary prolactin. Hypophysectomy, which led to the expected fall in serum prolactin to undetectable levels, and restraint stress, which resulted in a statistically significant 4-fold rise in serum prolactin, caused no change in prolactin concentrations in extrahypothalamic brain parts, indicating that brain PLI is regulated independently of pituitary prolactin and of circulating serum prolactin levels.

Animals↗
PubMed1985

Prolactin secretion and biological activity in females with galactorrhoea and normal circulating prolactin concentrations at rest.

Prolactin secretion and biological activity have been investigated in 20 females with persistent idiopathic galactorrhoea who had normal resting serum prolactin levels at presentation. Results were compared with those in 34 normal controls. Hyperprolactinaemia, which was persistent in one and intermittent in the other, developed in two patients over an observation period of 1.5 to 8.5 years. Resting prolactin levels stayed normal in the remaining eighteen who were further investigated. Menstruation was disordered in only six of the 18, while ovulation occurred (serum progesterone greater than 20 nmol/l) in all seven patients who were studied over a 5 week period. Serum prolactin concentrations over 24 h were similar in patients and controls (24 h mean +/- SEM prolactin, 288 +/- 36 mU/l, patients, n = 7; 291 +/- 21 mU/l, controls, n = 9) as were prolactin levels estimated twice weekly for 5 weeks. Prolactin responses to thyrotrophin-releasing hormone, 200 micrograms (at 20 min, 2417 +/- 658 mU/l, patients, n = 7; 2113 +/- 424 mU/l, controls, n = 8), the dopamine antagonist, domperidone, 10 mg (at 30 min, 5949 +/- 536 mU/l, patients, n = 7; 5858 +/- 460 mU/l, controls, n = 8) and insulin-induced hypoglycaemia (at 60 min, 1441 +/- 551 mU/l, patients, n = 7; 1298 +/- 183 mU/l, controls, n = 7) were similar in patients and controls. Two different radioimmunoassays using two different antisera gave similar estimates of serum prolactin levels and prolactin bioactivity in serum was normal in an in-vitro bioassay based on the ability of prolactin to stimulate proliferation of Nb2 node rat lymphoma cells (basal bioassayable prolactin, patients 355 +/- 43 mU/l, n = 10; controls 348 +/- 64 mU/l, n = 7). Metabolic abnormalities similar to those previously noted in hyperprolactinaemia were observed in the patients' 24 h profiles. These included mild hyperglycaemia (24 h mean +/- SEM glucose, 5.47 +/- 0.08 mmol/l, patients; 5.05 +/- 0.14 mmol/l, controls; P less than 0.05) and elevations in circulating lactate, pyruvate and alanine. Blood glycerol was decreased (24 h mean +/- SEM, 0.044 +/- 0.004 versus 0.058 +/- 0.004 mmol/l, P less than 0.05). In the majority of patients with idiopathic galactorrhoea, prolactin concentrations, regulation of secretion and bioactivity in vitro are normal. The galactorrhoea and metabolic abnormalities suggest increased tissue sensitivity to the lactogenic and metabolic actions of prolactin, while ovarian cyclical function is relatively spared.

Adult↗
PubMed1976

Prolactin inhibition test with L-dopa: decrease and restoration of plasma prolactin levels in the rat by a peripheral process.

L-DOPA, within 30 min after administration, induced a highly significant decrease of plasma prolactin levels (phase 1) in a number of groups of rats, differing in age and/or endocrine status, apparently by direct inhibition of prolactin release from the pituitary. Three hours after administration of L-DOPA these low plasma prolactin concentrations in treated animals had increased (phase 2) and did not differ significantly from levels in control animals, indicating that the effect of L-DOPA on plasma prolactin levels is only of short duration. During this process some interesting phenomena were observed, especially in the animals treated with oestrone. The elimination rate of prolactin from plasma was very high (t 1/2 = 2.8 min), as indicated by decreasing concentrations of the hormone during phase 1. Pituitary prolactin content did not change during phase 1, suggesting that prolactin synthesis was also stopped. Notwithstanding the high elimination rate, plasma prolactin regained initial concentrations in phase 2, suggesting release of a substantial part of the pituitary prolactin content. The latter,however, remained constant during the whole experiment (i.e. before L-DOPA administration and during phase 1 as well as phase 2). The results suggested another working mechanism of L-DOPA in decreasing plasma prolactin levels, namely by stimulating the uptake of this hormone in the periphery. After the effect of L-DOPA had ceased, most of the prolactin from the periphery returned into the bloodstream, causing a rapid restoration of plasma prolactin levels without substantial release from the pituitary. The nature of the processes responsible for the peripheral uptake of prolactin is discussed.

Animals↗
PubMed2001

Restriction of fetal growth has a differential impact on fetal prolactin and prolactin receptor mRNA expression.

Prolactin is present in the fetal circulation and prolactin receptors are expressed in a wide range of fetal tissues. The factors which regulate the synthesis and secretion of prolactin, and the expression of its receptors before birth, are poorly understood. We have investigated whether experimental restriction of placental growth in the sheep has an impact on the prolactin axis in the growth restricted fetus. The majority of uterine endometrial caruncles were removed before pregnancy in 10 ewes (placental restriction; PR group). Placental, fetal liver and kidney weights were reduced in the PR compared to the control group (n = 10). The ratio of fetal prolactin mRNA : 18S rRNA was significantly lower (P < 0.01) in the PR group (1.83 +/- 0.45, n = 6) than in the control group (4.11 +/- 0.54, n = 6). The ratio of prolactin mRNA : 18S rRNA in the fetal pituitary was positively correlated with fetal and with placental weight. Using stepwise linear regression, it was determined that the level of fetal prolactin mRNA : 18S rRNA expression was best described (as judged by the maximum adjusted R2) by prolactin mRNA: 18 S rRNA = - 3.0378 + 0.17 PO2 + 2.772 glucose (adjusted R2 = 0.765, F = 17.53, P < 0.001). Fetal plasma prolactin concentrations were significantly reduced (P < 0.05) in the PR group compared to control animals between 109 and 141 days gestation. Fetal prolactin receptor (PRLR) mRNA transcripts encoding long (PRLR1) and short forms (PRLR2) of PRLR were present in the liver and kidney of animals in the PR and control groups at 140-141 days gestation. PR did not alter the levels of PRLR1 or PRLR2 mRNA in the fetal liver or kidney. The suppression of the synthesis and secretion of prolactin in the growth restricted fetus may limit the action of prolactin on the growth and metabolism of key fetal organs during suboptimal intrauterine conditions

Animals↗
PubMed1994

Negative cooperativity in the prolactin-receptor interaction in the rabbit mammary gland: action of high prolactin concentration.

The concentration of serum prolactin in the lactating mother is elevated by milking, and the dissociation of prolactin from the receptor is accelerated by the presence of prolactin in vitro. The interaction of prolactin at high concentrations with the receptor was examined using lactating rabbit mammary microsomes. At low concentrations of prolactin, the Scatchard plots were linear. At concentrations > 30 ng/ml, however, the slope of the Scatchard plot line changed. The Hill coefficient decreased from 1.09 to .77 or from .80 to .65 as prolactin concentrations increased. When a receptor preloaded with prolactin was utilized, prolactin at concentrations > 20 ng/ml associated with the receptor in a concentration-dependent manner. The Hill coefficient of this reaction was .70. The receptor remained intact for re-association after prolactin-induced dissociation. These data indicate that, because of the presence of negative cooperativity, prolactin at exceedingly high concentrations greatly accelerates the prolactin-binding reaction. The elevation of serum prolactin induced by milking may be important in the maintenance of active milk synthesis.

Animals↗
PubMed1985

The relationship between serum prolactin and immunocytochemical staining for prolactin in patients with pituitary macroadenomas.

We have studied the relationship between mean pretreatment levels of serum prolactin and the presence of positive immunohistochemical staining for prolactin in the pituitary tumours of 55 patients. Pretreatment serum prolactin was significantly higher in patients with tumours showing many prolactin immunostaining cells than in those with none (P less than 0.001). When the pretreatment serum prolactin exceeded 6000 mU/l, the tumours contained over 90% of prolactin positive cells; one patient was an exception who had received long-term high dose bromocriptine therapy, and her tumour showed only occasional cells with positive staining. When the pretreatment serum prolactin level was under 2500 mU/l, a tumour was found which showed either no cells or fewer than 1% of cells which stained for prolactin. There was no significant difference in pretreatment serum prolactin levels between 11 patients with craniopharyngiomas and 34 patients with pituitary macroadenomas showing no prolactin immunostaining. Seventy-one percent (32) of the 45 patients with craniopharyngiomas or tumours with negative immunostaining for prolactin, had raised pretreatment serum prolactin levels (above 360 mU/l) although this was usually only slightly elevated; the levels exceeded 2500 mU/l in six (13%) of them (two craniopharyngiomas, four pituitary tumours) but in none did the levels exceed 6000 mU/l. Four of the 55 pituitary tumours showed occasional cells (less than 1%) that stained positively for growth hormone. In none of the patients with these tumours was there evidence of acromegaly or pathologically elevated circulating growth hormone levels.

Adenoma↗
PubMed1990

Characterization of monoclonal antibodies against ovine prolactin: suitability for use in immunocytochemical analysis of rat prolactin.

The aim of this study was to identify a monoclonal antibody (MAb) suitable for use in the immunocytochemical localization of prolactin in rat tissues. We took advantage of the conservation of certain amino acid sequences in prolactin among species by examining the crossreactivity patterns of five MAb, originally generated to ovine prolactin, with rat prolactin by enzyme-linked immunoassay (ELISA), Western blot analysis, and immunocytochemistry. Two of five antibodies (17D9 and 6F11) showed reactivity with 100 ng of immobilized rat prolactin (NIH RP-3) by ELISA, 6F11 reacting more strongly than 17D9. Only 6F11 reacted with prolactin in lysates of GH4C1 rat pituitary tumor cells by Western blot analysis. When we examined the crossreactivity of the MAb with rat prolactin in monolayer cultures of GH4C1 cells by indirect immunofluorescence, we found that both 17D9 and 6F11 reacted strongly with the cultures. The distribution of staining with 17D9 or 6F11 was coincident with staining with a polyclonal antiserum to rat prolactin. Preabsorption of the antibodies with a 20-fold excess of purified rat prolactin abolished the staining of GH4C1 cell cultures with either antibody. Therefore, we have selected from a series of MAb raised to ovine prolactin two antibodies (17D9 and 6F11) that react specifically with rat prolactin in immunocytochemical studies, whereas 6F11 also reacts strongly with rat prolactin by ELISA and Western blot analysis.

Animals↗
PubMed1976

Relationship between prolactin secretion and hypothalamic prolactin releasing factor in pregnant and puerperium rats.

The present study attempted to elucidate stimulatory factor(s) in the rat hypothalamus which controls prolactin secretion from the anterior pituitary. Rat serum prolactin was elevated so much in late pregnancy that we prepared the hypothalamic extract of late pregnant rats. Prolactin levels in serum and pituitary by radioimmunoassay. After injection of this extract into a lactating rat 48-60 hr after delivery, the serum prolactin level was elevated significantly one to four hr later and the pituitary prolactin level declined two hr later. On the other hand, the hypothalamic extract of normal female rats prepared in a similar manner inhibited prolactin secretion from the anterior pituitary in the lactating rat as described by other authors. These data indicate that the prolactin releasing factor may consist in the hypothalamus of late pregnant rat, and be predominant over the prolactin inhibiting factor during late pregnancy. Prolactin secretion was also investigated in lactating and non-lactating puerperium rats. Prolactin in serum and pituitary declined with days after delivery in non-lactating rats, but not in lactating rats. The presumed factor for such prolactin release in lactating rats is considered to be the prolactin releasing factor.

Animals↗
PubMed1983

Degradation of 125I-labelled prolactin in the rabbit: effect of nephrectomy and prolactin infusion.

Hyperprolactinaemia in patients with chronic renal disease undergoing dialysis has prompted the investigation of the relative roles of liver and kidney in the degradation of prolactin. Male rabbits were acutely nephrectomized, and compared with intact animals with or without prolactin infusion. Prolactin degradation was followed after intravenous injection of 125I-labelled ovine prolactin. Measurements were made of peptide-bound 125I and 125I-labelled degradation products in plasma, liver, kidney, bile, urine and muscle and total thyroid radioactivity. A significant (P less than 0.01) reduction in the metabolic clearance rate of 125I-labelled prolactin was observed due to nephrectomy, with double the accumulation of 125I-labelled peptides in the livers in this group. Prolactin infusion of nephrectomized animals had a further and larger effect than nephrectomy alone on prolactin degradation. Metabolic clearance rate significantly (P less than 0.01) decreased from 5.5 ml/min per kg in nephrectomized rabbits to 0.8 ml/min per kg with prolactin infusion. The accumulation of 125I-labelled prolactin degradation products in the blood was significantly (P less than 0.01) lower in this group of animals and the amount of peptide-bound 125I in plasma at 60 min after 125I-labelled prolactin administration was significantly (P less than 0.01) higher. Liver degradation of prolactin in the absence of exogenous hormone appears to be sufficient to maintain an approximately normal half-life for prolactin in plasma (intact t 1/2 = 6.8 min; nephrectomized t 1/2 = 8.5 min).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1980

Dopaminergic inhibition of prolactin synthesis and prolactin messenger RNA accumulation in cultured pituitary cells.

Prolactin synthesis was investigated in monolayer cultures of dispersed pituitary cells maintained in defined medium. Electrophoresis of cell extracts from cultures labeled with [35S]methionine demonstrated that treatment with the dopaminergic drug, ergocryptine, specifically inhibited prolactin synthesis. Analysis of the time course of ergocryptine effects demonstrated that prolactin synthesis decreased sharply after 1 to 2 days of treatment and appeared to reach a new level of 26 to 28% of control values after 4 to 6 days of treatment. The concentration of ergocryptine which produced half-maximal inhibition of prolactin synthesis was about 0.3 nM. The inhibition of prolactin synthesis produced by ergoctryptine treatment was reversed by removal of the ergocryptine. Dopamine, ergocryptine, and bromoergocryptine (also a dopamine agonist) all inhibited prolactin synthesis while epinephrine and norepinephrine had little effect. The concentration of prolactin mRNA in cultured cells was assayed by hybridization of total cell RNA to prolactin cDNA. Analysis of cultures treated either for varying times or with varying doses of ergocryptine demonstrated that there was a close correspondence between the inhibition of prolactin synthesis and the inhibition of prolactin mRNA levels. These studies demonstrate the ability of dopaminergic stimulation to specifically inhibit prolactin synthesis and to decrease prolactin mRNA levels in primary cultures of pituitary cells maintained in defined medium.

Animals↗
PubMed1984

Prolactin regulation of cryptic prolactin receptors in cultured rat mammary tumor cells.

Rat mammary tumors contain a unique class of cryptic cell-surface prolactin receptors that can be unmasked by depleting the cells of energy. These cryptic receptors, which are found in mammary tumors and nonlactating normal mammary cells but not in differentiated mammary tissue, are continuously inserted and rapidly removed from the cell surface. In this report we demonstrate that prolactin regulates the level of cryptic receptors. Treatment of primary cultures of rat mammary tumor cells with prolactin at concentrations between 0.1 and 0.5 ng/ml caused cryptic receptor levels to increase within 24 h, and this increase was maintained for up to 6 days. At prolactin concentrations of 10-50 ng/ml, receptor levels were the same as in cells incubated without hormone, while a decrease in the steady-state level of cryptic receptors was induced within 24 h by 100-500 ng prolactin/ml. Concentrations of 1,000-5,000 ng prolactin/ml caused a rapid, dose-dependent down regulation of cryptic receptor sites. Down regulation at 5,000 ng prolactin/ml was (1) complete (84 +/- 5% reduction) in 1 h; (2) specific for lactogenic hormones; (3) completely reversed within 10 h after prolactin removal; (4) energy dependent; and (5) not blocked by the cytoskeleton active agents cytochalasin B and colchicine or by NH4Cl, which inhibits hormone degradation. We conclude that rat mammary tumor cells have the capacity to auto-regulate cryptic prolactin receptors, a property that supports our notion that such receptors play a role in regulating prolactin responsiveness. The observed pattern of cryptic receptor autoregulation in response to prolactin concentration and time of exposure suggests that a pool of cryptic sites provides these cells with the capacity to respond to prolactin concentrations from pg to microgram/ml, a range well beyond the Kd for the receptor itself. Since prolactin receptors in mammary tumors are not down regulated unless prolactin concentrations are well beyond the saturation point, these cells may have a selective growth advantage over cells in normal mammary tissue.

Animals↗
PubMed2005

Mathematical modelling of prolactin-receptor interaction and the corollary for prolactin receptor gene expression in skin.

A mathematical model of prolactin regulating its own receptors was developed, and compared with experimental data on a qualitative level. The model incorporates the kinetics of prolactin-receptor interactions and subsequent signalling by prolactin-receptor dimers to regulate the production of receptor mRNA and hence the receptor population. The model relates changes in plasma prolactin concentration to prolactin receptor (PRLR) gene expression, and can be used for predictive purposes. The cell signalling that leads to the activation of target genes, and the mechanisms for regulation of transcription, were treated empirically in the model. The model's parameters were adjusted so that model simulations agreed with experimentally observed responses to administration of prolactin in sheep. In particular, the model correctly predicts insensitivity of receptor mRNA regulation to a series of subcutaneous injections of prolactin, versus sensitivity to prolonged infusion of prolactin. In the latter case, response was an acute down-regulation followed by a prolonged up-regulation of mRNA, with the magnitude of the up-regulation increasing with the duration of infusion period. The model demonstrates the feasibility of predicting the in vivo response of prolactin target genes to external manipulation of plasma prolactin, and could provide a useful tool for identifying optimal prolactin treatments for desirable outcomes.

Animals↗
PubMed1980

Immunocytochemical analysis of prolactin production by monolayer cultures of GH3 rat anterior pituitary tumor cells: II. Variation in prolactin content of individual cell colonies, and dynamics of stimulation with thyrotropin-releasing hormone (TRH).

The preceeding report (Hoyt and Tashjian, '80) correlates immunocytochemical localizations and mean prolactin concentrations in GH3 monolayers maximally stimulated with TRH; the present does so over the duration of TRH treatment. Low density seeding produced numerous discrete GH3 cell colonies. Cultures were harvested 1/2, 4, 12, 24, 72, and 144 hr after administration of TRH (50 ng/ml) or saline (control). All cells (42,658 total) in at least 10 microscopic fields/monolayer, 1 cell colony/field, were classed as unstained, heavily (H), moderately (M), or weakly (W) stained for prolactin. In controls, colonies contained 51-91 prolactin-positive cells/100 of population. Colonies with few positive cells had many more W than M cells, and the reverse was true in those with many positive cells. In all colonies, the effect of TRH was biphasic, Initial (0-4 hr) release of prolactin was overlapped, beginning at 3-4 hr, by a progressive increase of intracellular hormone. After 144 hr, the prolactin content of treated cultures had increased to 190% of control, and prolactin-positive cells were more numerous (114% of control). These increases were lower than those reported in the preceeding paper after 48 hr of TRH treatment, when intracellular prolactin equalled 450% of control and positive cells equalled 129% of control. These inconsistencies reflect differences in the control level of prolactin production rather than in the absolute effects of TRH, which were virtually identical in the successive experiments. We conclude that: 1) TRH acts to alter hormone production in cells already making prolactin; 2) TRH increases somewhat the number of prolactin-containing cells; 3) the relative contribution of such "new" cells to increased hormone output depends on the basal level of prolactin production, which differs among individual GH3 cell colonies and varies over time in culture. This diversity does not diminish the usefulness of GH3 cells as biochemical models of hormone biosynthesis. It does hinder their valid morphological evaluation, which apparently must be controlled as carefully as biochemical experiments and should include immunocytochemical localizations, at least for the hormone at issue.

Animals↗
PubMed1982

Age-related changes in prolactin cell percentage and serum prolactin levels in intact and neonatally gonadectomized male and female rats.

Electron microscopically the percentages of various pituitary cell types were calculated at 30 and 90 days of age. Prolactin cell percentage was more at 90 days of age than at 30 days in both intact male and female rats. No sexual difference was observed in the percentage of prolactin cells at 30 days of age, but at 90 days female pituitaries contained more numerous prolactin cells than males ones. Neonatal ovariectomy did not affect the prolactin cell percentage at 30 days of age, while it lowered the percentage at 90 days. Neonatal orchidectomy did not affect the prolactin cell percentage at both 30 and 90 days of age. Mitotic prolactin cells were more frequently observed in intact female rats at estrus than in intact male rats at 90 days of age. These results shown the presence of the sexual difference in the proliferation of prolactin cells. Serum prolactin levels increased with age in intact male and female rats. In neonatally gonadectomized male and female rats the serum prolactin levels failed to increase at 60 and 90 days of age. In general conclusion, the changes in serum prolactin levels are in line with the changes in prolactin cell population during postnatal development.

Age Factors↗
PubMed1978

Mammary gland prolactin receptor and pituitary prolactin secretion in lactating mice with different lactational performance.

SHN female mice, a high mammary tumour strain, are superior to SLN, a low mammary tumour strain, in lactational performance. Mammary gland prolactin receptor and pituitary prolactin secretion during lactation were compared between these strains. The binding activity, the number of receptor sites per mg tissue and the association constant were measured by the in vitro incubation of mammary gland slices with 125I-labelled bovine prolactin, and the pituitary and plasma levels of prolactin were assayed by homologous radioimmunoassay. There was only a slight difference between strains in any of the parameters for prolactin receptor and for prolactin secretion on either day 4 or day 9 of the first lactation. Almost all the correlation coefficients between each parameter for prolactin receptor and the pituitary or plasma level of prolactin were not statistically significant. These findings suggest that any parameter for prolactin examined in this study is not always directly indicative of lactational performance and further show that the individual variation in the pituitary prolactin secretion during lactation is not so great as to alter the prolactin receptor.

Animals↗
PubMed1991

Somatostatin partially impedes the stimulatory effects of thyrotrophin-releasing hormone and dibutyryl cyclic AMP on prolactin release: prolactin release through multiple routes.

Patterns of prolactin release were examined using stimulating and inhibiting agents. Primary cultured pituitary cells primed with oestrogens were used for perifusion experiments. TRH (100 nmol/l) increased the peak prolactin concentration to 360% of the basal concentration, while TRH, under inhibition by 1 nmol somatostatin/l, raised the peak prolactin concentration to 185% of the basal levels. When the somatostatin concentration was increased to 10, 100 and 1000 nmol/l, TRH still stimulated prolactin release to 128%, 121% and 140% respectively, indicating that concentrations of somatostatin of 10 nmol/l or higher did not further suppress the stimulatory effect of TRH. TRH (1 mumol/l) stimulated prolactin release under the influence of 0 (control), 1, 10, 100 and 1000 nmol dopamine/l (plus 0.1 mmol ascorbic acid/l) to 394, 394, 241, 73 and 68% of the basal concentration respectively, showing that the dopamine concentrations and peak prolactin concentrations induced by TRH have an inverse linear relationship in the range 1-100 nmol dopamine/l. The stimulatory effect of dibutyryl cyclic AMP (dbcAMP) on prolactin release was also tested. The relationship between dbcAMP and somatostatin was similar to that between TRH and somatostatin. When adenohypophyses of male rats were used for perifusion experiments, somatostatin (100 nmol/l) did not inhibit basal prolactin release from the fresh male pituitary in contrast with the primary cultured pituitary cells, but dopamine (1 mumol/l) effectively inhibited prolactin release. In conclusion, (1) oestrogen converts the somatostatin-insensitive route into a somatostatin-sensitive route for basal prolactin release, (2) TRH-induced prolactin release passes through both somatostatin-sensitive and -insensitive routes, (3) dopamine blocks both somatostatin-sensitive and -insensitive routes and (4) cAMP activates both somatostatin-sensitive and -insensitive routes.

Animals↗
PubMed1993

Prolactin receptor expression in the gastrointestinal tract: characterization of the prolactin receptor of gastric mucosa.

There is evidence that prolactin (PRL) influences gastrointestinal function. However, the sites at which prolactin exerts these effects are not known. A monoclonal antibody was therefore generated against the rabbit mammary gland prolactin receptor (MAb 218) and used to study the distribution of the prolactin receptor in the rabbit gastrointestinal tract (GIT) by immunohistochemistry. MAb 218 is an IgG1 kappa-precipitating antibody which precipitates major affinity cross-linked mammary gland prolactin receptor subunits of molecular masses 45 and 80 kDa. It has an affinity of 0.8 x 10(9) mol/l for the prolactin receptor and does not react with GH or insulin receptors in precipitation assays. MAb 218 immunoreactivity was observed in classical prolactin target cells such as mammary gland epithelium, and this immunoreactivity was abolished by preincubation of MAb 218 with purified prolactin receptor but not by preincubation with purified GH receptor. In the GIT, the most intense immunoreactivity was associated with the oesophageal epithelium, chief (zymogenic) cells of the fundic mucosa, pancreatic islets of Langerhans and surface epithelial cells of the duodenum and jejunum. Other specific elements of the GIT were immunoreactive at lower levels or were immunonegative. No immunoreactivity was observed in these locations with a control monoclonal antibody (MAb 50.8) of identical isotype to 218. To support the immunohistochemical findings, rabbit gastric mucosal membranes were used to show the presence of lactogen-specific binding. Scatchard analysis of 125I-labelled human GH binding to the gastric mucosal membranes with rat prolactin as displacing ligand yielded an affinity constant (Ka) of 1.0 +/- 0.2 x 10(9) mol/l with a capacity of 3.5 +/- 0.4 fmol/mg protein. Affinity cross-linking and sodium dodecyl sulphate-polyacrylamide gel electrophoresis of the gastric receptor revealed lactogenic hormone-binding subunits of molecular masses 43, 68 and 83 kDa. The 68 kDa subunit was not seen in rabbit mammary gland or ovarian tissue, and may be unique to gastric mucosa. In conclusion, we have demonstrated the presence of a high affinity lactogenic receptor in specific epithelial cell subpopulations of the GIT. This localization of the prolactin receptor in the GIT will assist in further functional assignment of prolactin to gastrointestinal physiology.

Animals↗