Neurophysin stimulates prolactin release from primary cultured rat pituitary cells

Shin, Seon H.; Heisler, Ryan L.; Lee, C. S.-S.

doi:10.1677/joe.0.1440225

Cited by 7 publications

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed this is also the case for other invertebrate neuropeptide precursor-related peptides such as adipokinetic hormone precursor-related peptides (APRPs) (Fischer-Lougheed et al 1993;Hekimi and O'Shea 1989), and for vertebrate examples such as the neurophysins (Ando et al 1988; Is crustacean hyperglycaemic hormone precursor-related peptide a circulating neurohormone in crabs? Shin et al 1995) and insulin intrachain connecting peptide (Wahren et al 1996). Accordingly, a first step towards identification of possible functions for CPRP would be to describe neuroanatomical architecture, in comparison with cHH, and release patterns of both peptides, in vitro and in vivo, to determine: (a) whether both peptides are co-released, (b) that CPRP circulates in the haemolymph, and (c) the clearance dynamics of CPRP in relation to cHH.…”

Section: Introductionmentioning

confidence: 99%

Is crustacean hyperglycaemic hormone precursor-related peptide a circulating neurohormone in crabs?

Wilcockson

Chung

Webster

2002

Cell and Tissue Research

View full text Add to dashboard Cite

Sites of synthesis and release patterns of crustacean hyperglycaemic hormone precursor-related peptide (CPRP) were investigated with those of crustacean hyperglycaemic hormone (cHH), in order to determine whether this precursor-related peptide satisfies certain criteria necessary for its definition as a secretable, circulating hormone. Using the edible crab, Cancer pagurus, sites of CPRP synthesis were determined by immunohistochemistry and release patterns of both peptides were determined in vivo and in vitro by radioimmunoassay of haemolymph and eyestalk superfusates. Both peptides were co-released from sinus glands (SGs) following potassium-evoked depolarization of isolated eyestalk preparations. However, stress-evoked in vivo release resulted in apparent non-stoichiometric circulating peptide profiles. This phenomenon is explained by notable differences in clearance rates of the peptides in haemolymph. In contrast to cHH, CPRP is very slowly degraded in vivo. Although CPRP is clearly a circulating peptide, whose release is concomitant with that of cHH, physiologically pertinent roles for this molecule remain to be discovered.

show abstract

Section: Introductionmentioning

confidence: 99%

Is crustacean hyperglycaemic hormone precursor-related peptide a circulating neurohormone in crabs?

Wilcockson

Chung

Webster

2002

Cell and Tissue Research

View full text Add to dashboard Cite

show abstract

“…Neurophysin 1 is the carrier protein of oxytocin, and neurophysin 2 is the carrier protein of vasopressin. Because the two neurohypophysial hormones are packaged together with neurophysin in secretory granules, a neurophysin is also released when a neurohypophysial hormone is released [ 39 ]. In avian species, vasopressin and oxytocin are replaced by arginine vasotocin (AVT) and mesotocin (MT), respectively, and they have also two types of neurophysins associated with the corresponding precursors [ 40 , 41 ].…”

Section: Discussionmentioning

confidence: 99%

Comparative proteomic analysis of pituitary glands from Huoyan geese between pre-laying and laying periods using an iTRAQ-based approach

Cao

Xing

et al. 2017

PLoS ONE

View full text Add to dashboard Cite

In this study, we performed a comprehensive evaluation of the proteomic profile of the pituitary gland of the Huoyan goose during the laying period compared to the pre-laying period using an iTRAQ-based approach. Protein samples were prepared from pituitary gland tissues of nine pre-laying period and nine laying period geese. Then the protein samples from three randomly selected geese within each period were pooled in equal amounts to generate one biological sample pool. We identified 684 differentially expressed proteins, including 418 up-regulated and 266 down-regulated proteins. GO annotation and KEGG pathway analyses of these proteins were conducted. Some of these proteins were found to be associated with hormone and neurotransmitter secretion and transport, neuropeptide signalling and GnRH signalling pathways, among others. Subsequently, the modification of the abundance of three proteins (prolactin, chromogranin-A and ITPR3) was verified using western blotting. Our results will provide a new source for mining genes and gene products related to the egg-laying performance of Huoyan geese, and may provide important information for the conservation and utilization of local goose breeds.

show abstract

“…Therefore, oxytocin and vasopressin might contribute little, if anything, to the direct PRF activity of the PP extract. Neurophysin, a carrier protein for oxytocin and vasopressin, is also abundant in the PP, and this peptide is reported to stimulate PRL release from cultured rat pituitary cells (Shin et al. 1995).…”

Section: Discussionmentioning

confidence: 99%

Bovine Posterior Pituitary Extract Stimulates Prolactin Release from the Anterior Pituitary Gland In Vitro and In Vivo in Cattle

Hashizume

Sasaki

Nonaka

et al. 2005

Reprod Domestic Animals

View full text Add to dashboard Cite

It has been reported that the posterior pituitary (PP) gland contains a potent, unknown prolactin (PRL)-releasing factor (PRF) in rats. PRFs are assumed to be produced in neurones located within the hypothalamus, and to be peptidergic in nature. However, little is known about PRFs in domestic animals. To characterize the PRF in the PP of domestic animals, the present study examined the PRL-releasing activity of an acidic extract from bovine PP (bPP) in vitro and in vivo in cattle. First, the PRL-releasing effect of bPP extract was compared with that of PRL-releasing peptide (PrRP), and thyrotropin-releasing hormone (TRH) from cultured bovine anterior pituitary cells. The extract significantly increased PRL concentrations in the culture medium, at doses of 0.002 and 0.02 eq./ml (one eq. is the PP extract from one animal), compared with the control (p < 0.05). PrRP failed to stimulate the release of PRL. TRH significantly increased PRL concentrations in the culture medium, at doses from 10(-9) to 10(-7) M, compared with the control (p < 0.05). The rate of increase in the PRL concentration, by 0.02 eq./ml bPP extract, was significantly greater than that in TRH (p < 0.05). Secondly, plasma PRL responses to the intravenous (i.v.) injection of bPP extract (0.5 eq./head), PrRP [3.59 mug/kg body weight (BW)], TRH (1 mug/kg BW), and a dopamine receptor antagonist (sulpiride, 0.1 mg/kg BW), were examined in calves. PrRP failed to stimulate PRL release; however, plasma PRL increased immediately following the injection of bPP extract, TRH and sulpiride. The PRL-releasing effect of i.v. injections of TRH and sulpiride was more potent than that of bPP extract. Finally, plasma PRL responses to the intra-hypothalamic injection of bPP extract were examined in calves. The intra-hypothalamic infusion (arcuate nucleus) of 0.0625 eq./head of bPP extract strongly stimulated PRL release in calves (p < 0.05). The present results show that PP contains a physiologically potent PRF in cattle.

show abstract

Neurophysin stimulates prolactin release from primary cultured rat pituitary cells

Cited by 7 publications

References 0 publications

Is crustacean hyperglycaemic hormone precursor-related peptide a circulating neurohormone in crabs?

Is crustacean hyperglycaemic hormone precursor-related peptide a circulating neurohormone in crabs?

Comparative proteomic analysis of pituitary glands from Huoyan geese between pre-laying and laying periods using an iTRAQ-based approach

Bovine Posterior Pituitary Extract Stimulates Prolactin Release from the Anterior Pituitary Gland In Vitro and In Vivo in Cattle

Contact Info

Product

Resources

About