UNIPROT:P01189 - FACTA Search

Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Target Concepts:

Query: UNIPROT:P01189 (beta-endorphin)
21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The objective of this study was to determine whether gonadotrophin-releasing hormone (GnRH), oxytocin (OT) and vasoactive intestinal polypeptide (VIP) modulate beta-endorphin-like immunoreactivity (beta-END-LI) secretion by dispersed anterior pituitary cells of pigs and in vivo priming with steroid hormones, estradiol benzoate (EB) and progesterone (P(4)), influences the cell reactivity to peptide hormones tested. Additionally, the aim of this research was to examine the involvement of cyclic nucleotides (cAMP and cGMP) in transduction of signals induced by GnRH, OT and VIP in porcine pituitary cells. Pituitaries were collected from ovariectomized (OVX) gilts that were divided into four experimental groups. Animals of group 1 (OVX) received 1ml corn oil (placebo)/100 kg body weight (b.w.), group 2 (OVX+EB I) and group 3 (OVX+EB II) were treated with EB at the dose 2.5mg/100 kg b.w., 30-36 and 60-66 h before slaughter, respectively. Animals of group 4 (OVX+P(4)) were injected with P(4) at the dose 120 mg/100 kg b.w. for 5 subsequent days before slaughter. Anterior pituitaries were dispersed with trypsin and then pituitary cells were cultured (10(6) per well) in McCoy's 5A medium containing horse serum (10%) and fetal calf serum (2.5%) for 3 days at 37 degrees C under an atmosphere of 95% air and 5% CO(2). Subsequently, plates were rinsed with fresh McCoy's 5A medium and pituitary cells were treated with one of the following agents: GnRH (100 ng/ml), OT (10(-6)M) or VIP (10(-7)M) and incubated for 3.5h at 37 degrees C.GnRH did not affect beta-END-LI secretion by pituitary cells of OVX (group 1) and OVX+P(4) (group 4) gilts. When the pituitary cells were incubated in the presence of OT and VIP, significant increases were observed. After priming of OVX gilts with EB, 30-36 h before slaughter (group 2), we noted a significant increase in beta-END-LI release from pituitary cells only in the presence of VIP. Pituitary cells from gilts treated with EB, 60-66 h before slaughter (group 3), produced markedly elevated amounts of beta-END-LI after GnRH, OT or VIP addition.GnRH markedly stimulated cGMP release from cultured pituitary cells in all experimental groups and significantly increased cAMP production by the cells from OVX, OVX+EB II and OVX+P(4) animals. The addition of OT enhanced both cAMP and cGMP output in all experimental groups of pigs. VIP stimulated cAMP release from pituitary cells derived from OVX, OVX+EB I and OVX+EB II animals. cGMP output was markedly elevated under the influence of VIP from pituitary cells of OVX, OVX+EB II and OVX+P(4) gilts. In conclusion, our results suggest that GnRH, OT and VIP can modulate beta-endorphin release from porcine pituitary cells and imply the involvement of cAMP and cGMP in transduction of signals induced by studied peptides in the cells.
...
PMID:The influence of GnRH, oxytocin and vasoactive intestinal peptide on the secretion of beta-endorphin and production of cAMP and cGMP by porcine pituitary cells in vitro. 1175 23

The present study reports, for the first time, that the recombinant hsp65 from Mycobacterium leprae (chaperonin 2) displays a proteolytic activity toward oligopeptides. The M. leprae hsp65 proteolytic activity revealed a trypsin-like specificity toward quenched fluorescence peptides derived from dynorphins. When other peptide substrates were used (beta-endorphin, neurotensin, and angiotensin I), the predominant peptide bond cleavages also involved basic amino acids in P(1), although, to a minor extent, the hydrolysis involving hydrophobic and neutral amino acids (G and F) was also observed. The amino acid sequence alignment of the M. leprae hsp65 with Escherichia coli HslVU protease suggested two putative threonine catalytic groups, one in the N-domain (T(136), K(168), and Y(264)) and the other in the C-domain (T(375), K(409), and S(502)). Mutagenesis studies showed that the replacement of K(409) by A caused a complete loss of the proteolytic activity, whereas the mutation of K(168) to A resulted in a 25% loss. These results strongly suggest that the amino acid residues T(375), K(409), and S(502) at the C-domain form the catalytic group that carries out the main proteolytic activity of the M. leprae hsp65. The possible pathophysiological implications of the proteolytic activity of the M. leprae hsp65 are now under investigation in our laboratory.
...
PMID:The Mycobacterium leprae hsp65 displays proteolytic activity. Mutagenesis studies indicate that the M. leprae hsp65 proteolytic activity is catalytically related to the HslVU protease. 1204 73

As previous work had shown that extreme N-terminal fragments of the ACTH precursor pro-opiomelanocortin (POMC) not containing gamma-melanotropin (gamma-MSH) were active adrenal mitogens but an antiserum raised against gamma-MSH paradoxically also inhibited adrenal growth we proposed that the adrenal mitogen is processed from pro-gamma-MSH by a neurally controlled protease at the growing adrenal. To this end we have characterised a novel serine protease (named adrenal secretory protease (AsP) as Psort predicted a leader motif) which is expressed at the glomerulosa/fasciculata boundary where mitosis takes place. The expression of AsP was also found to be essential for mitosis of the adrenal cortical tumor Y1 cell-line in POMC containing media and 3D homology modeling revealed the presence of a catalytic pocket flanked by the classical His/Asp/Ser motifs. An usual feature of the model was a cluster of arginine residues on the underside of the protease suggesting that this basically charged face would tend to retain it on the cell surface on secretion-immunocytochemistry using an antiserum raised against a synthetic peptide spanning residues 1-25 of AsP showed that this was the case for Y1 cells. Specificity of AsP (affinity purified from Y1 media) was demonstrated by its inability to cleave model substrates for either trypsin or pro-hormone converting enzymes but was able to cleave an internally quenched POMC (44-55) model peptide. Interestingly mass spectral analysis of products of the latter predicts that the protease cleaves between the bond between Val52 and Met53 suggesting the natural adrenal mitogen is POMC (1-52).
...
PMID:Adrenal growth is controlled by expression of specific pro-opiomelanocortin serine protease in the outer adrenal cortex. 1253 Jun 68

Opioid peptides are negative regulators of cell proliferation in several organs including the uterus. In the present study, the ontogeny of the direct inhibitory action of opioid peptides on the proliferation of cultured rat uterine cells was investigated. Uteri of 7, 14, 21, 28, 35 and 60-day-old rats were removed in a sterile way. Tissue blocks were dispersed by limited digestions with trypsin and collagenase. Cells were cultured in enriched Dulbecco's modified Eagle's medium (DMEM). Treatments were present during the entire culture period. Cell densities of the monolayers were determined by counting the cells following trypsinization and trypan blue exclusion. Rat uterine mixed cell cultures grew to confluence within 10 days. The average population doubling time gradually increased with the age of animals. Epidermal growth factor (EGF) increased cell densities of cultures from all age groups. The oestradiol (E2)-responsiveness appeared at 21 days of age. The effect of [D-Met2-Pro5]-enkephalinamide (ENK) was biphasic. ENK and [Met5]-enkephalin (OGF) decreased cell densities of both unstimulated and EGF-stimulated cultures from 7-day-old rats to the same extent. ENK failed to act in 14-day-old animals. From 21 days of age on, the E2- or EGF-stimulated proliferation was inhibited only by ENK and DAMGO, while 30 nm DPDPE, Dynorhin-A, OGF, [Leu5]-enkephalin, beta-endorphin, and morphiceptin were ineffective. The half-inhibitory concentration of ENK was 0.3 nm. The effects of ENK were prevented by concomitant treatment with naloxone. Our novel data demonstrate two different phases of the inhibitory action of opioid peptides on rat uterine cell proliferation during ontogeny with an insensitive interval in between.
...
PMID:Developmental changes in the inhibition of cultured rat uterine cell proliferation by opioid peptides. 1281 31

Ovoinhibitor is a serine protease-inhibiting protein that was originally purified from egg whites. It is secreted by the oviduct under the control of estrogen and progesterone and it specifically inhibits serine proteinases such as trypsin and chymotrypsin. During recent attempts to raise monoclonal antibodies (Mabs) against chicken bursa of Fabricius proteins, one Mab was produced that specifically recognized chicken ovoinhibitor. This was the first demonstration of ovoinhibitor in an avian immune organ. We presently report on the expression of an ovoinhibitor-like molecule by the pituitary of the chicken as revealed by immunocytochemistry and RT-PCR. Immunofluorescent dual staining experiments using the mouse anti-ovoinhibitor Mab in conjunction with polyclonal antibodies against various hypophysial hormones revealed partial co-localization of an ovoinhibitor-like molecule with growth hormone (GH), luteinizing hormone (LH), and pro-opiomelanocortin (POMC), in a subset of the respective hormone producing cells. By contrast, no co-localization with prolactin (PRL) could be reliably demonstrated. RT-PCR of hypophysial mRNA using ovoinhibitor gene-specific primers yielded an amplicon that was 20% shorter than predicted on the basis of the published ovoinhibitor sequence. Sequencing revealed that of the represented exons only the central portion was expressed in the pituitary and that both 5' and 3' ends of each exon had been truncated. While expression of ovalbumin-like serine protease inhibitors (serpins) has been previously reported in the rat pituitary, to our knowledge, this is the first report of a Kazal-type serine protease inhibitor in the vertebrate neuroendocrine system.
...
PMID:The chicken pituitary expresses an ovoinhibitor-like protein in subpopulations of some, but not all, hormone-producing cell types. 1465 38

Tritium-labeled selective agonist of non-opioid beta-endorphin receptor, the decapeptide immunorphine ([3H]SLTCLVKGFY) with specific activity of 24 Ci/mmol has been prepared. By its use, non-opioid beta-endorphin receptors were revealed and characterized on mouse peritoneal macrophages and rat myocardium, spleen, adrenal, and brain membranes. The non-opioid beta-endorphin receptor of macrophages has in addition to immunorphine (Kd of the [3H]immunorphine-receptor complex was 2.4 +/- 0.1 nM) and beta-endorphin (Ki of the [3H]immunorphine specific binding was 2.9 +/- 0.2 nM) a high affinity for Fc-fragment of human IgG1, pentarphine (VKGFY), cyclopentarphine [cyclo(VKGFY)], and [Pro3]pentarphine (VKPFY) (Ki values were 0.0060 +/- 0.0004, 2.7 +/- 0.2, 2.6 +/- 0.2, and 2.8 +/- 0.2 nM, respectively) and is insensitive to naloxone and [Met5]enkephalin (Ki > 100 microM). Treatment of macrophages with trypsin resulted in the loss of their ability for the specific binding of [3H]immunorphine. Values of the specific binding of 8.4 nM [3H]immunorphine to rat adrenal, spleen, myocardium, and brain membranes were determined to be 1146.0 +/- 44.7, 698.6 +/- 28.1, 279.1 +/- 15.4, and 172.2 +/- 1.8 fmol/mg protein, respectively. Unlabeled beta-endorphin, pentarphine, [Pro3]pentarphine, cyclopentarphine, cyclodipentarphine [cyclo(VKGFYVKGFY)], and Fc-fragment of IgG1 inhibited the binding of [3H]immunorphine to membranes from these organs. No specific binding of [3H]immunorphine to rat liver, lung, kidney, and intestine membranes was found.
...
PMID:Characteristics of non-opioid beta-endorphin receptor. 1517 Mar 74

We utilized mass spectrometry (MS) and bioinformatics to investigate the proteome of the anterior pituitary gland (AP). Subcellular fractions of APs from 2-month-old male Golden Syrian hamsters were prepared for protein denaturation, treatment with trypsin and analyses utilizing micro liquid chromatography MS/MS and the database search software SEQUEST. In the nuclear, non-nuclear 100,000 x g and cytosolic fractions we identified 76, 52 and 52 different proteins, respectively. A total of 145 distinct proteins were detected. We identified growth hormone, prolactin, pro-opiomelanocortin, the alpha-subunit for the glycoprotein hormones, luteinizing hormone-beta and follicle-stimulating hormone-beta. Groups of other identified proteins included hormone processing, secretion granule associated, non-hormonal endoplasmic reticulum associated, calcium binding, protein kinase C associated histone and non-histone chromosomal material, other RNA-binding, splicing factors, heterogeneous nuclear ribonucleoproteins, helicases, lamins, microfilament associated, microtubule associated, adenosine triphosphate and guanosine diphosphate associated, keratins, lysosomal, ribosomal, enzymes in glycolysis and the tricarboxylic and pentose phosphate paths, glutathione associated, transmethylation, catabolic and unknown protein products as well as blood hemoglobins. Proteins previously not reported in the AP, such as fertility protein SP22, were identified. The proteins identified in the present study form a foundation for defining the proteome in normal adult male AP.
...
PMID:Analysis of the golden Syrian hamster anterior pituitary gland proteome by ion trap mass spectrometry. 1569 19

We investigated the proteome of the anterior pituitary gland (AP) in a species in which the genome has been sequenced. Subcellular fractions of APs from 2-month-old male mice were prepared for protein denaturation, treatment with trypsin and analyses utilizing micro liquid chromatography tandem mass spectrometry and the database search software SEQUEST. In the nuclear, non-nuclear 100,000 g and cytosolic fractions, we identified 49, 36 and 68 different proteins, respectively. A total of 115 distinct proteins were detected. We identified growth hormone, prolactin, pro-opiomelanocortin, the alpha-subunit for the glycoprotein hormones, and luteinizing hormone-beta. Groups of other identified proteins included hormone-processing, secretion granule-associated, non-hormonal endoplasmic reticulum-associated, calcium-binding, protein kinase C-associated, histones, non-histone chromosomal, other RNA-binding, heterogeneous nuclear ribonucleoproteins, splicing factors, helicases, lamins, ribosomal, microtubule-associated, microfilament-associated, adenosine triphosphate- and guanosine triphosphate-associated, tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation, enzymes in glycolysis and the tricarboxylic and urea cycles and the pentose phosphate path, heat-shock, glutathione-associated, peroxidases, ubiquitin-associated, catabolic, protease inhibitors, other, and blood proteins. The 115 proteins reported in this study and the 145 proteins reported in a previous study on the AP of the adult male Golden Syrian hamster are compared and form a foundation for defining the proteome in normal adult male AP.
...
PMID:Mouse anterior pituitary gland: analysis by ion trap mass spectrometry. 1610 33

Increased blood-brain-barrier (BBB) permeability precedes any clinical or pathologic signs and is critical in the pathogenesis of multiple sclerosis (MS) and brain metastases. CD4+ TH1 cells mediate demyelination in MS, but how they get sensitized and enter the brain to induce brain inflammation remains obscure. TH2 cytokines associated with allergic disorders have recently been implicated in MS, while genes upregulated in MS plaques include the mast cell-specific tryptase, the IgE receptor (Fc-epsilon-RI) and the histamine-1 receptor. Mast cell specific tryptase is elevated in the CSF of MS patients, induces microvascular leakage and stimulates protease-activated receptors (PAR), leading to widespread inflammation. BBB permeability, MS and brain metastases appear to worsen in response to acute stress that leads to the local release of corticotropin-releasing hormone (CRH), which activates brain mast cells to selectively release IL-6, IL-8 and vascular endothelial growth factor (VEGF). Acute stress increases BBB permeability that is dependent on CRH and mast cells. Acute stress shortens the time of onset of experimental alleric encephalomyelitis (EAE) that does not develop in W/W mast cell deficient or CRH -/- mice. Brain mast cell inhibition and CRHR antagonists offer novel therapeutic possibilities.
...
PMID:Corticotropin-releasing hormone and the blood-brain-barrier. 1712 8

Metastases continue to be the chief cause of morbidity and mortality for many tumors, including brain metastases of lung and mammary adenocarcinoma. Stress appears to increase metastases, but the mechanism is not understood. Recent evidence suggests that local inflammation is conducive for cancer growth and a unique immune cell, the mast cell, accumulates in the stroma surrounding tumors and is critically located at the blood-brain-barrier (BBB). Mast cells express receptors for and can be stimulated by corticotropin-releasing hormone (CRH), secreted under stress, to release mediators such as histamine, IL-8, tryptase and vascular endothelial growth factor (VEGF), which disrupt the BBB permitting metastases. Stress and mast cells could serve as new targets for drug development to prevent brain metastases, especially since CRH receptor antagonists and brain mast cell inhibitors have recently been developed.
...
PMID:Impact of stress and mast cells on brain metastases. 1919 17

<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>