Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

ACTH and alpha-MSH levels were measured by radioimmunoassays in extracts of the caudal medulla oblongata of developing rats on postnatal (P) days 1-42 at 7 day intervals, and in adult rats. From P1 to adulthood, ACTH increased greater than 11-fold from 7.2 +/- 1.9 fmol to 82.4 +/- 12.6 fmol per medulla section (mean +/- S.E.M.). In comparison, alpha-MSH increased greater than 7-fold from 68.75 +/- 11.0 fmol to 491 +/- 97.8 fmol during this time period. ACTH/microgram of soluble protein decreased during postnatal development from 0.006 +/- 0.01 to 0.005 +/- 0.001 fmol/microgram of protein and alpha-MSH increased from 0.06 +/- 0.01 fmol/microgram of protein to 0.11 +/- 0.009 fmol/microgram of protein between P1 and P7, decreased to 0.015 +/- 0.003 fmol/microgram of protein by P42 and increased to 0.03 +/- 0.006 fmol/protein per unit protein by adulthood. These data indicate a significant shift in the levels of alpha-MSH detected during development with a decrease in the concentration of material occurring from early postnatal development (P1-P7) to adulthood, which does not appear to be solely related to a regional increase in protein. These studies, as well as radioimmunoassays for ACTH and alpha-MSH in combination with sizing chromatography of pooled extracts at P1, P7 and the adult, demonstrated the predominance of alpha-MSH at all ages.
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PMID:Postnatal development of ACTH and alpha-MSH in the medulla oblongata of rat: alpha-MSH is the predominant peptide. 300 73

Beta-endorphin (B-END) like immunoreactivity (i.r.) levels were measured by radioimmunoassay in the medulla oblongata of developing rats on postnatal ages P1-P42 at 7 day intervals, and in adult rats. From P1 to P42, B-END i.r. increased from 77.0 +/- 1.3 fm to 900.0 +/- 21.6 fm per medulla region (Mean +/- S.E.M.). Adult levels of B-END i.r. were 852.0 +/- 17.0 fm per medulla region. When B-END i.r. was determined per unit protein during this developmental period, a statistically significant change in levels was noted. B-END i.r. dropped from P1 to P7, and then increased from P7 to P14 (P less than 0.01). From P14 through adult, levels did not change significantly. Despite a "drop-out" in the observed immunostaining of B-END neurons in caudal medulla (perikarya in the nucleus tractus solitarius) at P21, radioimmunoassayable levels of this peptide remained constant from P21 through adult per unit protein.
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PMID:Postnatal development of beta-endorphin immunoreactivity in the medulla oblongata of rat. 315 36

Extracts of the anterior lobe and intermediate lobe of postnatal (P) (Day P1, P7, P14, P21, P28, P35, P42) and adult male Sprague-Dawley rats were analyzed by both a Beta-endorphin (B-END) radioimmunoassay and a radioimmunoassay for N-acetyl-B-END. In the anterior lobe, on P1, less than 2% of the adult level of B-END was present. By P42 this level had increased to 21% of adult levels. In the intermediate lobe, on P1, the B-END levels were less than 0.1% of the adult level, and by P42 this level approached approximately 45% of the adult levels. N-acetylated B-END was identified in both anterior lobe and intermediate lobe from P1 through adulthood. In the anterior lobe at P1, N-acetyl-B-END immunoreactivity contributes approximately 25% of the total B-END immunoreactivity. This level drops to less than 10% by P21, and to adult-like levels by P42 (less than 5%). On the other hand, in the intermediate lobe, the N-acetyl-B-END levels start at 70% of the total B-END immunoreactivity at P1 and by P14 reaches adult-like proportions of 90% or more of the total B-END immunoreactive material.
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PMID:Postnatal ontogeny of acetylated and non-acetylated B-endorphin in rat pituitary. 631 11

We investigated changes in mRNA expression of the somatotropic, thyrotropic, and corticotropic axes of Langshan (LS) and Arbor Acres (AA) broiler chickens during embryonic and postnatal development. We found an inverse expression profile between pituitary growth hormone (GH) and hepatic GH receptor mRNA [postnatal d (P)28 to P42], insulin-like growth factor (IGF)-I, and IGF-IR (P0 to P42), respectively. Hepatic IGF-I was a major point of control in the GH-IGF axis from P0 to P28. Pituitary GH-releasing hormone receptor may serve an autocrine-paracrine function from P0 to P28, and hypothalamic ghrelin may affect growth by stimulating the release of hepatic IGF-I from embryonic d (E)8 to P28. Hypothalamic ghrelin might interact with corticotropin-releasing hormone (CRH) from P0 to P28. Hepatic IGF-binding protein-2 regulated growth by regulating hepatic IGF-II bioavailability from P0 to P42. Hepatic IGF-binding protein-5 was an important IGF mediator. A coexpression profile was found between hypothalamic GH-releasing hormone (E10 to E16 and P0 to P42), somatostatin (SS; P0 to P28), thyrotropin-releasing hormone (E10 to E16 and P0 to P28), ghrelin (P0 to P42), and pituitary GH mRNA, hypothalamic SS (P0 to P28), corticotropin-releasing hormone (P0 to P42), thyrotropin-releasing hormone (E10 to E18 and P0-P42), and thyroid-stimulating hormone-beta mRNA, respectively. Moreover, AA chickens were fed a nutrient-rich AA diet (as a control group) and LS chickens were fed either a less nutritious LS diet or the AA diet. Langshan and AA chickens fed the same AA diet showed no differences in pituitary GH, hypothalamic SS, ghrelin, hepatic IGF-I, or GH receptor mRNA. Our data indicate that select genes may show parallel expression during certain periods of development, and that differences in BW and gene expression respond differently to nutrient intake in LS and AA chickens. Our findings may help improve the molecular breeding of chickens.
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PMID:Expression of genes involved in the somatotropic, thyrotropic, and corticotropic axes during development of Langshan and Arbor Acres chickens. 1880 71