Detail of "75790-53-3"

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Subcellular distribution of opioid peptides in rat hypothalamus and pituitary

Subcellular distribution of opioid peptides in rat hypothalamus and pituitary. Molineaux, C. J.; Rosenberger, J. G.; Cox, B. M. (Dep. Pharmacol., Unif. Serv. Univ. Health Sci., Bethesda, MD 20814, USA). J. Neurochem., 43(6), 1616-23 (English) 1984. CODEN: JONRA9. ISSN: 0022-3042. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Homogenates of rat anterior lobe (AL) and neurointermediate lobe (NIL) pituitary and rat hypothalamus were subjected to subcellular fractionation and d. gradient centrifugation. The subcellular distribution of immunoreactive (ir) dynorphin A (Dyn A) [88161-22-2] in NIL was similar to that of ir-arginine vasopressin (AVP) [113-79-1]. The ir-Dyn A migrated as a discrete band on sucrose d. gradients, which corresponded in sedimentation rate to that of ir-AVP, suggesting that these 2 peptides are stored within organelles of similar size and d. Two other products of prodynorphin, ir-a-neoendorphin (a-nEND) [69671-17-6] and ir-1-8-Dyn A [75790-53-3] also comigrated with ir-AVP. The ir-5-leucine-enkephalin (LE) [58822-25-6], which may be a product of prodynorphin or proenkephalin, also migrated in this region of the gradient. When a homogenate of rat hypothalamus was prepd. using a method that has been developed for synaptosome isolation, ir-Dyn A comigrated with Na+/K+-activated ATPase, a synaptosomal marker enzyme. By using a more concd. homogenate, ir-Dyn A migrated to a less dense region where peptide-contg. synaptic vesicles have previously been localized. When a synaptosomal prepn. was lysed in hypotonic soln., a shift was seen in the migration rate of ir-Dyn A to this region of the gradient (contg. putative synaptic vesicles). Thus, the bulk of hypothalamic Dyn appears to be present within synaptosome-like structures which, on lysis, release a less dense, smaller subcellular organelle corresponding in sedimentation characteristics to other types of peptide-contg. synaptic vesicles. By using either method, ir-AVP migrated to a position that was different from that of ir-Dyn A and was unaffected by lysis conditions, indicating that the majority of the Dyn in the hypothalamus is not stored with vasopressin at the subcellular level. Immunoreactivities assocd. with 1-8-Dyn A, a-nEND, LE, and 5-methionine-enkephalin-Arg6-Phe7 (ME-RF) [73024-95-0] in hypothalamus all migrated with ir-Dyn A and all shifted to approx. the same location by lysis. Thus, all of the prodynorphin and proenkephalin products examd. appear to be stored within synaptic vesicle-like organelles present primarily within nerve terminals in the hypothalamus.

Ontogenetic development of the proenkephalin B (= prodynorphin) opioid peptide system in the rat pituitary

Ontogenetic development of the proenkephalin B (= prodynorphin) opioid peptide system in the rat pituitary. Seizinger, Bernd R.; Liebisch, Daniel C.; Grimm, Cornelia; Herz, Albert (Dep. Neuropharmacol., Max-Planck-Inst. Psychiatr., Martinsried D-8033, Fed. Rep. Ger.). Neuroendocrinology, 39(5), 414-22 (English) 1984. CODEN: NUNDAJ. ISSN: 0028-3835. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) The postnatal development of the proenkephalin-B-derived opioid peptides dynorphin1-17 [80448-90-4], dynorphin1-8 [75790-53-3], dynorphin B [83335-41-5], a-neoendorphin [69671-17-6], and b-neoendorphin [77752-00-2] was examd. in rat pituitary lobes. The concns. of proenkephalin-B-derived peptides from the anterior pituitary were 4-12-fold and those from the neurointermediate pituitary 17-122-fold lower in newborn as compared to adult rats. Similarly, the concns. of vasopressin [11000-17-2] in the neurointermediate pituitary increased 50-fold between birth and adulthood; those of oxytocin [50-56-6], however, increased >540-fold over this period. The mol. wt. pattern of dynorphin1-17, dynorphin1-8, dynorphin B, a- and b-neoendorphin-immunoreactive peptides in the anterior and neurointermediate pituitary did not differ between 3-day-old pups and adult rats. In the neurointermediate pituitary, the major immunoreactive components had the same chromatog. properties as synthetic dynorphin1-17, dynorphin1-8, dynorphin B, a- and b-neoendorphin, resp., on gel filtration and HPLC. Thus, neonatal rats were already capable of processing the precursor proenkephalin B [88402-55-5] into these various opioid peptides. In newborn rats, however, the amt. of dynorphin1-8 in the neurointermediate pituitary was 3 times lower than that of its putative intermediate precursor peptide dynorphin1-17. Similarly, the amt. of b-neoendorphin was almost 4 times lower than that of its putative precursor a-neoendorphin. In contrast, in the neurointermediate pituitary of adult rats, dynorphin1-17 and dynorphin1-8, in addn. to a a- and b-neoendorphin, occurred in equimolar amts. The enzymic processing of proenkephalin B to dynorphin1-8 and b-neoendorphin apparently is carried out to a lesser extent in neonatal as compared to adult rats.