Dynorphin B (10-13)

Found 29 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
410.2737	[M+H-2H2O]+ PPM:6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_17 - MTBLS58 Resolution: 17μm, 208x108 Description 1 male adult wild-type rat was obtained from Inserm U1085 - Irset Research Institute (University of Rennes1, France). Animals were age 60 days and were reared under ad-lib conditions. Care and handling of all animals complied with EU directive 2010/63/EU on the protection of animals used for scientific purposes. The whole epididymis was excised from each animal immediately post-mortem, loosely wrapped rapidly in an aluminum foil and a 2.5% (w/v) carboxymethylcellulose (CMC) solution was poured to embed the epididymis to preserve their morphology. To remove air bubbles, the filled aluminum molds was gently freezed by depositing it on isopentane or dry ice, then on the nitrogen vapors and finally by progressively dipping the CMC/sample coated with aluminum foil into liquid nitrogen (or only flush with liquid nitrogen). Frozen tissues were stored at -80 °C until use to avoid degradation.
428.2927	[M+H-H2O]+ PPM:13.9	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_17 - MTBLS58 Resolution: 17μm, 208x108 Description 1 male adult wild-type rat was obtained from Inserm U1085 - Irset Research Institute (University of Rennes1, France). Animals were age 60 days and were reared under ad-lib conditions. Care and handling of all animals complied with EU directive 2010/63/EU on the protection of animals used for scientific purposes. The whole epididymis was excised from each animal immediately post-mortem, loosely wrapped rapidly in an aluminum foil and a 2.5% (w/v) carboxymethylcellulose (CMC) solution was poured to embed the epididymis to preserve their morphology. To remove air bubbles, the filled aluminum molds was gently freezed by depositing it on isopentane or dry ice, then on the nitrogen vapors and finally by progressively dipping the CMC/sample coated with aluminum foil into liquid nitrogen (or only flush with liquid nitrogen). Frozen tissues were stored at -80 °C until use to avoid degradation.
410.2737	[M+H-2H2O]+ PPM:6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_18 - MTBLS58 Resolution: 17μm, 208x104 Description
428.2927	[M+H-H2O]+ PPM:13.9	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_18 - MTBLS58 Resolution: 17μm, 208x104 Description
410.2737	[M+H-2H2O]+ PPM:6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_43 - MTBLS58 Resolution: 17μm, 298x106 Description
428.2927	[M+H-H2O]+ PPM:13.9	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_43 - MTBLS58 Resolution: 17μm, 298x106 Description
410.2738	[M+H-2H2O]+ PPM:5.8	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_44 - MTBLS58 Resolution: 17μm, 299x111 Description
428.293	[M+H-H2O]+ PPM:14.6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_44 - MTBLS58 Resolution: 17μm, 299x111 Description
410.2737	[M+H-2H2O]+ PPM:6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_46 - MTBLS58 Resolution: 17μm, 298x106 Description
428.293	[M+H-H2O]+ PPM:14.6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_46 - MTBLS58 Resolution: 17μm, 298x106 Description
410.2738	[M+H-2H2O]+ PPM:5.8	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_47 - MTBLS58 Resolution: 17μm, 301x111 Description
428.2932	[M+H-H2O]+ PPM:15.1	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_47 - MTBLS58 Resolution: 17μm, 301x111 Description
410.274	[M+H-2H2O]+ PPM:5.3	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_48 - MTBLS58 Resolution: 17μm, 294x107 Description
428.2934	[M+H-H2O]+ PPM:15.6	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_48 - MTBLS58 Resolution: 17μm, 294x107 Description
410.2739	[M+H-2H2O]+ PPM:5.5	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_04 - MTBLS58 Resolution: 17μm, 178x91 Description
428.2928	[M+H-H2O]+ PPM:14.2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_04 - MTBLS58 Resolution: 17μm, 178x91 Description
410.274	[M+H-2H2O]+ PPM:5.3	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_03 - MTBLS58 Resolution: 17μm, 159x110 Description
428.2929	[M+H-H2O]+ PPM:14.4	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_03 - MTBLS58 Resolution: 17μm, 159x110 Description
410.2739	[M+H-2H2O]+ PPM:5.5	Rattus norvegicus	normal	MALDI (DHB)	epik_dhb_head_ito01_05 - MTBLS58 Resolution: 17μm, 183x105 Description
428.2929	[M+H-H2O]+ PPM:14.4	Rattus norvegicus	normal	MALDI (DHB)	epik_dhb_head_ito01_05 - MTBLS58 Resolution: 17μm, 183x105 Description
410.2738	[M+H-2H2O]+ PPM:5.8	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_06 - MTBLS58 Resolution: 17μm, 183x103 Description
428.2928	[M+H-H2O]+ PPM:14.2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_06 - MTBLS58 Resolution: 17μm, 183x103 Description
410.2741	[M+H-2H2O]+ PPM:5	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_14 - MTBLS58 Resolution: 17μm, 205x103 Description
428.2929	[M+H-H2O]+ PPM:14.4	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_14 - MTBLS58 Resolution: 17μm, 205x103 Description
428.2911	[M+H-H2O]+ PPM:10.2	Homo sapiens	esophagus	DESI ()	LNTO22_1_3 - MTBLS385 Resolution: 75μm, 121x68 Description
428.2898	[M+H-H2O]+ PPM:7.2	Homo sapiens	esophagus	DESI ()	LNTO22_1_9 - MTBLS385 Resolution: 75μm, 89x74 Description
446.2978	[M+H]+ PPM:1.1	Homo sapiens	colorectal adenocarcinoma	DESI ()	80TopL, 50TopR, 70BottomL, 60BottomR-profile - MTBLS415 Resolution: 17μm, 137x136 Description The human colorectal adenocarcinoma sample was excised during a surgical operation performed at the Imperial College Healthcare NHS Trust. The sample and procedures were carried out in accordance with ethical approval (14/EE/0024).
410.28	[M+H-2H2O]+ PPM:9.3	Homo sapiens	esophagus	DESI ()	TO31T - MTBLS385 Resolution: 75μm, 56x54 Description
428.2895	[M+H-H2O]+ PPM:6.5	Homo sapiens	esophagus	DESI ()	LNTO22_1_7 - MTBLS385 Resolution: 75μm, 69x54 Description

Dynorphin B (10-13) is fraction of Dynorphin B with only Lys-Val-Val-Thr peptide chain. Dynorphin B is an agonist of nuclear opioid receptors coupling nuclear protein Kinase C activation to the transcription of cardiogenic genes in GTR1 embryonic stem cells. Dynorphin B is a form of dynorphin.Dynorphins are a class of opioid peptides that arise from the precursor protein prodynorphin. When prodynorphin is cleaved during processing by proprotein convertase 2 (PC2), multiple active peptides are released: dynorphin A, dynorphin B, and a/b-neo-endorphin. Depolarization of a neuron containing prodynorphin stimulates PC2 processing, which occurs within synaptic vesicles in the presynaptic terminal. Occasionally, prodynorphin is not fully processed, leading to the release of "big dynorphin."This 32-amino acid molecule consists of both dynorphin A and dynorphin B.Dynorphin A, dynorphin B, and big dynorphin all contain a high proportion of basic amino acid residues, in particular lysine and arginine (29.4\\%, 23.1\\%, and 31.2\\% basic residues, respectively), as well as many hydrophobic residues (41.2\\%, 30.8\\%, and 34.4\\% hydrophobic residues, respectively). Although dynorphins are found widely distributed in the CNS, they have the highest concentrations in the hypothalamus, medulla, pons, midbrain, and spinal cord. Dynorphins are stored in large (80-120 nm diameter) dense-core vesicles that are considerably larger than vesicles storing neurotransmitters. These large dense-core vesicles differ from small synaptic vesicles in that a more intense and prolonged stimulus is needed to cause the large vesicles to release their contents into the synaptic cleft. Dense-core vesicle storage is characteristic of opioid peptides storage. The first clues to the functionality of dynorphins came from Goldstein et al. in their work with opioid peptides. The group discovered an endogenous opioid peptide in the porcine pituitary that proved difficult to isolate. By sequencing the first 13 amino acids of the peptide, they created a synthetic version of the peptide with a similar potency to the natural peptide. Goldstein et al. applied the synthetic peptide to the guinea ileum longitudinal muscle and found it to be an extraordinarily potent opioid peptide. The peptide was called dynorphin (from the Greek dynamis=power) to describe its potency. Dynorphins exert their effects primarily through the κ-opioid receptor (KOR), a G-protein-coupled receptor. Two subtypes of KORs have been identified: K1 and K2. Although KOR is the primary receptor for all dynorphins, the peptides do have some affinity for the μ-opioid receptor (MOR), d-opioid receptor (DOR), N-methyl-D-aspartic acid (NMDA)-type glutamate receptor. Different dynorphins show different receptor selectivities and potencies at receptors. Big dynorphin and dynorphin A have the same selectivity for human KOR, but dynorphin A is more selective for KOR over MOR and DOR than is big dynorphin. Big dynorphin is more potent at KORs than is dynorphin A. Both big dynorphin and dynorphin A are more potent and more selective than dynorphin B (Wikipedia). Dynorphin B (10-13) is fraction of Dynorphin B with only Lys-Val-Val-Thr peptide chain.