Journal
JOURNAL OF NEUROCHEMISTRY
Volume 113, Issue 4, Pages 871-880Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1471-4159.2010.06653.x
Keywords
cannabinoid; carboxypeptidase E; hemoglobin; neuropeptide; peptide processing
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Funding
- National Institutes of Health [DA-04494]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [04/04933-2, 04/14846-0]
- Financiadora de Estudos e Projetos [A-03/134]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico
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P>Many hemoglobin-derived peptides are present in mouse brain, and several of these have bioactive properties including the hemopressins, a related series of peptides that bind to cannabinoid CB1 receptors. Although hemoglobin is a major component of red blood cells, it is also present in neurons and glia. To examine whether the hemoglobin-derived peptides in brain are similar to those present in blood and heart, we used a peptidomics approach involving mass spectrometry. Many hemoglobin-derived peptides are found only in brain and not in blood, whereas all hemoglobin-derived peptides found in heart were also seen in blood. Thus, it is likely that the majority of the hemoglobin-derived peptides detected in brain are produced from brain hemoglobin and not erythrocytes. We also examined if the hemopressins and other major hemoglobin-derived peptides were regulated in the Cpefat/fat mouse; previously these mice were reported to have elevated levels of several hemoglobin-derived peptides. Many, but not all of the hemoglobin-derived peptides were elevated in several brain regions of the Cpefat/fat mouse. Taken together, these findings suggest that the post-translational processing of alpha and beta hemoglobin into the hemopressins, as well as other peptides, is up-regulated in some but not all Cpefat/fat mouse brain regions.
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