Substance P in the human brain

Mai, J.K.; Stephens, P.H.; Hopf, A; Cuello, A. Claudio

doi:10.1016/0306-4522(86)90041-2

Cited by 179 publications

(64 citation statements)

References 66 publications

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“…In humans, Glyt-1 expression is absent in [38]. Thus, NEP distribution seems to be only matched, notably in striatonigral pathway, with that of SP, but not in the cerebral cortex where both SP-and VIP-containing neurons and their processes are abundantly located [34,35]. This only partially matched distribution pattern was also demonstrated in a detailed immunohistochemistry analysis [37].…”

Section: Expression Of the Oatp1a2-and Oatp2b1-immunoreactivity In Thmentioning

confidence: 90%

“…In the retina angiotensin converting enzyme was only detected in chicken after pretreatment with protease inhibitors [57], but not in the rat [50], suggesting a at best a low expression level in this tissue. Taken together, the partially matched distribution pattern raises a possibility that alternative mechanism(s) may be involved in determining turning over the released neuroactive peptides in the synaptic cleft, particularly in areas that are short of degrading enzymes but rich in peptides, such as the cerebral cortex [34,35,47] and retina. Our findings that OATP1A2 and OAPT2B1 are abundantly present in the cerebral cortex and retina, and that they exhibit saturable transport activity for SP and VIP argue for a functional role of these OATPs in clearing released neuropeptides.…”

Section: Expression Of the Oatp1a2-and Oatp2b1-immunoreactivity In Thmentioning

confidence: 99%

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Differential cellular expression of organic anion transporting peptides OATP1A2 and OATP2B1 in the human retina and brain: implications for carrier-mediated transport of neuropeptides and neurosteriods in the CNS

Gao

Vavricka

Meier

et al. 2014

Pflugers Arch - Eur J Physiol

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Organic anion transporting polypeptides (OATPs) are polyspecific organic anion transporters, which are expressed in the blood-brain barrier, the choroid plexus, and other organs. The physiologic function of OATPs in extrahepatic tissues remains ambiguous. In rat retina, members of the OATP family are expressed. We therefore investigated the human retina for the expression of OATP1A2 and OATP2B1 and extended the study to human brain. Furthermore, we searched for peptide neurotransmitters as novel OATP substrates. OATP1A2 displayed a broad expression pattern in human retina as assessed by immunofluorescence localization. It is expressed in photoreceptor bodies and somas of amacrine cells. OATP1B2 expression is restricted to the inner nuclear layer and to the inner plexiform layer. Using paraffin sections from human cortex, cerebellum, and hippocampus, OATP1A2 was localized to neurons and neuronal processes, while OATP2B1 is expressed in endothelial cells of brain capillaries. Substance P and vasoactive intestinal peptide were identified as substrates for OATP1A2 and OATP2B1. Doublelabeling immunofluorescence of human retina demonstrated the presence of substance P and of vasoactive intestinal peptides in neurons expressing OATP1A2 and OATP2B1, respectively. The expression of OATP1A2 and OATP2B1 in retinal neurons implies a role of these transporters in the reuptake of peptide neurotransmitters released from retinal neurons. The abundant expression of OATP1A2 in brain neurons points to the possibility that OATP1A2 could be involved in the homeostasis of neurosteroids. The high expression of OATP2B1 in brain capillaries supports an important function of OATPs in substance penetration across the blood-brain barrier. Order of Authors Secondary Information:Abstract: Organic anion transporting polypeptides (OATPs) are polyspecific organic anion transporters, which are expressed in the blood brain barrier, the choroid plexus and other organs. The physiologic function of OATPs in extrahepatic tissues remains ambiguous. In rat retina, members of the OATP family are expressed. We therefore investigated the human retina for the expression of OATP1A2 and OATP2B1 and extend the study to human brain. Furthermore, we searched for peptide neurotransmitters as novel OATP substrates. OATP1A2 displayed a broad expression pattern in human retina as assessed by immunofluorescence localization in fixedfrozen section. It is expressed in photoreceptor bodies and somas of amacrine cells. OATP1B2 expression is restricted to the inner nuclear layer and to the inner plexiform layer. Using paraffin sections from human cortex, cerebellum and hippocampus, OATP1A2 was localized to neurons and neuronal processes, while OATP2B1 is expressed in endothelial cells of brain capillaries. Substance P and vasoactive intestinal peptide were identified as substrates for OATP1A2 and OATP2B1. Doublelabeling immunofluorescence of human retina demonstrated the presence of substance P and of vasoactive intestinal peptides in neurons, which express OAT...

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Section: Expression Of the Oatp1a2-and Oatp2b1-immunoreactivity In Thmentioning

confidence: 90%

Section: Expression Of the Oatp1a2-and Oatp2b1-immunoreactivity In Thmentioning

confidence: 99%

Differential cellular expression of organic anion transporting peptides OATP1A2 and OATP2B1 in the human retina and brain: implications for carrier-mediated transport of neuropeptides and neurosteriods in the CNS

Gao

Vavricka

Meier

et al. 2014

Pflugers Arch - Eur J Physiol

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“…This area was included as part of the pallidum based both on histological criteria and the fact that it received its input from the VS (Heimer, 1978). Pallidal neurons have a distinct morphology, which is nicely outlined using immunohistochemistry for the peptides, enkephalin, and substance P. Staining for these peptides was particularly useful for determining the boundaries of the VP (DiFiglia et al, 1982;Fox et al, 1974;Haber and Nauta, 1983;Haber and Watson, 1985;Mai et al, 1986;Reiner et al, 1999). Based on these staining patterns and its input from the VS, the VP is now considered to encompass not only the subcommissural regions, but also the rostral pole of the external segment and the medial rostral internal segment of the globus pallidus.…”

Section: Ventral Pallidum (Figure 8)mentioning

confidence: 99%

The Reward Circuit: Linking Primate Anatomy and Human Imaging

Haber

Knutson

2009

Neuropsychopharmacol

3,183

193

2,859

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Although cells in many brain regions respond to reward, the cortical-basal ganglia circuit is at the heart of the reward system. The key structures in this network are the anterior cingulate cortex, the orbital prefrontal cortex, the ventral striatum, the ventral pallidum, and the midbrain dopamine neurons. In addition, other structures, including the dorsal prefrontal cortex, amygdala, hippocampus, thalamus, and lateral habenular nucleus, and specific brainstem structures such as the pedunculopontine nucleus, and the raphe nucleus, are key components in regulating the reward circuit. Connectivity between these areas forms a complex neural network that mediates different aspects of reward processing. Advances in neuroimaging techniques allow better spatial and temporal resolution. These studies now demonstrate that human functional and structural imaging results map increasingly close to primate anatomy.

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“…The highest SP concentration is found in rat and primate hypothalamic extracts (2)(3)(4)(5). A high density of immunoreactive SP is present in the rat and primate hypothalamus in areas involved in the control of anterior pituitary function (2)(3)(4).…”

Section: Introductionmentioning

confidence: 97%

Interaction between substance P and gastrin-releasing peptide on thyrotropin secretion by rat pituitary in vitro

Moura

Santos

et al. 1999

Braz J Med Biol Res

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The effect of substance P (SP) on thyrotropin (TSH) secretion is controversial. In this study we evaluated the effect of SP on TSH secretion by hemipituitaries of 3-month-old Wistar rats in vitro and its interaction with gastrin-releasing peptide (GRP) at equimolar concentrations (1 µM and 10 µM). TSH release was measured under basal conditions and 30 min after incubation in the absence or presence of SP, GRP or both peptides. Pituitary TSH content was also measured in the pituitary homogenate after incubation. SP at both concentrations caused a significant (P<0.05) increase in TSH secretion compared with all other groups, which was approximately 60% (1 µM) and 85% (10 µM) higher than that of the control group (23.3 ± 3.0 ng/ml). GRP at the lower concentration did not produce a statistically significant change in TSH secretion, whereas at the concentration of 10 µM it produced a 50% reduction in TSH. GRP co-incubated with substance P completely blocked the stimulatory effect of SP at both concentrations. Pituitary TSH content decreased in the SP-treated group compared to controls (0.75 ± 0.03 µg/hemipituitary) at the same proportion as the increase in TSH secretion, and this effect was also blocked when GRP and SP were co-incubated. In conclusion, in an in vitro system, SP increased TSH secretion acting directly at the pituitary level and this effect was blocked by GRP, suggesting that GRP is more potent than SP on TSH secretion, and that this inhibitory effect could be the predominant effect in vivo.

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Substance P in the human brain

Cited by 179 publications

References 66 publications

Differential cellular expression of organic anion transporting peptides OATP1A2 and OATP2B1 in the human retina and brain: implications for carrier-mediated transport of neuropeptides and neurosteriods in the CNS

Differential cellular expression of organic anion transporting peptides OATP1A2 and OATP2B1 in the human retina and brain: implications for carrier-mediated transport of neuropeptides and neurosteriods in the CNS

The Reward Circuit: Linking Primate Anatomy and Human Imaging

Interaction between substance P and gastrin-releasing peptide on thyrotropin secretion by rat pituitary in vitro

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