TRH in the rat cerebellum: II. Uptake by cerebellar slices

Pacheco, Mauro F.; Woodward, Donald J.; McKelvy, Jeffrey F.; Griffin, W. Sue T.

doi:10.1016/s0196-9781(81)80120-9

Cited by 14 publications

(3 citation statements)

References 18 publications

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“…Further, a number of uptake studies provide functional evidence for the presence of a peptide transporter in the plasma membrane; early on, Abraham et al (1964) observed that the dipeptide carnosine (β-Ala-His) was taken up by rat brain slices in an energy-dependent process. Similarly, uptake of the tripeptide TRH (thyrotropin releasing hormone, Glu-His-Pro) was demonstrated in rat cerebellar and hypothalamic slices (Pacheco et al 1981;Charli et al 1984). More recently, carnosine uptake has been demonstrated to occur only in cultured astrocytes, and not in cultured oligodendrocytes or neurons (Schulz et al 1987;Hoffmann et al 1996).…”

Section: Discussionmentioning

confidence: 95%

Distribution of peptide transporter PEPT2 mRNA in the rat nervous system

Berger¹,

Hediger²

1999

Anatomy and Embryology

130

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The signaling action of neuropeptides in the brain is terminated by breakdown through extracellular peptidases and subsequent removal of the peptide fragments from the extracellular fluid via specific transporter proteins. Here we describe the anatomical distribution in the rat nervous system of the recently isolated high affinity peptide transporter PEPT2. Using nonisotopic in situ hybridization we demonstrate that PEPT2 mRNA is expressed in brain by astrocytes, subependymal cells, ependymal cells and epithelial cells of choroid plexus. Furthermore, PEPT2 is expressed in retina by Müller cells and in dorsal root ganglia by satellite cells. The mRNA levels of PEPT2 in astrocytes are moderate and relatively homogenous throughout the brain except for an area in ventral forebrain where PEPT2 levels are below average. PEPT2 mRNA expression is weakly upregulated in reactive astrocytes that were stimulated through an injection of the glutamatergic neurotoxin quinolinic acid. These data suggest that removal of neuropeptide fragments from brain extracellular fluid occurs via PEPT2 expressed in astrocytes, ependymal cells and choroid plexus epithelial cells.

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Section: Discussionmentioning

confidence: 95%

Distribution of peptide transporter PEPT2 mRNA in the rat nervous system

Berger¹,

Hediger²

1999

Anatomy and Embryology

130

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“…These transporters are integral membrane proteins that uptake di- and tri-peptides: PEPT1 is the low-affinity, high-capacity transporter and is mainly expressed in the small intestine, PEPT2 is the high-affinity, low-capacity transporter and has a broader distribution in the body. Expression of PEPT2 has been shown in glia [ 132 ] and evidence for the uptake of TRH by glial cells has been provided by Pacheco et al [ 133 ]. Nevertheless, this mechanism seems to mainly have a role of clearance of these di- and tri-neuropeptides.…”

Section: Activation Of Gpcrs In Internal Cell Compartmentsmentioning

confidence: 99%

GPCRs in Intracellular Compartments: New Targets for Drug Discovery

et al. 2022

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The architecture of eukaryotic cells is defined by extensive membrane-delimited compartments, which entails separate metabolic processes that would otherwise interfere with each other, leading to functional differences between cells. G protein-coupled receptors (GPCRs) are the largest class of cell surface receptors, and their signal transduction is traditionally viewed as a chain of events initiated from the plasma membrane. Furthermore, their intracellular trafficking, internalization, and recycling were considered only to regulate receptor desensitization and cell surface expression. On the contrary, accumulating data strongly suggest that GPCRs also signal from intracellular compartments. GPCRs localize in the membranes of endosomes, nucleus, Golgi and endoplasmic reticulum apparatuses, mitochondria, and cell division compartments. Importantly, from these sites they have shown to orchestrate multiple signals that regulate different cell pathways. In this review, we summarize the current knowledge of this fascinating phenomenon, explaining how GPCRs reach the intracellular sites, are stimulated by the endogenous ligands, and their potential physiological/pathophysiological roles. Finally, we illustrate several mechanisms involved in the modulation of the compartmentalized GPCR signaling by drugs and endogenous ligands. Understanding how GPCR signaling compartmentalization is regulated will provide a unique opportunity to develop novel pharmaceutical approaches to target GPCRs and potentially lead the way towards new therapeutic approaches.

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“…We have recently studied the breakdown of neuropeptides by isolated nerve-endings incubated under 'physiological' conditions and results (Table 2) indicate the presence of a number of neutral endopeptidases. There is recent evidence for the active uptake of TRH (Pacheco et al, 1981) and fragments of substance P (Nakata et al,198t ). Also, it remains to be established whether centrally acting peptides are internalized as part of a receptor-peptide complex, since such a mechanism appears to operate at peripheral target sites (King and Cuatrecasas, 1981).…”

Section: Intra-neuronal Storage Of Brain Peptidesmentioning

confidence: 99%

The biochemistry of peptide‐mediated signalling in the central nervous system

Edwardson

1982

J of Inher Metab Disea

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TRH in the rat cerebellum: II. Uptake by cerebellar slices

Cited by 14 publications

References 18 publications

Distribution of peptide transporter PEPT2 mRNA in the rat nervous system

Distribution of peptide transporter PEPT2 mRNA in the rat nervous system

GPCRs in Intracellular Compartments: New Targets for Drug Discovery

The biochemistry of peptide‐mediated signalling in the central nervous system

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