Delta sleep-inducing peptide

Last updated
Delta sleep-inducing peptide
Identifiers
SymbolDSIP
UniProt P01158

Delta sleep-inducing peptide, abbreviated DSIP, is a neuropeptide that when infused into the mesodiencephalic ventricle of recipient rabbits induces spindle and delta EEG activity and reduced motor activities. [1]

Slow-wave sleep

Slow-wave sleep (SWS), often referred to as deep sleep, consists of stage three of non-rapid eye movement sleep. Initially, SWS consisted of both Stage 3, which has 20-50 percent delta wave activity, and Stage 4, which has more than 50 percent delta wave activity. However, as of 2008, the American Academy of Sleep Medicine (AASM) has discontinued the use of Stage four as a separate stage. Thus, the two stages are now combined as "Stage three" or N3. An epoch which consists of 20% or more slow-wave (delta) sleep is now considered to be stage three.

Neuropeptide

Neuropeptides are small protein-like molecules (peptides) used by neurons to communicate with each other. They are neuronal signalling molecules that influence the activity of the brain and the body in specific ways. Different neuropeptides are involved in a wide range of brain functions, including analgesia, reward, food intake, metabolism, reproduction, social behaviors, learning and memory.

Contents

Its aminoacid sequence is Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu. However, the gene is unknown[ citation needed ], raising serious questions regarding the actual existence of this peptide in nature.

Tryptophan chemical compound

Tryptophan is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a non-polar aromatic amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin and vitamin B3. It is encoded by the codon UGG.

Alanine chemical compound

Alanine (symbol Ala or A) is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently, its IUPAC systematic name is 2-aminopropanoic acid, and it is classified as a nonpolar, aliphatic α-amino acid. Under biological conditions, it exists in its zwitterionic form with its amine group protonated (as −NH3+) and its carboxyl group deprotonated (as −CO2−). It is non-essential to humans as it can be synthesised metabolically and does not need to be present in the diet. It is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG).

Glycine chemical compound

Glycine (symbol Gly or G; ) is an amino acid that has a single hydrogen atom as its side chain. It is the simplest amino acid, with the chemical formula NH2‐CH2‐COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form. For the same reason, it is most abundant amino acid in collagen triple-helices. Glycine is also an inhibitory neurotransmitter - interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction.

Discovery

Delta sleep-inducing peptide was first discovered in 1974 by the Swiss Schoenenberger-Monnier group who isolated it from the cerebral venous blood of rabbits in an induced state of sleep. It was primarily believed to be involved in sleep regulation due to its apparent ability to induce slow-wave sleep in rabbits, but studies on the subject have been contradictory. [2]

Delta-sleep-inducing peptide (DSIP)-like material has been found in human breast milk. [3]

Structure and Interactions

DSIP is an amphiphilic peptide of molecular weight 850 daltons with the amino acid motif:
N-Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu-C [4]

It has been found in both free and bound forms in the hypothalamus, limbic system and pituitary as well as various peripheral organs, tissues and body fluids. [5] In the pituitary it co-localises with many peptide and non-peptide mediators such as corticotropin-like intermediate peptide (CLIP), adrenocorticotrophic hormone (ACTH), melanocyte-stimulating hormone (MSH), thyroid-stimulating hormone (TSH) and melanin concentrating hormone (MCH). It is abundant in the gut secretory cells and in the pancreas where it co-localises with glucagon. [4]

Hypothalamus part of diencephalon

The hypothalamus is a portion of the brain that contains a number of small nuclei with a variety of functions. One of the most important functions of the hypothalamus is to link the nervous system to the endocrine system via the pituitary gland. The hypothalamus is located below the thalamus and is part of the limbic system. In the terminology of neuroanatomy, it forms the ventral part of the diencephalon. All vertebrate brains contain a hypothalamus. In humans, it is the size of an almond. The hypothalamus is responsible for the regulation of certain metabolic processes and other activities of the autonomic nervous system. It synthesizes and secretes certain neurohormones, called releasing hormones or hypothalamic hormones, and these in turn stimulate or inhibit the secretion of hormones from the pituitary gland. The hypothalamus controls body temperature, hunger, important aspects of parenting and attachment behaviours, thirst, fatigue, sleep, and circadian rhythms. The hypothalamus derives its name from Greek ὑπό, under and θάλαμος, chamber.

Limbic system part of brain located on both sides of the thalamus, immediately beneath the cerebrum; supports a variety of functions including emotion, behavior, motivation, long-term memory, and olfaction.

The limbic system, also known as the paleomammalian cortex, is a set of brain structures located on both sides of the thalamus, immediately beneath the medial temporal lobe of the cerebrum primarily in the midbrain.

Corticotropin-like intermediate [lobe] peptide (CLIP), also known as adrenocorticotropic hormone fragment 18-39, is a naturally occurring, endogenous neuropeptide with a docosapeptide structure and the amino acid sequence Arg-Pro-Val-Lys-Val-Tyr-Pro-Asn-Gly-Ala-Glu-Asp-Glu-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe. CLIP is generated as a proteolyic cleavage product of adrenocorticotropic hormone (ACTH), which in turn is a cleavage product of proopiomelanocortin (POMC). Its physiological role has been investigated in various tissues, specifically in the central nervous system.

In the brain its action may be mediated by NMDA receptors. [6] In another study Delta sleep-inducing peptide stimulated Acetyltransferase activity through α1 receptors in rats. [7] It is unknown where DSIP is synthesized.

In vitro it has been found to have a low molecular stability with a half life of only 15 minutes due to the action of a specific aminopeptidase-like enzyme. [8] It has been suggested that in the body it complexes with carrier proteins to prevent degradation, or exists as a component of a large precursor molecule, [9] but as yet no structure or gene has been found for this precursor.

Evidence supports the current belief that it is regulated by glucocorticoids. [10]

Gimble et al. suggest that DSIP interacts with components of the MAPK cascade and is homologous to glucocorticoid-induced leucine zipper (GILZ). [11] GILZ can be induced by Dexamethasone. It prevents Raf-1 activation, which inhibits phosphorylation and activation of ERK. [12]

Function

Many roles for DSIP have been suggested following research carried out using peptide analogues with a greater molecular stability [13] and through measuring DSIP-like immunological (DSIP-LI) response by injecting DSIP antiserum and antibodies. [14]

Roles in endocrine regulation

Roles in physiological processes

Roles in disease and medicine

Safety and possible side-effects of long-term DSIP use haven't been established in clinical research studies.

Related Research Articles

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References

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  2. ↑ Schoenenberger GA, Maier PF, Tobler HJ, Monnier M (1977). "A naturally occurring delta-EEG enhancing nonapeptide in rabbits". European Journal of Physiology. 369 (2): 99–109. doi:10.1007/BF00591565. PMID   560681.
  3. ↑ Graf MV, Hunter CA, Kastin AJ (1984). "Presence of Delta-Sleep-Inducing Peptide-Like Material in Human Milk". Journal of Clinical Endocrinology & Metabolism. 59 (1): 127–32. doi:10.1210/jcem-59-1-127. PMID   6547144.
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  13. ↑ synthesized by V. N. Kalikhevich and S. I. Churkina, University Chemical Institute, St. Petersburg, Russia, and I. I. Mikhaleva and I. A. Prudchenko, Institute of Bio-organic Chemistry, Russian Academy of Sciences, Moscow
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