Peptides derived from the granins (chromogranins/secretogranins)

doi:10.1016/0300-9084(94)90158-9

Biochimie

Volume 76, Issues 3–4, 1994, Pages 277-282

https://doi.org/10.1016/0300-9084(94)90158-9 Get rights and content

Abstract

This review summarizes the role of granins (chromogranins/secretogranins) as precursors to biologically active peptides. We discuss the structural basis of the proteolytic processing of the granins, the consequences of their processing and the biological effects of granin-derived peptides.

References (48)

W.B. Huttner et al.
The granin (chromogranin/secretogranin) family
Trends Biochem Sci
(1991)
H. Winkler et al.
The chromogranins A and B: the first 25 years and future perspectives
Neuroscience
(1992)
A. Zanini et al.
Characterisation of adenohypophyseal polypeptides by two-dimensional gel electrophoresis
Mol Cell Endocrinol
(1981)
P. Rosa et al.
Characterization of adenohypophyseal polypeptides by two-dimensional gel electrophoresis
Mol Cell Endocrinol
(1981)
R.W. Lee et al.
Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase
J Biol Chem
(1983)
G. Falkensammer et al.
Cell-free and cellular synthesis of chromogranin A and B of bovine adrenal medulla
Neuroscience
(1985)
H.-H. Gerdes et al.
The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation
J Biol Chem
(1989)
T.M. Pohl et al.
The organisation of the mouse chromogranin B (secretogranin 1) gene
FEBS Lett
(1990)
H.J. Wu et al.
Structure and function of the chromogranin A gene
J Biol Chem
(1991)
P. Rosa et al.
Monensin and brefeldin A differentially affect the phosphorylation and sulfation of secretory proteins
J Biol Chem
(1992)

D.S. Konecki et al.

The primary structure of human chromogranin A and pancreastatin

J Biol Chem

(1987)

S. Benjannet et al.

Chromogranin B (secretogranin I), a putative precursor of two novel pituitary peptides through processing at paired basic residues

FEBS Lett

(1987)

J.C. Hutton et al.

The molecular cloning of the chromogranin A-like precursor of betagranin and pancreastatin from the endocrine pancreas

FEBS Lett

(1988)

H. Iguchi et al.

Different processing of chromogranin B into GAWK-immunoreactive fragments in the bovine adrenal medulla and pituitary gland

Life Sci

(1988)

S. Aardal et al.

The vasoinhibitory activity of bovine chromogranin A fragment (vasostatin) and its independence of extracellular calcium in isolated segments of human blood vessels

Regul Pept

(1992)

R. Kirchmair et al.

Secretoneurin-A neuropeptide generated in brain, adrenal medulla and other endocrine tissues by proteolytic processing of secretogranin II (chromogranin C)

Neuroscience

(1993)

A. Saria et al.

Secretoneurin releases dopamine from rat striatal slices: a biological effect of a peptide derived from secretogranin II (chromogranin C)

Neuroscience

(1993)

N.G. Seidah et al.

Chromogranin A can act as a reversible processing enzyme inhibitor

FEBS Lett

(1987)

E. Galindo et al.

Chromostatin receptors control calcium channel activity in adrenal chromaffin cells

J Biol Chem

(1992)

L. Dillen et al.

Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B

Biochim Biophys Acta

(1992)

H. Vaudry et al.

Identification of a peptide arising from the specific post-translation processing of secretogranin II

FEBS Lett

(1991)

P. Rosa et al.

Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway

J Cell Biol

(1985)

U.M. Benedum et al.

The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells

EMBO J

(1986)

A. Iacangelo et al.

Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues

Nature

(1986)

Cited by (43)

Molecular cloning and characterization of secretogranin II in the catfish Heteropneustes fossilis: Sex and seasonal brain regional variations and its gonadotropin regulation
2019, Comparative Biochemistry and Physiology -Part A : Molecular and Integrative Physiology
Citation Excerpt :
SgII is associated with the secretory pathway responsible for granule formation and delivery of different neuropeptide hormones and neurotransmitters (Courel et al., 2010; Mikwar et al., 2016). Granins are proteolytically processed by prohormone or pro-protein convertases at multiple dibasic and monobasic cleavage sites to produce different small bioactive peptides (Nataori and Huttner, 1994; Zhao et al., 2009a). The granin family comprises of two groups: the chromogranin group (Cgs) distinct with a disulfide-bonded loop at the N-terminus and the secretogranin group (Sgs), where the disulfide loop is absent (Zhao et al., 2009a).
Secretoneurin (SN) is a novel functional peptide derived from secretogranin II, a protein belonging to the class of chromogranins. Catfish Heteropneustes fossilis is an economically important species of the Asian subcontinent and holds an important place in reproductive physiology study. In the present study, the full-length cDNA encoding secretogranin IIb (SgIIb) was cloned from the brain of catfish H. fossilis. Sequence analysis showed that a 33 amino acid SN peptide (SNb) is present in SgIIb proprotein. The full-length sequence of SgIIb is 2912 bp with open–reading frame 1761 bp long. The 5'UTR is 681 bp long upstream and the 3'UTRis 470 bp long downstream. The ORF encodes 586 amino acid residues comprising signal peptide (24 amino acids) and SNb (33 amino acids), EM66 (66 amino acids). Catfish SgIIb showed 88% nucleotide homology and 90% protein identity with Ictalurus punctatus. Tissue expression showed that it is highly expressed in the brain among all tissues studied. In situ hybridization and quantitative real-time PCR showed significant brain regional distribution with highest transcript abundance in the pituitary. In ovary tissue SgIIb transcripts were localized in the granulosa layer. In the brain, hCG administration stimulated expression highly at 16 h. In ovary, hCG treatment under in vivo and in vitro condition decreased SgIIb expression at all doses. Thus, in the present study in situ localization of SgIIb mRNAs in different regions of brain and pituitary, and ovary suggest its putative role in regulating hypothalamic-pituitary-gonadal (HPG) axis and also suggest that the SgIIb expression pattern in the brain and ovary could be related to reproductive activity and may be involved in the neuroendocrine role of SgIIb in the catfish H. fossilis.
Exploring genetic polymorphism in innate immune genes in Indian cattle (Bos indicus) and buffalo (Bubalus bubalis) using next generation sequencing technology
2015, Meta Gene
Citation Excerpt :
They are secreted from these cells in a physiologically regulated manner having autocrine and paracrine activities (Feldman and Eiden, 2003). The chromatogranin family includes chromatogranin A (CHGA, Secretory protein 1/SP-1), chromatogranin B (CHGB, Secretogranin I/SCG I), and chromatogranin C (CHGC, Secretogranin II/SCG II) (Natori and Huttner, 1994). Genetic polymorphism in some innate immune genes in Indian livestock has been associated with resistance against natural pathogens.
Activation of innate immunity initiates various cascades of reactions that largely contribute to defense against physical, microbial or chemical damage, prompt for damage repair and removal of causative organisms as well as restoration of tissue homeostasis. Genetic polymorphism in innate immune genes plays prominent role in disease resistance capabilities in various breeds of cattle and buffalo. Here we studied single nucleotide variations (SNP/SNV) and haplotype structure in innate immune genes viz CHGA, CHGB, CHGC, NRAMP1, NRAMP2, DEFB1, BNBD4, BNBD5, TAP and LAP in Gir cattle and Murrah buffalo. Targeted sequencing of exonic regions of these genes was performed by Ion Torrent PGM sequencing platform. The sequence reads obtained corresponding to coding regions of these genes were mapped to reference genome of cattle BosTau7 by BWA program using genome analysis tool kit (GATK). Further variant analysis by Unified Genotyper revealed 54 and 224 SNPs in Gir and Murrah respectively and also 32 SNVs was identified. Among these SNPs 43, 36, 11,32,81,21 and 22 variations were in CHGA, CHGB, CHGC, NRAMP1, NRAMP2, DEFB1 and TAP genes respectively. Among these identified 278 SNPs, 24 were found to be reported in the dbSNP database. Variant analysis was followed by structure formation of haplotypes based on multiple SNPs using SAS software revealed a large number of haplotypes. The SNP discovery in innate immune genes in cattle and buffalo breeds of India would advance our understanding of role of these genes in determining the disease resistance/susceptibility in Indian breeds. The identified SNPs and haplotype data would also provide a wealth of sequence information for conservation studies, selective breeding and designing future strategies for identifying disease associations involving samples from distinct populations.
New insights into granin-derived peptides: evolution and endocrine roles
2009, General and Comparative Endocrinology
The granin protein family is composed of two chromogranin and five secretogranin members that are acidic, heat-stable proteins in secretory granules in cells of the nervous and endocrine systems. We report that there is little evidence for evolutionary relationships among the granins except for the chromogranin group. The main granin members, including chromogranin A and B, and secretogranin II are moderately conserved in the vertebrates. Several small bioactive peptides can be generated by proteolysis from those homologous domains existing within the granin precursors, reflecting the conservation of biological activities in different vertebrates. In this context, we focus on reviewing the distribution and function of the major granin-derived peptides, including vasostatin, bovine CgB_1–41 and secretoneurin in vertebrate endocrine systems, especially those associated with growth, glucose metabolism and reproduction.
Neuropeptides of the islets of Langerhans: A peptidomics study
2007, General and Comparative Endocrinology
Neuropeptides from the endocrine pancreas (the islets of Langerhans) play an important role in the regulation of blood glucose levels. Therefore, our aim is to identify the “peptidome” (the in vivo peptide profile at a certain time) of the pancreatic islets, which is beneficial for medical progress related to the treatment of diabetes. So far, there are few neuropeptides isolated and sequenced from the endocrine pancreas and mainly in situ hybridisation and immunocytochemical techniques have been used to demonstrate the occurrence of peptides in the pancreas. These techniques do not allow for unequivocal identification of peptides. In contrary, mass spectrometry identifies peptides unambiguously. We have analysed the peptidome of the islets using peptidomics, i.e. a combination of liquid chromatography, mass spectrometry and bioinformatics. We are able to identify the peptidome of islets extracts. We not only confirm the presence of peptides with a well-known effect on blood glucose levels, but also identify new peptides, which are unknown to affect blood glucose levels.
Neuroendocrine secretory protein 55 (NESP55) immunoreactivity in male and female rat superior cervical ganglion and other sympathetic ganglia
2007, Autonomic Neuroscience: Basic and Clinical
Neuroendocrine secretory protein 55 (NESP55) is a soluble, acidic and heat-stable protein, belonging to the class of chromogranins. It is expressed specifically in endocrine cells and the nervous system, and is probably involved in both constitutive and regulated secretion. In the present study, we investigated the distribution of NESP55 in various rat sympathetic ganglia by immunohistochemistry. The expression of NESP55-IR was detected in a subpopulation of principal neurons in the rat SCG, which was also TH positive, and, thus, adrenergic. In the rat stellate ganglion, more than two thirds of NESP55 positive neurons were adrenergic. Colocalization of NESP55 and calcitonin gene-related peptide (CGRP) in cholinergic neurons was also observed. In the rat thoracic chain, however, the majority of NESP55 positive neurons appeared to lack TH. No detectable NESP55-IR was found in the mouse SCG. Furthermore, in the sexually dimorphic SCG, it was demonstrated that, 80% of the NESP55 positive principal neurons were also NPY positive in the male rat, while a slightly higher, but statistically significant proportion, 87%, was found in the female. Whether or not this small difference is physiologically significant is unknown. The present data provide basic knowledge about the expression of NESP55 in the sympathetic autonomic nervous system of rat, which may further our understanding of the functional significance of NESP55.
2 The Post-Translational Phase of Gene Expression in Tumor Diagnosis
2006, Handbook of Immunohistochemistry and in Situ Hybridization of Human Carcinomas

View all citing articles on Scopus

View full text

Peptides derived from the granins (chromogranins/secretogranins)

Abstract

Trends Biochem Sci

Neuroscience

Mol Cell Endocrinol

Mol Cell Endocrinol

J Biol Chem

Neuroscience

J Biol Chem

FEBS Lett

J Biol Chem

J Biol Chem

J Biol Chem

FEBS Lett

FEBS Lett

Life Sci

Regul Pept

Neuroscience

Neuroscience

FEBS Lett

J Biol Chem

Biochim Biophys Acta

FEBS Lett

Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway

J Cell Biol

The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells

EMBO J

Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues

Nature