Structure of chicken calcitonin predicted by partial nucleotide sequence of its precursor (original) (raw)
Related papers
Journal of Molecular Endocrinology, 1991
We have isolated from a bovine genomic library a clone which contains the calcitonin (CT) and CT gene-related peptide (CGRP) sequences, using probes representing the human CT and CGRP sequences. Sequence analysis has identified the nucleotide sequence coding for bovine CT, its C-terminal flanking peptide and bovine CGRP. The deduced amino acid sequence of bovine CGRP revealed a significant homology with other CGRPs so far reported. It differs by only one amino acid from rat CGRPα and porcine CGRP, and by three and four amino acids from human CGRPβ and α respectively. Bovine CT has, however, only 14 out of 32 residues in common with human CT. As in the human CT precursor, the C-terminal flanking peptide of bovine CT precursor is a 21 amino acid peptide. It shares only 11 residues in common with its human counterpart. This study thus provides further evidence that CGRP, in contrast to CT and its C-terminal flanking peptide, is a highly conserved molecule.
Cell free translation of chicken calcitonin messenger RNA
FEBS Letters, 1983
The primary step of calcitonin biosynthesis was studied in a normal organ: chicken ultimobranchial gland, a tissue particularly rich in calcitonin secretory cells. Poly(A)-rich RNA was extracted and purified from ultimobranchial organs and translated in a reticulocyte lysate in the presence of labelled methionine. Polyacrylamide gel electrophoresis of specific immunoprecipitates revealed a major band of M, 14500 and a band of ik& 13300. Thus, in chicken the precursor of calcitonin is a M, 14500 polypeptide. The minor component of I% 13300 could represent limited processing by the reticulocyte lysate.
Molecular cloning and characterization of the porcine calcitonin gene-related …
Endocrinology
Calcitonin gene-related peptide (CGRP) receptors (CGRP-Rs) are widely distributed throughout the central and peripheral nervous systems. A novel CGRP-R was identified from a porcine lung complementary DNA library. Sequence analysis indicated that the CGRP-R is 462 amino acids in length and shares 93% sequence identity with the human CGRP-R. Northern blot analysis indicated a messenger RNA species of 5.4 kilobases, which is abundantly expressed in the lung. Ligand binding studies of the cloned CGRP-R expressed in human embryonic kidney (HEK-293) cells showed the presence of high affinity receptor for CGRP with a K d of 38.5 pM. The pharmacological profiles of various ligands competing for [ 125 I]CGRP binding to the expressed receptor were in accordance with those for
Occurrence of calcitonin gene-related peptide in the chicken amacrine cells
Brain Research, 1985
The distribution of calcitonin gene-related peptide (CGRP)-Iike immunoreactivity (CGRPI) in the chicken retina was investigated by means of immunohistochemistry. CGRPI was localized in the stratified amacrine cells, The terminal branching pattern of these cells was different between the central and peripheral retinal regions. Flat-mount preparations revealed these CGRPI cells to be evenly distributed in the entire retina with surprisingly rich arborization.
Ontogenesis of calcitonin mRNA in the rabbit
Journal of Bone and Mineral Research, 1990
Since plasma calcium levels are higher in the fetus than in the mother at the end of gestation, it has been suggested that calcitonin (CT) biosynthesis would be very active in the fetus. This hypothesis was tested in rabbit fetuses and newborns by measuring the amount of CT mRNAs found in the thyroid glands and the thyroidal CT stores. Dot-blot and Northern hybridizations with a specific CT cDNA probe (a Bglll-Nsil fragment of the human CT cDNA) were used to determine the CT mRNA level. In fetuses, newborns, and mothers, only one molecular species of mRNA around 1 kb was detected by Northern hybridization with the specific CT cDNA probe. By dot-blot, CT mRNAs could be detected at 20 days of gestation on pooled fetal thyroid glands as a weak positive signal. The amount of CT mRNAs increased on day 24; at this stage they were also observed by Northern hybridization. During the last 6 days of gestation a 3-fold increase in CT mRNAs occurred in rabbit fetuses; concomitantly a 5-fold rise in the total thyroidal CT content was observed. Fetal plasma concentrations of both CT and calcium increased slightly between 24 and 30 days of gestation. After birth, the CT mRNA level was 10-fold increased between 2 and 30 days; these changes were not reflected in the plasma CT level but were probably accounted for by a rise in the number of C cells of the thyroid gland.
Immunochemical characterization and distribution of calcitonin in the lizard
European Journal of Endocrinology, 1981
Immunological and chromatographic methods were used to investigate the distribution of calcitonin (CT) in various tissues of Lacerta muralis, a common wall lizard. Salmon CT-like immunoreactivity was found in high concentration in extracts of ultimobranchial gland (UBG) and in significant amounts in lung and brain extracts, but not in other tissues (oesophagus, stomach, duodenum, liver, skin, muscle and thyroid). Serial dilution of UBG, lung and brain extracts gave parallel displacement curves to that of synthetic salmon CT (sCT), but no reactivity was found in the human CT assay. On Sephadex G-50, UBG, lung and brain extracts contained an sCT-like immunoreactive peak which co-eluted with synthetic sCT. However, on high performance liquid chromatography (HPLC) the sCT-like peak in UB, lung and brain extracts eluted 2 ml later than synthetic sCT. This paper describes the first immunochemical characterization of CT in the UBG of the lizard, demonstrates the distribution of extra-ultimobranchial CT and throws some light on the evolution of the calcitonins.
2009
Calcitonin gene-related peptide has been extracted from the skin exudate of a single living specimen of the frog Phyllomedusa bicolor and purified to homogeneity by a two-step protocol. A total volume of 250 �l of exudate yielded 380 �g of purified peptide. Mass spectrometric analysis and gas phase sequencing of the purified peptide as well as chemical synthesis and cDNA analysis were consistent with the structure SCDTSTCATQRLAD-FLSRSGGIGSPDFVPTDVSANSF amide and the presence of a disulfide bridge linking Cys 2 and Cys 7. The skin peptide, named skin calcitonin gene-related peptide, differs significantly from all other members of the calcitonin gene-related peptide family of peptides at nine positions but binds with high affinity to calcitonin gene-related peptide receptors in the rat brain and acts
Annals of the New York Academy of Sciences, 1992
The existence of the calcitonin gene-related peptide (a-rCGRP) was predicted in 1983 in the rat;I a similar peptide was identified in the human a short while later (a-hCGRP).* Another very similar peptide in the rat (P-hCGRP), differing by one amino acid from a-hCGRP, and in the human (P-hCGRP), differing by three amino acids from a-hCGRP, was predicted from cDNA analysis in the rat and in man.3.4 The existence of the latter was proved by isolation, and its full characterization was accomplished by amino acid sequencing and fast atom bombardment mass spectrometry (FAB-MS).' Both a-and P-CGRP are present in plasma, cerebrospinal fluid, and the spinal cord.h However, CGRP is present in these body fluids and in tissues in a number of different molecular weight CGRP is a potent that is present in the circulation7-' and in cerebrospinal fluid'" in man. CGRP is thought likely to play an important role in the regulation of vascular function as well as in the modulation of neurologic Distribution and Localization CGRP receptors have been studied in man and in the rat and are widely distributed in the nervous including discrete brain area^,^^.^^ and in 104 104
Identification of a 3RD Ubiquitous Calpain Species - Chicken Muscle Expresses 4 Distinct Calpains
Biochimica Et Biophysica Acta-Gene Structure and Expression, 1995
In the mammalian calpain system, two isozymes, /x-and m-types, have been well-characterized, and are considered to be conserved in the avian system as well. Thus, chicken calpain, whose large subunit was cloned in 1984, has long been regarded as "m-type', since chicken also possesses '/z-type' activity, although its structure has not yet been elucidated. In this study, we identified three kinds of cDNAs encoding distinct chicken calpain large subunits. Two of the three were highly similar to the mammalian /x-type and p94, respectively. The third shows a much higher similarity to mammalian m-type than the first identified chicken calpain, indicating that this molecule, which has been considered as 'm-type', should be renamed. We, therefore, designated it 'jz/m-calpain', because its sequence and Ca2+-sensitivity lie between /z-and m-types. Northern blot analyses revealed that chicken mCL and p.CL, as well as /x/mCL, show ubiquitous expression, while p94 was detected predominantly in skeletal muscle, as previously reported. Chicken skeletal muscle, therefore, expresses at least four types of calpain, three ubiquitous and one tissue-specific.