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Nucleotide sequence of cloned cDNAs encoding chicken preproparathyroid hormone
Year:
1988
Authors :
Hurvitz, Shmuel (Animal science)
;
.
Pines, Mark
;
.
Volume :
3
Co-Authors:
Khosla, S., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States, Mayo Clinic, Rochester, Minnesota, 55905, United States
Demay, M., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States
Pines, M., Volcani Center Institute of Animal Sciences, Bet Dagan, Israel
Hurwitz, S., Volcani Center Institute of Animal Sciences, Bet Dagan, Israel
Potts, J.T., Jr., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States
Kronenberg, H.M., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States
Facilitators :
From page:
689
To page:
698
(
Total pages:
10
)
Abstract:
In order to characterize an avian parathyroid hormone gene, a λgt10 cDNA library constructed from chicken parathyroid gland mRNA was screened with a human preproparathyroid hormone (preproPTH) cDNA probe. Nucleotide sequence analysis of three independent clones confirmed that they encoded chicken preproPTH. This analysis, complemented by primer extension and Northern blot analysis of mRNA, demonstrated a 5′‐untranslated region for chicken preproPTH of 127 nucleotides, a coding region of 357 nucleotides, and a 3′‐untranslated region of approximately 2500 nucleotides. The coding sequence predicts a mature chicken PTH of 88 amino acids in contrast to the 84 amino acids of the mammalian hormones. Comparison of the avian and the mammalian hormones shows striking homology in the region of amino acids 1–32. The middle and carboxyl‐terminal portions of chicken PTH, however, differ considerably from the mammalian hormones and include deletions of sequences conserved in mammalian PTH and insertions of novel peptide sequences. Comparison of the avian and mammalian structures suggests potential alterations of the mammalian sequences that may lead to altered bioactivity and/or hormone metabolism. Copyright © 1988 ASBMR
Note:
Related Files :
Animal
animal cell
Base Sequence
DNA
Gene
gene expression regulation
Molecular Sequence Data
RNA, Messenger
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Related Content
More details
DOI :
10.1002/jbmr.5650030615
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27752
Last updated date:
21/08/2022 07:45
Creation date:
17/04/2018 00:33
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Scientific Publication
Nucleotide sequence of cloned cDNAs encoding chicken preproparathyroid hormone
3
Khosla, S., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States, Mayo Clinic, Rochester, Minnesota, 55905, United States
Demay, M., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States
Pines, M., Volcani Center Institute of Animal Sciences, Bet Dagan, Israel
Hurwitz, S., Volcani Center Institute of Animal Sciences, Bet Dagan, Israel
Potts, J.T., Jr., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States
Kronenberg, H.M., Endocrine Unit, Massachusetts General Hospital, Boston, Massachusetts, 02114, United States
Nucleotide sequence of cloned cDNAs encoding chicken preproparathyroid hormone
In order to characterize an avian parathyroid hormone gene, a λgt10 cDNA library constructed from chicken parathyroid gland mRNA was screened with a human preproparathyroid hormone (preproPTH) cDNA probe. Nucleotide sequence analysis of three independent clones confirmed that they encoded chicken preproPTH. This analysis, complemented by primer extension and Northern blot analysis of mRNA, demonstrated a 5′‐untranslated region for chicken preproPTH of 127 nucleotides, a coding region of 357 nucleotides, and a 3′‐untranslated region of approximately 2500 nucleotides. The coding sequence predicts a mature chicken PTH of 88 amino acids in contrast to the 84 amino acids of the mammalian hormones. Comparison of the avian and the mammalian hormones shows striking homology in the region of amino acids 1–32. The middle and carboxyl‐terminal portions of chicken PTH, however, differ considerably from the mammalian hormones and include deletions of sequences conserved in mammalian PTH and insertions of novel peptide sequences. Comparison of the avian and mammalian structures suggests potential alterations of the mammalian sequences that may lead to altered bioactivity and/or hormone metabolism. Copyright © 1988 ASBMR
Scientific Publication
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