Amino acid sequence of porcine parathyroid hormone

Sauer, Robert T.; Niall, Hugh D.; Hogan, M. L.; Keutmann, Henry T.; O’Riordan, J. L. H.; Potts, John T.

doi:10.1021/bi00706a033

Cited by 98 publications

(34 citation statements)

References 12 publications

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“…Sequential Edman degradationi of fragmiients recovered from plasma after injection of '251-bPTH in vivo showed that the major sites of proteolysis are between positions 33 and 34 and between 36 and 37 of the intact sequence, yielding fragmnents that appear to be identical with those founid in studies 'Abbreviaitionis tused in tb1is 1)aper: MRCU, Medical Research Couniicil Units; PTH, parathyroid hormonie; I)PTH, bovine parath roid hormiionie. of unlabeled hormone.…”

Section: Introductionmentioning

confidence: 99%

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Effects of Hepatectomy, Nephrectomy, and Nephrectomy/Uremia on the Metabolism of Parathyroid Hormone in the Rat

Segre¹,

D'Amour²,

Hultman³

et al. 1981

J. Clin. Invest.

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A B S T R A C T Reports from several laboratories, showing extensive hepatic extraction of circulating parathyroid hormone, led us to examine the effect of neartotal hepatectomy on the metabolism of the hormone to circulating fragments, and on its clearance from plasma. The rate of disappearance of 1251-labeled and unlabeled bovine parathyroid hormone from plasma, and the appearance, disappearance, and chemical and immunochemical characteristics of circulating fragments were examined by gel filtration and either sequence-specific radioimmunoassays or sequence analysis using the Edman reaction. Results from awake rats subjected to near-total hepatectomy were compared with those found in sham-treated, nephrectomized, and short-term uremic rats (studied 2 d after nephrectomy). When compared with the sham-treated group, all other groups clear 1251-labeled hormone more slowly; after hepatectomy, however, the clearance rate is most strikingly decreased.After injection of intact hormone, the concentration of carboxy-terminal fragments in the circulation of hepatectomized rats is greatly reduced at all time intervals when compared with that in sham-treated rats. Sequence analysis of plasma samples, collected from rats into which 1251-labeled hormone had been injected, shows that carboxy-terminal fragments having positions 34 and 37 ofthe intact hormone sequence as their aminoterminal amino acids are abundant in sham-treated, nephrectomized, and nephrectomized/uremic rats, but are undetectable in hepatectomized rats.

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Section: Introductionmentioning

confidence: 99%

“…The present studies principally focus on the role of the liver in the metabolism of PTH (33,34). Biologic activity of bPTH-(1-84) was 3,000 Medical Research Council Units (MRCU)/ mg in the in vitro rat cortical adenylate cyclase assay (35) and 2,500 MRCU/mg in the in vivo chick hypercalcemia assay (36).…”

Section: Introductionmentioning

confidence: 99%

Effects of Hepatectomy, Nephrectomy, and Nephrectomy/Uremia on the Metabolism of Parathyroid Hormone in the Rat

Segre¹,

D'Amour²,

Hultman³

et al. 1981

J. Clin. Invest.

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“…As we showed in the accompanying report, near-total hepatectomy results in the markedly delayed clearance of intact hormone from plasma and the virtual disappearance of COOH-terminal fragments that characteristically appear in the circulation as a result of cleavage of intravenously injected intact hormone. These unique properties of the liver, particularly the liver's role in generating and releasing COOH-terminal fragments groups of lysine residues, were prepared (3,4). bPTH-(1-34) was synthesized by solid-phase methods and purified (5).…”

Section: Introductionmentioning

confidence: 99%

Metabolism of Parathyroid Hormone by Isolated Rat Kupffer Cells and Hepatocytes

Segre¹,

Perkins²,

Witters³

et al. 1981

J. Clin. Invest.

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102

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A B S T R A C Tshowed that the dominant hormonal fragments recovered in the medium have an apparent molecular weight of -6,000, lack amino-terminal antigenic determinants, and react in assays that specifically recognize determinants in the carboxy-terminal portion of the intact hormone. Amino-terminal fragments also were detected in high concentrations, particularly after short incubation periods. Radioiodinated fragments resulting from incubation of 125I-labeled bovine parathyroid hormone with Kupffer cells had the same apparent size as fragments derived from the metabolism of unlabeled, intact hormone; when analyzed by Edman degradation, positions 34 and 37 of the intact hormone sequence were the amino-terminal amino acids of these dominant carboxy-terminal fragments. Hepatocytes did not hydrolyze the hormone. Thus, metabolism of parathyroid hormone by Kupffer cells results in the appearance of fragments in the media

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“…Overall, these changes represent conservative amino (Vasicek et al 1983), macaque (unpublished, Q9XT35), rat (Heinrich et al 1984), bovine (Kronenberg et al 1979), porcine (Sauer et al 1974), and canine (Rosol et al 1995) PTH are used. Residues conserved across most species are left unshaded, whereas somewhat conserved and highly variable residues have been highlighted by light and dark shading, respectively, using the BoxShade program (www.ch.embnet.org).…”

Section: Genomic Organization and Deduced Amino Acid Sequencementioning

confidence: 99%

The murine gene encoding parathyroid hormone: genomic organization, nucleotide sequence and transcriptional regulation

Tong²,

Hiou-Tim³

et al. 2002

Journal of Molecular Endocrinology

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The type 1 parathyroid hormone receptor (PTHR1) binds, with equal affinity, two ligands with distinct biological functions: PTH, the major peptide hormone controlling calcium homeostasis, and the paracrine factor, PTH-related peptide (PTHrP), a local regulator of cellular proliferation and differentiation. To clarify the complexity of possible interactions between two distinct ligands, PTH and PTHrP, and their common receptor in the intact organism, and to identify as yet unrecognized roles for PTH in normal physiology, we have cloned and characterized the structural organization, nucleotide sequence and transcriptional regulation of the murine gene encoding PTH. One recombinant clone isolated from a mouse genomic library contained 14 kb of DNA, encompassing the entire Pth gene. The transcriptional unit spans 3·2 kb of genomic DNA and, analogous to the human PTH gene, it is interrupted by two introns. The deduced mRNA encodes the 115-amino acid precursor, preproPTH. Comparison of the murine preproPTH sequence with other mammalian forms of the protein shows it to be highly conserved and to share limited structural similarity to PTHrP at the amino-terminal region, a domain critical for binding and activation of their common receptor. Putative binding motifs for the transcription factors sex-determining region Y gene product, transcriptional repressor CDP, hepatic nuclear factor 3β, GATA-binding factor 1, glucocorticoid receptor, SRY-related high mobility group box protein 5 and cAMP response element binding protein were identified in the 5′ flanking region of the Pth gene. When placed upstream of a reporter gene, these sequences failed to confer transcriptional regulation in response to 1,25(OH) 2 vitamin D 3 , but responded positively to the addition of isoproterenol and forskolin. Mutational analysis identified a cAMP-response element in the Pth promoter.

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Amino acid sequence of porcine parathyroid hormone

Cited by 98 publications

References 12 publications

Effects of Hepatectomy, Nephrectomy, and Nephrectomy/Uremia on the Metabolism of Parathyroid Hormone in the Rat

Effects of Hepatectomy, Nephrectomy, and Nephrectomy/Uremia on the Metabolism of Parathyroid Hormone in the Rat

Metabolism of Parathyroid Hormone by Isolated Rat Kupffer Cells and Hepatocytes

The murine gene encoding parathyroid hormone: genomic organization, nucleotide sequence and transcriptional regulation

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