Strategies for the biosynthesis of bioactive peptides

Mains, Richard E.; Eipper, Betty A.; Glembotski, Christopher C.; Dores, Robert M.

doi:10.1016/0166-2236(83)90100-5

Cited by 191 publications

(72 citation statements)

References 36 publications

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“…The other difference between the mature PF-1 peptide and the structure predicted by Pungercar et al is found at the C-terminus, where the last three residues (GRR) are removed. The presence of GIy-X-X (X = basic amino acid) sequence at the carboxyl ends of many precursors to amidated peptides has been identified as the universal combined amidation/proteolytic cleavage recognition site [31]. Therefore, prophenin-1 most likely also exists as the amidated form, as do several other cathelin-encoded peptides of porcine (protegrin and PR-39) and bovine leukocytes (indolicidin).…”

Section: Discussionmentioning

confidence: 99%

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Harwig

Kokryakov²,

Swiderek

et al. 1995

FEBS Letters

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We purified and characterized an unusual antimicrobial peptide, prophenin-1 (PF-I), from porcine leukocytes. The peptide had a mass of 8,683 and contained 79 residues, including 42 (53.2%) prolines and 15 (19.0%) phenylalanines. Its N-terminal 60 residues consisted of three perfect and three nearly perfect repeats of a decamer, FPPPNFPGPR. Prophenin-I was encoded on a cathelin-containing precursor and showed substantially more activity against E. coli, a Gram-negative bacterium, than against Listeria monocytogenes, a Gram-positive organism, in vitro.

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Section: Discussionmentioning

confidence: 99%

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Harwig

Kokryakov²,

Swiderek

et al. 1995

FEBS Letters

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“…O. and 0.05% NaN 3 ) containing 0.5% normal rabbit serum. The anti-rat ghrelin-(1-11) or anti-rat ghrelin- (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28) antisera were used at final dilutions of 1:6,000,000 and 1:20,000, respectively. After incubation for 12 h, 100 l of 125 I-labeled tracer (15,000 cpm) was added.…”

Section: Methodsmentioning

confidence: 99%

“…Many of the known proteolytic precursor cleavage events occur at pairs of basic amino acid residues (Lys or Arg), and both basic residues are usually absent from the resultant products (19). However, some proteolytic cleavages, as in the case of cholecystokinin, occur immediately after a C-terminal single basic residue (especially Arg) (20).…”

Section: Figmentioning

confidence: 99%

Structural Divergence of Human Ghrelin

Hosoda¹,

Kojima²,

Mizushima³

et al. 2003

Journal of Biological Chemistry

284

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Ghrelin, a novel 28-amino acid peptide with an n-octanoyl modification at Ser 3 , was isolated from rat stomach and found to be an endogenous ligand for the growthhormone secretagogue receptor (GHS-R). This octanoyl modification is essential for ghrelin-induced GH release. We report here the purification and identification of human ghrelin from the stomach, as well as structural analysis of the human ghrelin gene and quantitation of changes in plasma ghrelin concentration before and after gastrectomy. Human ghrelin was purified from the stomach by gel filtration and high performance liquid chromatography, using a ghrelin-specific radioimmunoassay and an intracellular calcium influx assay on a stable cell line expressing GHS-R to test the fractions. In the course of purification, we isolated human ghrelin of the expected size, as well as several other ghrelin-derived molecules. Classified into four groups by the type of acylation observed at Ser 3 ; these peptides were found to be non-acylated, octanoylated (C8:0), decanoylated (C10:0), and possibly decenoylated (C10:1). All peptides found were either 27 or 28 amino acids in length, the former lacking the C-terminal Arg 28, and are derived from the same ghrelin precursor through two alternative pathways. The major active form of human ghrelin is a 28-amino acid peptide octanoylated at Ser 3 , as was found for rat ghrelin. Synthetic octanoylated and decanoylated ghrelins produce intracellular calcium increases in GHS-R-expressing cells and stimulate GH release in rats to a similar degree. Both ghrelin and the ghrelin-derived molecules were found to be present in plasma as well as stomach tissue. Plasma levels of immunoreactive ghrelin after total gastrectomy in three patients were reduced to approximately half of their pre-gastrectomy values, after which they gradually increased. This suggests that the stomach is the major source of circulating ghrelin and that other tissues compensate for the loss of ghrelin production after gastrectomy.

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“…Below the bovine nucleotide sequence the porcine differences are indicated as well as the amino acid changes. The GAL sequence is outlined; the amide on the C-terminal alanine residue of galanin contributed by the glycine [17] residue is next to it (dotted box). The ATAA sequence (bases 507-510) thought to be involved in polyadenylation [22] is underlined.…”

Section: Screening Of the Cdna Library And Sequence Analysismentioning

confidence: 99%

Nucleotide sequence analysis of cDNAs encoding a bovine galanin precursor protein in the adrenal medulla and chemical isolation of bovine gut galanin

1988

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A description is given of the primary structure of a bovine adrenal medullary precursor protein (123 amino acids), containing a nonrepetitive galanin sequence, different in four amino acid positions from pig galanin, structural information deduced from the nucleotide sequence analysis of two cDNA clones. Pairs of lysine and arginine residues separate the galanin sequence N-terminally from the initiating methionine and a 29 amino acid leader peptide and C-terminally from a 59 amino acid peptide. The deduced amino acid composition was confirmed by the isolation and determination of the amino acid composition for bovine intestinal galanin. Northern blot analysis revealed the presence of an apparent single galanin mRNA species, of approx. 85&900 bases in size, which was present in a population of chromaffin cells scattered throughout the bovine adrenal medulla.

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Strategies for the biosynthesis of bioactive peptides

Cited by 191 publications

References 36 publications

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Prophenin‐1, an exceptionally proline‐rich antimicrobial peptide from porcine leukocytes

Structural Divergence of Human Ghrelin

Nucleotide sequence analysis of cDNAs encoding a bovine galanin precursor protein in the adrenal medulla and chemical isolation of bovine gut galanin

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