Angiogenesis Inhibition by a Short 13 Amino Acid Peptide Sequence of Tetrastatin, the α4(IV) NC1 Domain of Collagen IV

The lettuce midrib rot pathogen Pseudomonas cichorii SF1-54 produces seven bioactive compounds with biosurfactant properties. Two compounds exhibited necrosis-inducing activity on chicory leaves. The structure of the two phytotoxic compounds, named cichopeptin A and B, was tentatively characterized. They are related cyclic lipopeptides composed of an unsaturated C12-fatty acid chain linked to the N-terminus of a 22–amino acid peptide moiety. Cichopeptin B differs from cichopeptin A only in the last C-terminal amino acid residue, which is probably Val instead of Leu/Ile. Based on peptide sequence similarity, cichopeptins are new cyclic lipopeptides related to corpeptin, produced by the tomato pathogen Pseudomonas corrugata. Production of cichopeptin is stimulated by glycine betaine but not by choline, an upstream precursor of glycine betaine. Furthermore, a gene cluster encoding cichopeptin synthethases, cipABCDEF, is responsible for cichopeptin biosynthesis. A cipA-deletion mutant exhibited significantly less virulence and rotten midribs than the parental strain upon spray inoculation on lettuce. However, the parental and mutant strains multiplied in lettuce leaves at a similar rate. These results demonstrate that cichopeptins contribute to virulence of P. cichorii SF1-54 on lettuce.

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Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion

Glycobiology ◽

10.1093/glycob/5.4.435 ◽

1995 ◽

Vol 5 (4) ◽

pp. 435-441 ◽

Cited By ~ 29

Author(s):

Heike Hall ◽

Thomas Vorherr ◽

Melitta Schachner

Keyword(s):

Cell Adhesion ◽

Amino Acid ◽

Peptide Sequence ◽

Carbohydrate Binding ◽

Amino Acid Peptide

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Glycoinositol phospholipid anchor and protein C-terminus of bovine erythrocyte acetylcholinesterase: analysis by mass spectrometry and by protein and DNA sequencing

Biochemical Journal ◽

10.1042/bj3140817 ◽

1996 ◽

Vol 314 (3) ◽

pp. 817-825 ◽

Cited By ~ 15

Author(s):

Robert HAAS ◽

Brent C. JACKSON ◽

Bruce REINHOLD ◽

John D. FOSTER ◽

Terrone L. ROSENBERRY

Keyword(s):

Mass Spectrometry ◽

Amino Acid ◽

Dna Sequencing ◽

Protein Sequencing ◽

Peptide Sequence ◽

Partial Reduction ◽

Bovine Erythrocyte ◽

Gpi Anchor ◽

Amino Acid Peptide ◽

Fragmentation Patterns

Purified bovine erythrocyte acetylcholinesterase (AChE) was radiomethylated on its amine groups and incubated with bacterial phosphatidylinositol-specific phospholipase C to remove the lipid portion of the AChE glycoinositol phospholipid (GPI) anchor, and a C-terminal tryptic fragment that contained the residual GPI glycan was isolated by HPLC. Analysis by electrospray-ionization mass spectrometry revealed a parent ion of m/z 3798. The fragmentation patterns produced by collision-induced dissociation mass spectrometry of the +4 and +5 states of the parent ion indicated a 23-amino acid peptide in amide linkage to ethanolamine-PO4-Hex-Hex-Hex(PO4-ethanolamine) (HexNAc)-HexN(Me)2-inositol phosphate. The glycan structure is completely consistent with that obtained previously for the GPI anchor of human erythrocyte AChE except for the addition of the HexNAc substituent. A nearly complete peptide sequence was deduced from the fragmentation patterns, although four assignments were based only on single fragments of very low abundance. To resolve this uncertainty, a segment of bovine genomic DNA corresponding to the C-terminal AChE sequence was amplified by PCR. DNA sequencing established the 23-amino acid peptide sequence to be FLPKLLSATASEAPCTCSGPAHG, in agreement with the MS data and consistent with results from Edman protein sequencing. Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a …CTC… motif, in contrast with human AChE which contains only a single cysteine in this segment. Although bovine AChE contained no free thiol groups reactive with iodo[14C]acetamide, partial reduction and alkylation with iodo[14C]acetamide revealed that conversion into monomers occurred with an overall incorporation of only one alkyl group per monomer. An identical level of alkylation was observed when dimeric human AChE was converted into monomers by partial reduction. The question of whether the bovine AChE contains one or two intersubunit disulphide linkages is considered.

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Comparison between the Backbone Dynamics of an 11-Amino Acid Peptide Sequence in α-Helical and β-Hairpin Structural Contexts†

Biochemistry ◽

10.1021/bi0608919 ◽

2006 ◽

Vol 45 (37) ◽

pp. 11179-11189 ◽

Cited By ~ 1

Author(s):

Virginia A. Jarymowycz ◽

Ewa Krupinska ◽

Martin J. Stone

Keyword(s):

Amino Acid ◽

Backbone Dynamics ◽

Peptide Sequence ◽

Amino Acid Peptide

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Stimulation of gonadotropin release by a non-GnRH peptide sequence of the GnRH precursor

Science ◽

10.1126/science.3082009 ◽

1986 ◽

Vol 232 (4746) ◽

pp. 68-70 ◽

Cited By ~ 51

Author(s):

RP Millar ◽

PJ Wormald ◽

RC Milton

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Basic Amino Acid ◽

Prolactin Secretion ◽

Biologically Active ◽

Peptide Sequence ◽

Pituitary Cells ◽

Amino Acid Residues ◽

Amino Acid Peptide ◽

Gonadotropin Release

The human gonadotropin-releasing hormone (GnRH) precursor comprises the GnRH sequence followed by an extension of 59 amino acids. Basic amino acid residues in the carboxyl terminal extension may represent sites of processing to biologically active peptides. A synthetic peptide comprising the first 13 amino acids (H X Asp-Ala-Glu-Asn-Leu-Ile-Asp-Ser-Phe-Gln-Glu-Ile-Val X OH) of the 59-amino acid peptide was found to stimulate the release of gonadotropic hormones from human and baboon anterior pituitary cells in culture. The peptide did not affect thyrotropin or prolactin secretion. A GnRH antagonist did not inhibit gonadotropin stimulation by the peptide, and the peptide did not compete with GnRH for GnRH pituitary receptors, indicating that the action of the peptide is independent of the GnRH receptor. The GnRH precursor contains two distinct peptide sequences capable of stimulating gonadotropin release from human and baboon pituitary cells.

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Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100147776 ◽

1993 ◽

Vol 51 ◽

pp. 388-389

Author(s):

Chi-Ming Wei ◽

Margaret Hukee ◽

Christopher G.A. McGregor ◽

John C. Burnett

Keyword(s):

Amino Acid ◽

Natriuretic Peptide ◽

Vascular Tone ◽

Cardiac Tissue ◽

Ring Structure ◽

Terminal Amino Acid ◽

Amino Acid Peptide ◽

Normal Human ◽

Terminal Amino ◽

The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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Glucose phosphorylation. Interaction of a 50-amino acid peptide of yeast hexokinase with trinitrophenyl ATP.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)34124-9 ◽

1990 ◽

Vol 265 (9) ◽

pp. 5324-5328

Author(s):

K K Arora ◽

P Shenbagamurthi ◽

M Fanciulli ◽

P L Pedersen

Keyword(s):

Amino Acid ◽

Amino Acid Peptide ◽

Glucose Phosphorylation ◽

Yeast Hexokinase

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A C-peptide complex with albumin and Zn2+ increases measurable GLUT1 levels in membranes of human red blood cells

Scientific Reports ◽

10.1038/s41598-020-74527-6 ◽

2020 ◽

Vol 10 (1) ◽

Author(s):

M. Geiger ◽

T. Janes ◽

H. Keshavarz ◽

S. Summers ◽

C. Pinger ◽

...

Keyword(s):

Type 1 Diabetes ◽

Amino Acid ◽

Blood Cells ◽

Glucose Transporter ◽

Peptide Binding ◽

C Peptide ◽

Amino Acid Peptide ◽

Human Red Blood Cells

Abstract People with type 1 diabetes (T1D) require exogenous administration of insulin, which stimulates the translocation of the GLUT4 glucose transporter to cell membranes. However, most bloodstream cells contain GLUT1 and are not directly affected by insulin. Here, we report that C-peptide, the 31-amino acid peptide secreted in equal amounts with insulin in vivo, is part of a 3-component complex that affects red blood cell (RBC) membranes. Multiple techniques were used to demonstrate saturable and specific C-peptide binding to RBCs when delivered as part of a complex with albumin. Importantly, when the complex also included Zn2+, a significant increase in cell membrane GLUT1 was measured, thus providing a cellular effect similar to insulin, but on a transporter on which insulin has no effect.

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