Beyond CGRP: the calcitonin peptide family as targets for migraine and pain

2021 ◽  
Author(s):  
T. A. Rees ◽  
E. R. Hendrikse ◽  
D. L. Hay ◽  
C. S. Walker
Keyword(s):  
Peptide Family

Recent advances in natriuretic peptide family genes and cardiovas-cular diseases

2012 ◽  
Vol 34 (2) ◽  
pp. 127-133 ◽  
Author(s):  
Zhi-Jun WU ◽  
Wei JIN ◽  
Feng-Ru ZHANG ◽  
Yan LIU
Keyword(s):  
Natriuretic Peptide ◽  
Recent Advances ◽  
Peptide Family

scholarly journals Natriuretic Peptide Family as a Novel Antimigration Factor of Vascular Smooth Muscle Cells

1997 ◽  
Vol 17 (4) ◽  
pp. 731-736 ◽  
Author(s):  
Miwako Ikeda ◽  
Masakazu Kohno ◽  
Kenichi Yasunari ◽  
Koji Yokokawa ◽  
Takeshi Horio ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Natriuretic Peptide ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Peptide Family

scholarly journals The PSY Peptide Family—Expression, Modification and Physiological Implications

Genes ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 218
Author(s):  
Amalie Scheel Tost ◽  
Astrid Kristensen ◽  
Lene Irene Olsen ◽  
Kristian Buhl Axelsen ◽  
Anja Thoe Fuglsang
Keyword(s):  
Plant Development ◽  
Higher Plants ◽  
Expression Patterns ◽  
Transcriptional Level ◽  
Amino Acid Peptide ◽  
Developmental Factors ◽  
Peptide Family ◽  
The Family ◽  
Modified Peptides ◽  
High Conservation

Small post-translationally modified peptides are gaining increasing attention as important signaling molecules in plant development. In the family of plant peptides containing tyrosine sulfation (PSYs), only PSY1 has been characterized at the mature level as an 18-amino-acid peptide, carrying one sulfated tyrosine, and involved in cell elongation. This review presents seven additional homologs in Arabidopsis all sharing high conservation in the active peptide domain, and it shows that PSY peptides are found in all higher plants and mosses. It is proposed that all eight PSY homologs are post-translationally modified to carry a sulfated tyrosine and that subtilisin-like subtilases (SBTs) are involved in the processing of PSY propeptides. The PSY peptides show differential expression patterns indicating that they serve several distinct functions in plant development. PSY peptides seem to be at least partly regulated at the transcriptional level, as their expression is greatly influenced by developmental factors. Finally, a model including a receptor in addition to PSY1R is proposed.

scholarly journals Receptor Activity-modifying Protein-directed G Protein Signaling Specificity for the Calcitonin Gene-related Peptide Family of Receptors

2016 ◽  
Vol 291 (42) ◽  
pp. 21925-21944 ◽  
Author(s):  
Cathryn Weston ◽  
Ian Winfield ◽  
Matthew Harris ◽  
Rose Hodgson ◽  
Archna Shah ◽  
...  
Keyword(s):  
G Protein ◽  
Calcitonin Gene Related Peptide ◽  
Receptor Activity ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Signaling Specificity ◽  
Related Peptide ◽  
Peptide Family ◽  
Calcitonin Gene

scholarly journals Antimicrobial Nodule-Specific Cysteine-Rich Peptides Induce Membrane Depolarization-Associated Changes in the Transcriptome of Sinorhizobium meliloti

2013 ◽  
Vol 79 (21) ◽  
pp. 6737-6746 ◽  
Author(s):  
Hilda Tiricz ◽  
Attila Szűcs ◽  
Attila Farkas ◽  
Bernadett Pap ◽  
Rui M. Lima ◽  
...  
Keyword(s):  
Stress Responses ◽  
Sinorhizobium Meliloti ◽  
Antimicrobial Agents ◽  
Cellular Functions ◽  
Gram Positive ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Peptide Family ◽  
Wide Range ◽  
Natural Target

ABSTRACTLeguminous plants establish symbiosis with nitrogen-fixing alpha- and betaproteobacteria, collectively called rhizobia, which provide combined nitrogen to support plant growth. Members of the inverted repeat-lacking clade of legumes impose terminal differentiation on their endosymbiotic bacterium partners with the help of the nodule-specific cysteine-rich (NCR) peptide family composed of close to 600 members. Among the few tested NCR peptides, cationic ones had antirhizobial activity measured by reduction or elimination of the CFU and uptake of the membrane-impermeable dye propidium iodide. Here, the antimicrobial spectrum of two of these peptides, NCR247 and NCR335, was investigated, and their effect on the transcriptome of the natural targetSinorhizobium melilotiwas characterized. Both peptides were able to kill quickly a wide range of Gram-negative and Gram-positive bacteria; however, their spectra were only partially overlapping, and differences were found also in their efficacy on given strains, indicating that the actions of NCR247 and NCR335 might be similar though not identical. Treatment ofS. meliloticultures with either peptide resulted in a quick downregulation of genes involved in basic cellular functions, such as transcription-translation and energy production, as well as upregulation of genes involved in stress and oxidative stress responses and membrane transport. Similar changes provoked mainly in Gram-positive bacteria by antimicrobial agents were coupled with the destruction of membrane potential, indicating that it might also be a common step in the bactericidal actions of NCR247 and NCR335.

scholarly journals Cysteine-Rich Peptide Family with Unusual Disulfide Connectivity from Jasminum sambac

2015 ◽  
Vol 78 (11) ◽  
pp. 2791-2799 ◽  
Author(s):  
Geeta Kumari ◽  
Aida Serra ◽  
Joon Shin ◽  
Phuong Q. T. Nguyen ◽  
Siu Kwan Sze ◽  
...  
Keyword(s):  
Peptide Family ◽  
Jasminum Sambac

The natriuretic-peptide family

The Lancet ◽  
1997 ◽  
Vol 349 (9061) ◽  
pp. 1307-1310 ◽  
Author(s):  
Martin R Wilkins ◽  
Juliana Redondo ◽  
Lesley A Brown
Keyword(s):  
Natriuretic Peptide ◽  
Peptide Family

scholarly journals Are GPCRs Still a Source of New Targets?

2013 ◽  
Vol 18 (9) ◽  
pp. 947-966 ◽  
Author(s):  
Stephen L. Garland
Keyword(s):  
Drug Targets ◽  
Protein Complexes ◽  
X Ray Crystallography ◽  
Peptide Family ◽  
Wide Range ◽  
The Family ◽  
Receptor Pharmacology ◽  
Technical Advances ◽  
Allosteric Mechanisms ◽  
G Protein Coupled

G-protein–coupled receptors (GPCRs) still offer enormous scope for new therapeutic targets. Currently marketed agents are dominated by those with activity at aminergic receptors and yet they account for only ~10% of the family. Progress up until now with other subfamilies, notably orphans, Family A/peptide, Family A/lipid, Family B, Family C, and Family F, has been, at best, patchy. This may be attributable to the heterogeneous nature of GPCRs, their endogenous ligands, and consequently their binding sites. Our appreciation of receptor similarity has arguably been too simplistic, and screening collections have not necessarily been well suited to identifying leads in new areas. Despite the relative shortage of high-quality tool molecules in a number of cases, there is an emerging, and increasingly substantial, body of evidence associating many as yet “undrugged” receptors with a very wide range of diseases. Significant advances in our understanding of receptor pharmacology and technical advances in screening, protein X-ray crystallography, and ligand design methods are paving the way for new successes in the area. Exploitation of allosteric mechanisms; alternative signaling pathways such as G12/13, Gβγ, and β-arrestin; the discovery of “biased” ligands; and the emergence of GPCR-protein complexes as potential drug targets offer scope for new and much improved drugs.

scholarly journals Conserved Structure and Function in the Granulysin and NK-Lysin Peptide Family

2005 ◽  
Vol 73 (10) ◽  
pp. 6332-6339 ◽  
Author(s):  
Charlotte M. A. Linde ◽  
Susanna Grundström ◽  
Erik Nordling ◽  
Essam Refai ◽  
Patrick J. Brennan ◽  
...  
Keyword(s):  
Mycobacterium Smegmatis ◽  
Three Dimensional ◽  
Antimycobacterial Activity ◽  
Structure And Function ◽  
Loop Structure ◽  
E Coli ◽  
Short Loop ◽  
Peptide Family ◽  
And Function ◽  
Related Proteins

ABSTRACT Granulysin and NK-lysin are homologous bactericidal proteins with a moderate residue identity (35%), both of which have antimycobacterial activity. Short loop peptides derived from the antimycobacterial domains of granulysin, NK-lysin, and a putative chicken NK-lysin were examined and shown to have comparable antimycobacterial but variable Escherichia coli activities. The known structure of the NK-lysin loop peptide was used to predict the structure of the equivalent peptides of granulysin and chicken NK-lysin by homology modeling. The last two adopted a secondary structure almost identical to that of NK-lysin. All three peptides form very similar three-dimensional (3-D) architectures in which the important basic residues assume the same positions in space. The basic residues in granulysin are arginine, while those in NK-lysin and chicken NK-lysin are a mixture of arginine and lysine. We altered the ratio of arginine to lysine in the granulysin fragment to examine the importance of basic residues for antimycobacterial activity. The alteration of the amino acids reduced the activity against E. coli to a larger extent than that against Mycobacterium smegmatis. In granulysin, the arginines in the loop structure are not crucial for antimycobacterial activity but are important for cytotoxicity. We suggest that the antibacterial domains of the related proteins granulysin, NK-lysin, and chicken NK-lysin have conserved their 3-D structure and their function against mycobacteria.

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