scholarly journals Neuropeptide S receptor in GtoPdb v.2021.3

2021 ◽  
Vol 2021 (3) ◽  
Author(s):  
Girolamo Caló ◽  
Olivier Civelli ◽  
Rainer K. Reinscheid ◽  
Chiara Ruzza

The neuropeptide S receptor (NPS, provisional nomenclature [23]) responds to the 20 amino-acid peptide neuropeptide S derived from a precursor (NPS, P0C0P6).

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Girolamo Caló ◽  
Olivier Civelli ◽  
Rainer K. Reinscheid ◽  
Chiara Ruzza

The neuropeptide S receptor (NPS, provisional nomenclature [18]) responds to the 20 amino-acid peptide neuropeptide S derived from a precursor (NPS, P0C0P6).


Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett

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.


2020 ◽  
Vol 10 (1) ◽  
Author(s):  
M. Geiger ◽  
T. Janes ◽  
H. Keshavarz ◽  
S. Summers ◽  
C. Pinger ◽  
...  

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.


1995 ◽  
Vol 59 (2-3) ◽  
pp. 147 ◽  
Author(s):  
H. Witkowski ◽  
I. Rombeck ◽  
T. Wienkötter ◽  
S. Höhmann ◽  
A. Erxleben ◽  
...  

Virology ◽  
2002 ◽  
Vol 296 (2) ◽  
pp. 234-240 ◽  
Author(s):  
William J. McGrath ◽  
Katharine S. Aherne ◽  
Walter F. Mangel

2010 ◽  
Vol 11 (2) ◽  
pp. 141-142
Author(s):  
B. Zapala ◽  
A. Sliwa ◽  
J. Goralska ◽  
L. Kaczynski ◽  
I. Wybranska

Author(s):  
Bhupinder Kapoor ◽  
Arshid Nabi ◽  
Reena Gupta ◽  
Mukta Gupta

  Objective: The increased microbial resistance against commercially available drugs initiated the development of novel and safe antimicrobial agents in last few decades. In this view, a series of amino acid/dipeptide derivatives of quinazolin-3(4H)-one was synthesized and was evaluated for their antimicrobial potential.Method: Synthesis of amino acid/peptide derivatives were carried out by coupling 5-(2-(2-chlorophenyl)-4-oxoquinazolin-3(4H)-yl)-2-hydroxy benzoic acid with amino acid/dipeptide methyl esters in the presence of dicyclohexylcarbodiimide and N-methylmorpholine. The chemical structures of synthesized compounds were characterized by 1H nuclear magnetic resonance and infrared spectroscopy and were screened for antibacterial activity by disc diffusion method.Results: All the synthesized derivatives exhibited moderate to significant antibacterial activity against both Gram-positive and Gram-negative bacteria. The potency of compound 5d was comparable to standard drug ciprofloxacin in all the strains of bacteria used. The compound 5a was found to be more active against Streptococcus pyogenes and Staphylococcus aureus while compound 5c against Pseudomonas aeruginosa and Escherichia coli. Conclusion: Peptide derivatives of quinazolinone are promising antimicrobial agent and can be used for the synthesis of other novel compounds.


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