D-Amino-Acid Peptide Specific for Cerebral A_-Amyloid in Man Cross-Reacts with Canine Cerebral Amyloid

2004 ◽  
pp. 402-404
Author(s):  
K Wiesehan ◽  
R Oos ◽  
J Rofina ◽  
R Linke ◽  
D Willbold ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Cerebral Amyloid

D-Amino-Acid Peptide Specific for Cerebral Aβ-Amyloid in Man Cross-Reacts with Canine Cerebral Amyloid

2004 ◽  
pp. 402-404
Author(s):  
R.P. Linke ◽  
R. Oos ◽  
J.E. Rofina ◽  
K. Wiesehan ◽  
D. Willbold ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Aβ Amyloid ◽  
Cerebral Amyloid

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

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.

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

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.

Ternary metal/nucleobase (oligonucleotide)/amino acid (peptide) complexes

1995 ◽  
Vol 59 (2-3) ◽  
pp. 147 ◽  
Author(s):  
H. Witkowski ◽  
I. Rombeck ◽  
T. Wienkötter ◽  
S. Höhmann ◽  
A. Erxleben ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Peptide ◽  
Ternary Metal ◽  
Peptide Complexes

scholarly journals In the Virion, the 11-Amino-Acid Peptide Cofactor pVIc Is Covalently Linked to the Adenovirus Proteinase

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