scholarly journals C Terminus L‐type Ca 2+ Channel Calmodulin‐Binding Domains are ‘Auto‐Agonist’ Ligands in Rabbit Ventricular Myocytes

2003 ◽  
Vol 550 (3) ◽  
pp. 731-738 ◽  
Author(s):  
Igor Dzhura ◽  
Yuejin Wu ◽  
Rong Zhang ◽  
Roger J. Colbran ◽  
Susan L. Hamilton ◽  
...  
Keyword(s):  
Ventricular Myocytes ◽  
Calmodulin Binding ◽  
Binding Domains ◽  
C Terminus ◽  
Rabbit Ventricular Myocytes ◽  
Agonist Ligands

scholarly journals Regulation of Sarcoplasmic Reticulum [Ca2+] during Rest in Rabbit Ventricular Myocytes

2011 ◽  
Vol 100 (3) ◽  
pp. 560a
Author(s):  
Elisa Bovo ◽  
Aleksey V. Zima
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Ventricular Myocytes ◽  
Rabbit Ventricular Myocytes

Effects of Volatile Anesthetic Isoflurane on ATP-Sensitive K+Channels in Rabbit Ventricular Myocytes

1996 ◽  
Vol 229 (3) ◽  
pp. 852-856 ◽  
Author(s):  
Jin Han ◽  
Euiyong Kim ◽  
Won Kyung Ho ◽  
Yung E. Earm
Keyword(s):  
Ventricular Myocytes ◽  
Volatile Anesthetic ◽  
K Channels ◽  
Rabbit Ventricular Myocytes

Calmodulin-binding peptides isolated from α-casein peptone

1995 ◽  
Vol 62 (4) ◽  
pp. 587-592 ◽  
Author(s):  
Kenji Kizavva ◽  
Keiko Naganuma ◽  
Umeji Murakami
Keyword(s):  
Enzyme Activity ◽  
Cyclic Nucleotide ◽  
Cyclic Nucleotide Phosphodiesterase ◽  
Phosphodiesterase Activity ◽  
Calmodulin Binding ◽  
C Terminus ◽  
Binding Peptides

SUMMARYPeptides that inhibit calmodulin-dependent cyclic nucleotide phosphodiesterase were isolated from a pepsin digest of α-casein. Analysis of these peptides showed that they corresponded to the αs2-casein sequences 164–179 (Leu–Lys–Lys–Ile–Ser–Gln–Arg–Tyr–Gln–Lys–Phe–Ala–Leu–Pro–Gln–Tyr), 183–206 (Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr) and 183–207 (C-terminus, Val–Tyr–Gln–His–Gln–Lys–Ala–Met–Lys–Pro–Trp–Ile–Gln–Pro–Lys–Thr–Lys–Val–Ile–Pro–Tyr–Val–Arg–Tyr–Leu). These peptides inhibited calmodulin-induced cyclic nucleotide phosphodiesterase activity over the range 1–50 μM without affecting the basal enzyme activity. These results demonstrated that the affinities of these peptides for calmodulin are comparable to the affinities of certain endogenous neurohormones and proteins that interact with calmodulin.

scholarly journals Caveolae in Rabbit Ventricular Myocytes: Distribution and Dynamic Diminution after Cell Isolation

2017 ◽  
Vol 113 (5) ◽  
pp. 1047-1059 ◽  
Author(s):  
Rebecca A.B. Burton ◽  
Eva A. Rog-Zielinska ◽  
Alexander D. Corbett ◽  
Rémi Peyronnet ◽  
Ilona Bodi ◽  
...  
Keyword(s):  
Ventricular Myocytes ◽  
Cell Isolation ◽  
Rabbit Ventricular Myocytes

scholarly journals Influence of Molecular Design on the Targeting Properties of ABD-Fused Mono- and Bi-Valent Anti-HER3 Affibody Therapeutic Constructs

Cells ◽  
2018 ◽  
Vol 7 (10) ◽  
pp. 164 ◽  
Author(s):  
Mohamed Altai ◽  
Charles Leitao ◽  
Sara Rinne ◽  
Anzhelika Vorobyeva ◽  
Christina Atterby ◽  
...  
Keyword(s):  
Half Life ◽  
Molecular Design ◽  
Growth Factor Receptor ◽  
Fusion Construct ◽  
Affibody Molecules ◽  
Binding Domains ◽  
Biodistribution Studies ◽  
C Terminus ◽  
Type 3

Overexpression of human epidermal growth factor receptor type 3 (HER3) is associated with tumour cell resistance to HER-targeted therapies. Monoclonal antibodies (mAbs) targeting HER3 are currently being investigated for treatment of various types of cancers. Cumulative evidence suggests that affibody molecules may be appropriate alternatives to mAbs. We previously reported a fusion construct (3A3) containing two HER3-targeting affibody molecules flanking an engineered albumin-binding domain (ABD035) included for the extension of half-life in circulation. The 3A3 fusion protein (19.7 kDa) was shown to delay tumour growth in mice bearing HER3-expressing xenografts and was equipotent to the mAb seribantumab. Here, we have designed and explored a series of novel formats of anti-HER3 affibody molecules fused to the ABD in different orientations. All constructs inhibited heregulin-induced phosphorylation in HER3-expressing BxPC-3 and DU-145 cell lines. Biodistribution studies demonstrated extended the half-life of all ABD-fused constructs, although at different levels. The capacity of our ABD-fused proteins to accumulate in HER3-expressing tumours was demonstrated in nude mice bearing BxPC-3 xenografts. Formats where the ABD was located on the C-terminus of affibody binding domains (3A, 33A, and 3A3) provided the best tumour targeting properties in vivo. Further development of these promising candidates for treatment of HER3-overexpressing tumours is therefore justified.

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