Serine 68 Phospholemman Phosphorylation during Forskolin-Induced Swine Carotid Artery Relaxation | Zendy

Christopher M. Rembold | Zendy; Marcia L. Ripley | Zendy; Melissa K. Meeks | Zendy; Lisa M. Geddis | Zendy; Howard Kutchai | Zendy; Francesca M. Marassi | Zendy; Joseph Y. Cheung | Zendy; J. Randall Moorman | Zendy

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Serine 68 Phospholemman Phosphorylation during Forskolin-Induced Swine Carotid Artery Relaxation

Author(s) -

Christopher M. Rembold,

Marcia L. Ripley,

Melissa K. Meeks,

Lisa M. Geddis,

Howard Kutchai,

Francesca M. Marassi,

Joseph Y. Cheung,

J. Randall Moorman

Publication year - 2005

Publication title -

journal of vascular research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.58

H-Index - 74

eISSN - 1423-0135

pISSN - 1018-1172

DOI - 10.1159/000088102

Subject(s) - phosphorylation , forskolin , medicine , endocrinology , extracellular , biology , stimulation , protein kinase a , biochemistry

Phospholemman (PLM) is an abundant phosphoprotein in the plasma membrane of cardiac, skeletal and smooth muscle. It is a member of the FXYD family of proteins that bind to and regulate the Na,K-ATPase. Protein kinase A (PKA) is known to phosphorylate PLM on serine 68 (S68), although the functional effect of S68 PLM phosphorylation is unclear. We therefore evaluated S68 PLM phosphorylation in swine carotid arteries.

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