Membrane-mediated actions of 1,25-dihydroxy vitamin D3: A review of the roles of phospholipase A2 activating protein and Ca2+/calmodulin-dependent protein kinase II

Maryam Doroudi, Zvi Schwartz, Barbara D. Boyan

Research output: Contribution to journalReview articlepeer-review

28 Scopus citations

Abstract

The secosteroid 1α,25-dihydroxy vitamin D3 [1α,25(OH)2D3] acts on cells via classical steroid hormone receptor-mediated gene transcription and by initiating rapid membrane-mediated signaling pathways. In its membrane-initiated pathway, after 1α,25(OH)2D3 interacts with protein disulfide isomerase, family A, member 3 (Pdia3) in caveolae, phospholipase A2 (PLA2) and protein kinase C (PKC) are activated. Recent efforts to determine the signaling proteins involved in the 1α,25(OH)2D3 signal from Pdia3 to PLA2 have indicated that phospholipase A2 activating protein (PLAA) and Ca2+/calmodulin-dependent kinase II (CaMKII) are required. PLAA is located in caveolae, where it interacts with Pdia3 and caveolin-1 (Cav-1) to initiate rapid signaling via CaMKII, activating PLA2, leading to activation of protein kinase C (PKC) and PKC-dependent responses.

Original languageEnglish (US)
Pages (from-to)81-84
Number of pages4
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume147
DOIs
StatePublished - Mar 2015

Keywords

  • 1α,25(OH)D
  • Ca/calmodulin-dependent protein kinase II
  • PDIA3
  • PLA
  • PLAA
  • Protein kinase C

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'Membrane-mediated actions of 1,25-dihydroxy vitamin D3: A review of the roles of phospholipase A<sub>2</sub> activating protein and Ca<sup>2+</sup>/calmodulin-dependent protein kinase II'. Together they form a unique fingerprint.

Cite this