Regulatory properties of p105: A novel PKC isoenzyme in mantle tissue from marine mussels

LUIS ALBERTO MERCADO VIANCO, Asunción Cao, Ramiro Barcia, Juan Ignacio Ramos-Martinez

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12 Scopus citations

Abstract

Previous results suggested operative similarities between Apl II from nervous cells of Aplysia californica, εPKC from brain of vertebrates, and p105 from mantle tissue of Mytilus galloprovincialis Lmk., all of them belonging to the nPKC family. The optimal substrate for Apl II and p105 from mussel is protamine sulfate. In contrast, Ca2+ inhibits p105 but does not affect Apl II. As occurs in other εPKC, p105 is autophosphorylable; however, in Apl II, no P-Tyr residues are detected in the most phosphorylated form. The presence of p105 in all the tissues of M. galloprovincialis studied, proves the important, yet unknown, physiological role that this enzyme must play.

Original languageEnglish
Pages (from-to)771-775
Number of pages5
JournalBiochemistry and Cell Biology
Volume80
Issue number6
DOIs
StatePublished - 1 Dec 2002

Keywords

  • Mussel
  • Mytilus
  • Protein kinase C
  • Regulation

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