Regulatory properties of p105: a novel PKC isoenzyme in mantle tissue from marine mussels.
Previous results suggested operative similarities between Apl II from nervous cells of Aplysia californica, epsilonPKC 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 epsilonPKC, 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.
Mercado
Luis
L
Departamento de Bioquímica y Biología Molecular, Facultad de Veterinaria, Universidad de Santiago de Compostela, Campus de Lugo, E-27002 Lugo, Spain.
Cao
Asunción
A
Barcia
Ramiro
R
Ramos-Martinez
Juan Ignaclo
JI
D000818:Animals; D049872:Bivalvia / Q000033:anatomy & histology / Q000201:enzymology*; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D009928:Organ Specificity; D010766:Phosphorylation; D011493:Protein Kinase C / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
D007527:Isoenzymes; D011493:Protein Kinase C