TY - JOUR
T1 - Regulatory properties of p105
T2 - A novel PKC isoenzyme in mantle tissue from marine mussels
AU - Mercado, Luis
AU - Cao, Asunción
AU - Barcia, Ramiro
AU - Ramos-Martinez, Juan Ignacio
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
KW - Mussel
KW - Mytilus
KW - Protein kinase C
KW - Regulation
UR - http://www.scopus.com/inward/record.url?scp=0042455772&partnerID=8YFLogxK
U2 - 10.1139/o02-165
DO - 10.1139/o02-165
M3 - Article
C2 - 12555810
AN - SCOPUS:0042455772
SN - 0829-8211
VL - 80
SP - 771
EP - 775
JO - Biochemistry and Cell Biology
JF - Biochemistry and Cell Biology
IS - 6
ER -
