Ca²⁺-independent PKC (p105) mediates the PMA-activation of marine mussel hemocytes and the Ca²⁺-dependent PKC (p60) does not intervene
Previous works revealed the presence of a Ca²⁺-dependent protein kinase (p60) and a Ca²⁺-independent protein kinase (p105) in the mantle tissue from the sea mussel Mytilus galloprovincialis Lmk. The expression of both isoforms shows a balance between cytosolic and membrane fractions in mantle, gills...
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| Veröffentlicht in: | Molecular and cellular biochemistry 2009-12, Vol.332 (1-2), p.243-249 |
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| creator | Gonzalez-Riopedre, M Barcia, R Ramos-Martínez, J. I |
| description | Previous works revealed the presence of a Ca²⁺-dependent protein kinase (p60) and a Ca²⁺-independent protein kinase (p105) in the mantle tissue from the sea mussel Mytilus galloprovincialis Lmk. The expression of both isoforms shows a balance between cytosolic and membrane fractions in mantle, gills, and hepatopancreas, whereas, in hemocytes, their expression is mainly cytosolic, as happens in muscle tissues with p60 alone. Both enzymatic forms contain phosphorylated serines, and no phosphorylation was detected in tyrosines. Only the form p105 mediates the PMA-induced activation of the hemocytes of M. galloprovincialis, and it does so by a process of down-regulation. The form p60 does not respond to the presence of the phorbol ester, suggesting structural differences related to the binding sites of the diacylglycerol. |
| doi_str_mv | 10.1007/s11010-009-0197-z |
| format | Article |
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I</creatorcontrib><title>Ca²⁺-independent PKC (p105) mediates the PMA-activation of marine mussel hemocytes and the Ca²⁺-dependent PKC (p60) does not intervene</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>Previous works revealed the presence of a Ca²⁺-dependent protein kinase (p60) and a Ca²⁺-independent protein kinase (p105) in the mantle tissue from the sea mussel Mytilus galloprovincialis Lmk. The expression of both isoforms shows a balance between cytosolic and membrane fractions in mantle, gills, and hepatopancreas, whereas, in hemocytes, their expression is mainly cytosolic, as happens in muscle tissues with p60 alone. Both enzymatic forms contain phosphorylated serines, and no phosphorylation was detected in tyrosines. Only the form p105 mediates the PMA-induced activation of the hemocytes of M. galloprovincialis, and it does so by a process of down-regulation. 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| ispartof | Molecular and cellular biochemistry, 2009-12, Vol.332 (1-2), p.243-249 |
| issn | 0300-8177 1573-4919 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Animals Biochemistry Biomedical and Life Sciences Bivalvia - enzymology Blotting, Western Calcium Calcium - metabolism Carcinogens - pharmacology Cardiology Cellular biology Hemocytes - drug effects Hemocytes - enzymology Isoenzymes Life Sciences Medical Biochemistry Molecular biology Mollusks Oncology Protein Kinase C - isolation & purification Protein Kinase C - metabolism Tetradecanoylphorbol Acetate - pharmacology Tissue Distribution |
| title | Ca²⁺-independent PKC (p105) mediates the PMA-activation of marine mussel hemocytes and the Ca²⁺-dependent PKC (p60) does not intervene |
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