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The 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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Abstract

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.

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Abbreviations

ALS:

Alsever buffer

BA:

Bioamines

PKA:

cAMP-dependent protein kinase

p60:

Ca2+-dependent protein kinase C

p105:

Ca2+-independent protein kinase C

DAG:

Diacylglycerol

ERK:

Extracellular-signal-regulated kinase

H2O2 :

Hydrogen peroxide

OH:

Hydroxyl radical

HPA:

Hypothalamic-pituitary-adrenal axis

IL-2:

Interleukin-2

NO:

Nitric oxide

PMA:

Phorbol myristate acetate

ONOO :

Peroxynitrite

PKC:

Protein kinase C

RB:

Respiratory burst

O2 :

Superoxide ion

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Acknowledgments

This work was supported by the Grants XUGA 26100 PB96 and PGIDT MAR 26102PR from the Autonomous Government of Galicia (Spain). We thank María Mosquera for excellent technical assistance.

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Correspondence to J. I. Ramos-Martínez.

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Gonzalez-Riopedre, M., Barcia, R. & Ramos-Martínez, J.I. The Ca2+-independent PKC (p105) mediates the PMA-activation of marine mussel hemocytes and the Ca2+-dependent PKC (p60) does not intervene. Mol Cell Biochem 332, 243–249 (2009). https://doi.org/10.1007/s11010-009-0197-z

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