Atrial Natriuretic Peptide Induces the Expression of MKP-1, a Mitogen-activated Protein Kinase Phosphatase, in Glomerular Mesangial Cells

Atrial natriuretic peptide (ANP) and B-type natriuretic peptide (BNP), two distinct members of the natriuretic peptide family, share many features in common. However, differences in expression indicate that the processing mechanisms must be different. The leader sequence of rat BNP contains three potential phosphorylation sites for proline-directed kinases that are not present in the leader sequence of ANP. This study has examined how these sites are used by two somewhat different proline-directed kinases. A peptide containing these sites was phosphorylated in vitro by HeLa p34cdc2 kinase and by sea star p44mpk kinase at rates that were comparable to the rates with peptide substrates that are used to assay these enzymes. Sequence analysis of the phosphopeptide shows that both kinases phosphorylate only the two potential phosphorylation sites surrounding the cleavage site of the BNP precursor. The enzymatic potential for such a phosphorylation of BNP in cardiac tissue is demonstrated by immunoblots and kinase assays, showing that in fetal and in adult rat heart both the atria and the ventricles contain a mitogen-activated protein kinase homologue that can phosphorylate this preproBNP sequence.Key words: atrial natriuretic peptide, cdc2 kinase, mitogen-activated protein kinase, phosphorylation.

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Mitogen-activated protein kinase cascade is activated in glomeruli of diabetic rats and glomerular mesangial cells cultured under high glucose conditions

Diabetes ◽

10.2337/diabetes.46.5.847 ◽

1997 ◽

Vol 46 (5) ◽

pp. 847-853 ◽

Cited By ~ 39

Author(s):

M. Haneda ◽

S. Araki ◽

M. Togawa ◽

T. Sugimoto ◽

M. Isono ◽

...

Keyword(s):

Protein Kinase ◽

High Glucose ◽

Mesangial Cells ◽

Diabetic Rats ◽

Mitogen Activated Protein Kinase ◽

Glomerular Mesangial Cells ◽

Mitogen Activated Protein ◽

Kinase Cascade ◽

Protein Kinase Cascade ◽

Cells Cultured

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Effects of atrial natriuretic peptide and cGMP on uptake of IgG complexes by macrophages

AJP Cell Physiology ◽

10.1152/ajpcell.1993.265.1.c92 ◽

1993 ◽

Vol 265 (1) ◽

pp. C92-C98 ◽

Cited By ~ 15

Author(s):

J. Mattana ◽

P. C. Singhal

Keyword(s):

Angiotensin Ii ◽

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Guanylate Cyclase ◽

Soluble Guanylate Cyclase ◽

Mesangial Cells ◽

Glomerular Mesangial Cells ◽

Direct Role ◽

Cyclic Monophosphate ◽

Atrial Natriuretic

Macromolecular handling by macrophages and glomerular mesangial cells may be important in the development of renal injury. We undertook the present study to determine whether atrial natriuretic peptide (ANP), a particulate guanylate cyclase stimulator, plays a direct role in uptake of immunoglobulin G (IgG) complexes by macrophages. Macrophages incubated with ANP at 10(-5) and 10(-6) M showed significantly suppressed uptake of IgG complexes compared with control. Macrophage uptake of IgG complexes was also significantly suppressed by the soluble guanylate cyclase stimulator sodium nitroprusside. Dibutyryl guanosine 3',5'-cyclic monophosphate and dibutyryl adenosine 3',5'-cyclic monophosphate both significantly suppressed IgG complex uptake as well. ANP was found to significantly enhance macrophage guanosine 3',5'-cyclic monophosphate (cGMP) levels compared with control cells, and this effect was antagonized by angiotensin II. Angiotensin II significantly enhanced uptake of IgG complexes and suppressed macrophage adenosine 3',5'-cyclic monophosphate synthesis, and both effects were antagonized by coincubation with ANP. These results suggest that ANP modulates uptake of IgG complexes by macrophages and that this effect may be mediated via cGMP.

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Antiproliferative effect of nitric oxide on rat glomerular mesangial cells via inhibition of mitogen-activated protein kinase

European Journal of Biochemistry ◽

10.1046/j.0014-2956.2001.02534.x ◽

2001 ◽

Vol 268 (24) ◽

pp. 6358-6368 ◽

Cited By ~ 15

Author(s):

Ting-Yu Chin ◽

Yin-Shan Lin ◽

Sheau-Huei Chueh

Keyword(s):

Nitric Oxide ◽

Protein Kinase ◽

Mesangial Cells ◽

Antiproliferative Effect ◽

Mitogen Activated Protein Kinase ◽

Glomerular Mesangial Cells ◽

Mitogen Activated Protein

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Atrial natriuretic peptide inhibits endothelin-1-induced activation of JNK in glomerular mesangial cells

Kidney International ◽

10.1046/j.1523-1755.1998.00869.x ◽

1998 ◽

Vol 53 (5) ◽

pp. 1133-1142 ◽

Cited By ~ 29

Author(s):

Motohide Isono ◽

Masakazu Haneda ◽

Shiro Maeda ◽

Mariko Omatsu-Kanbe ◽

Ryuichi Kikkawa

Keyword(s):

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Mesangial Cells ◽

Glomerular Mesangial Cells ◽

Endothelin 1 ◽

Atrial Natriuretic

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Cellular signaling by endothelin peptides: pathways to the nucleus.

Journal of the American Society of Nephrology ◽

10.1681/asn.v210s116 ◽

1992 ◽

Vol 2 (10) ◽

pp. S116

Author(s):

M S Simonson ◽

Y Wang ◽

M J Dunn

Keyword(s):

Protein Kinase ◽

Mesangial Cells ◽

Regulatory Peptides ◽

Mitogen Activated Protein Kinase ◽

Activator Protein 1 ◽

Glomerular Mesangial Cells ◽

Short Term ◽

Activator Protein ◽

Mitogen Activated Protein

Endothelins (ET) are potent regulatory peptides that evoke diverse responses in glomerular mesangial cells. These include short-term actions, such as contraction and secretion, and long-term, adaptive responses, such as cell growth. Although much attention has been focused on the second messenger cascades, which govern short-term effects, the pathways of cytosolic and nuclear signaling, which effect long-term changes, remain unclear. Several distal signaling events by ET receptors have been characterized in rat mesangial cells. These include activation of a cytosolic protein kinase, mitogen-activated protein kinase and an inducible transcription factor, activator protein-1 (AP-1). This review focuses on the activation of mitogen-activated protein kinase and activator protein-1 by ET and discusses the potential role of these third and fourth messengers in controlling long-term cellular adaptations. Characterization of these and other cytosolic and nuclear signals should provide important insights into the pleiotropic actions of ET peptides.

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