scholarly journals Interactions of basic polypeptides and proteins with calmodulin

1980 ◽  
Vol 189 (3) ◽  
pp. 455-459 ◽  
Author(s):  
T Itano ◽  
R Itano ◽  
J T Penniston
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Complexes ◽  
Histone H2b ◽  
Basic Proteins ◽  
Inhibitory Compounds ◽  
Low Concentrations ◽  
Synthetic Polypeptides ◽  
Basic Polypeptides ◽  
Stimulation Of

Low concentrations (less than 10 microgram/ml) of a number of highly basic polypeptides inhibit the calmodulin-stimulated cyclic nucleotide phosphodiesterase. Inhibitory compounds include synthetic polypeptides [polylysine (D and L) and polyarginine] and basic proteins (protamine, histones H1, H2A, H2B, H3 and H4 and myelin basic protein). Polylysine of mol.wt. about 2000 or higher was inhibitory, but pentalysine did not inhibit. Other basic proteins and compounds did not inhibit, including bradykinin, spermine and putrescine. In mixtures of calmodulin and basic protein, complexes were formed whether Ca2+ was present or not. This was true for polylysine, myelin basic protein and histone H2B. These interactions suggest that the inhibition of the phosphodiesterase is due to interaction of these basic proteins with calmodulin. The wide variety of basic polypeptides and proteins that affect the calmodulin stimulation of phosphodiesterase indicates that these interactions are not specific.

scholarly journals Proteolytic and peroxidatic reactions of commercial horseradish peroxidase with myelin basic protein

1978 ◽  
Vol 169 (3) ◽  
pp. 567-575 ◽  
Author(s):  
Wendy Cammer ◽  
Lesley Z. Bieler ◽  
William T. Norton
Keyword(s):  
Horseradish Peroxidase ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein A ◽  
Low Molecular Weight ◽  
Basic Proteins ◽  
Molecular Weights ◽  
Low Concentrations ◽  
High Concentrations ◽  
A Minor

Degradation of myelin basic protein during incubations with high concentrations of horseradish peroxidase has been demonstrated [Johnson & Cammer (1977) J. Histochem. Cytochem.25, 329–336]. Possible mechanisms for the interaction of the basic protein with peroxidase were investigated in the present study. Because the peroxidase samples previously observed to degrade basic protein were mixtures of isoenzymes, commercial preparations of the separated isoenzymes were tested, and all three degraded basic protein, but to various extents. Three other basic proteins, P2 protein from peripheral nerve myelin, lysozyme and cytochrome c, were not degraded by horseradish peroxidase under the same conditions. Inhibitor studies suggested a minor peroxidatic component in the reaction. Therefore the peroxidatic reaction with basic protein was studied by using low concentrations of peroxidase along with H2O2. Horseradish peroxidase plus H2O2 caused the destruction of basic protein, a reaction inhibited by cyanide, azide, ferrocyanide, tyrosine, di-iodotyrosine and catalase. Lactoperoxidase plus H2O2 and myoglobin plus H2O2 were also effective in destroying the myelin basic protein. Low concentrations of horseradish peroxidase plus H2O2 were not active against other basic proteins, but did destroy casein and fibrinogen. Although high concentrations of peroxidase alone degraded basic protein to low-molecular-weight products, suggesting the operation of a proteolytic enzyme contaminant in the absence of H2O2, incubations with catalytic concentrations of peroxidase in the presence of H2O2 converted basic protein into products with high molecular weights. Our data suggest a mechanism for the latter, peroxidatic, reaction where polymers would form by linking the tyrosine side chains in basic-protein molecules. These data show that the myelin basic protein is unusually susceptible to peroxidatic reactions.

HSP70-myelin basic protein complexes in multiple sclerosis brains

1998 ◽  
Vol 90 (1) ◽  
pp. 78
Author(s):  
K. Selmaj ◽  
H. Cwiklinska ◽  
O. Ludvsammorov ◽  
M. Kwinkowski ◽  
C.F. Brosnan ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Complexes

Shape change of blood platelets brought about by myelin basic protein and other basic polypeptides

1979 ◽  
Vol 310 (1) ◽  
pp. 87-92 ◽  
Author(s):  
Andreas Laubscher ◽  
Alfred Pletscher ◽  
Conrad G. Honegger ◽  
John G. Richards
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Shape Change ◽  
Blood Platelets ◽  
Basic Polypeptides

Physicochemical characterization of dodecylphosphocholine/palmitoyllysophosphatidic acid/myelin basic protein complexes

Biochemistry ◽  
1991 ◽  
Vol 30 (26) ◽  
pp. 6509-6516 ◽  
Author(s):  
George L. Mendz ◽  
David J. Miller ◽  
Ian M. Jamie ◽  
John W. White ◽  
Larry R. Brown ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Complexes ◽  
Physicochemical Characterization

Two-dimensional gel electrophoresis of human brain proteins. V. Non-equilibrium gel electrophoresis, with detection of a myelin basic protein mutation--MBL-Duarte.

1982 ◽  
Vol 28 (4) ◽  
pp. 813-818 ◽  
Author(s):  
D E Comings ◽  
A Pekkula-Flagan
Keyword(s):  
Human Brain ◽  
Myelin Basic Protein ◽  
Gel Electrophoresis ◽  
Basic Protein ◽  
Myelin Proteins ◽  
Two Dimensional Gel Electrophoresis ◽  
Brain Proteins ◽  
Basic Proteins ◽  
A Charge ◽  
Non Equilibrium

Abstract To examine the basic human brain proteins, we subjected 9 mmol/L urea extracts to non-equilibrium gel electrophoresis. The pattern observed differs distinctly from that with equilibrium gel electrophoresis. With this technique, the myelin proteins (myelin basic protein, proteolipids, and basic Wolfgram proteins) and many other unindentified major basic proteins can be demonstrated. The myelin basic proteins occur as two major polypeptides of different charge and slightly different molecular mass, indicating the action of at least two genes. The proteolipid proteins occur as a long series of charge isomers, suggesting multiple genes or extensive post-transcriptional modification. In one patient with schizophrenia, a charge-change mutation of the larger myelin basic protein (MBL) was observed and is termed "MBL-Duarte."

scholarly journals Orthovanadate Stimulates Cyclic Guanosine Monophosphate-Inhibited Cyclic Adenosine Monophosphate Phosphodiesterase Activity in Isolated Rat Fat Pads through Activation of Particulate Myelin Basic Protein Kinase by Protein Tyrosine Kinase

Endocrinology ◽  
1997 ◽  
Vol 138 (7) ◽  
pp. 2784-2789 ◽  
Author(s):  
Hiroshi Ueki ◽  
Shuichi Mitsugi ◽  
Yoshihito Kawashima ◽  
Toshio Motoyashiki ◽  
Tetsuo Morita
Keyword(s):  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Myelin Basic Protein ◽  
Protein Tyrosine Kinase ◽  
Basic Protein ◽  
Major Protein ◽  
Dependent Manner ◽  
Protein Tyrosine ◽  
Fat Pads ◽  
Stimulation Of

Abstract Involvement of protein kinases in the stimulation of cGMP-inhibited cAMP phosphodiesterase (PDE) activity by orthovanadate (vanadate) was studied. When the fat pads were incubated with 2 mm vanadate or 10 nm insulin, the stimulation of myelin basic protein kinase (MBPK) activity in the particulate by vanadate reached a maximum at 60 min. In contrast, insulin showed a transient increase at 20 min. A 60-min incubation of the fat pads with vanadate stimulated all activities of protein tyrosine kinase (PTK), MBPK, and PDE in the particulate, in a similar dose-dependent manner. Amiloride, a PTK inhibitor, inhibited the stimulations of three enzymes by vanadate in a similar concentration range. Enzyme fractions, which were separated from the solubilized particulate, were subjected to the immunoblot analysis. A fraction of MBPK was identified to contain a major protein of mol wt (44K) and a minor one (42K), both of which are immunoreactive with a mitogen-activated protein kinase (MAPK) antibody. The partially purified PDE activity was stimulated by the addition of the partially purified MBPK. The further stimulation was observed with the PTK-activated MBPK. These results suggest that vanadate stimulates in part the PDE activity through the activation of the particulate MBPK, probably MAPKs, by PTK sensitive to vanadate.

scholarly journals The binding of calmodulin to myelin basic protein and histone H2B

1980 ◽  
Vol 189 (2) ◽  
pp. 227-240 ◽  
Author(s):  
R J Grand ◽  
S V Perry
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Binding Protein ◽  
Bovine Brain ◽  
Sequence Determination ◽  
Partial Amino Acid Sequence ◽  
Histone H2b ◽  
Calmodulin Binding

1. A calmodulin-binding protein of apparent mol.wt. 19 000 has been purified from chicken gizzard. Similar proteins have been isolated from bovine uterus, rabbit skeletal muscle and rabbit liver. 2. These proteins migrated as an equimolar complex with bovine brain calmodulin on electroporesis on polyacrylamide gels in the presence of Ca2+ and 6M-urea. The complex was dissociated in the presence of EGTA. 2. The chicken gizzard calmodulin-binding protein has been shown to be identical with chicken erythrocyte histone H2B on the basis of partial amino acid sequence determination. 4. The calmodulin-binding proteins of apparent mol.wt. 22 000 isolated previously from bovine brain [Grand & Perry (1979) Biochem. J. 183, 285-295] has been shown, on the basis of partial amino-acid-sequence determination, to be identical with myelin basic protein. 5. The activation of bovine brain phosphodiesterase by calmodulin is inhibited by excess bovine uterus calmodulin-binding protein (histone H2B). 6. The phosphorylation of myelin basic protein by phosphorylase kinase is partially inhibited, whereas the phosphorylation of uterus calmodulin-binding protein (histone H2B) is unaffected by calmodulin or troponin C. 7. The subcellular distribution of myelin basic protein and calmodulin suggests that the two proteins do not exist as a complex in vivo.

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