Probing the functional importance of the amino acid residues in the synthetic peptide actin 1–28 on interaction with troponin I and myosin

Peptides ◽  
1994 ◽  
pp. 961-962
Author(s):  
J. E. Van Eyk ◽  
O. D. Monera ◽  
R. S. Hodges
Keyword(s):  
Amino Acid ◽  
Synthetic Peptide ◽  
Troponin I ◽  
Amino Acid Residues ◽  
Functional Importance

Plasmin-platelet interaction involves cleavage of functional thrombin receptor

1996 ◽  
Vol 271 (1) ◽  
pp. C54-C60 ◽  
Author(s):  
M. Kimura ◽  
T. T. Andersen ◽  
J. W. Fenton ◽  
W. F. Bahou ◽  
A. Aviv
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Platelet Activation ◽  
Synthetic Peptide ◽  
Time Dependent ◽  
Thrombin Receptor ◽  
Amino Acid Residues ◽  
Enzymatic Action ◽  
High Concentrations ◽  
Inhibition Of Thrombin

We tested the hypothesis that the inhibition of thrombin-induced platelet activation by plasmin is mediated via the enzymatic action of plasmin on the functional thrombin receptor. We monitored the binding of the anti-thrombin receptor antibody [anti-TR-(34-46)] to platelets; this binding is sensitive to the cleavage of the thrombin receptor at amino acid residues Arg-41 to Ser-42. Plasmin inhibited anti-TR-(34-46) binding in dose- and time-dependent manners. The inactive synthetic peptide with the amino acid sequence 40-55 of the thrombin receptor (D-FPRSFLLRNPNDKYEPF) was similarly cleaved by thrombin and plasmin to an active peptide (SFLLRNPNDKYEPF) that produced robust cytosolic Ca2+ responses. At high concentrations, plasmin itself can activate platelets. We explored this effect with the use of anti-TR-(1-160). This antibody abolished the cytosolic Ca2+ responses to thrombin and to the thrombin receptor-activating peptide SFLLRN but did not attenuate the plasmin-induced cytosolic Ca2+ response. Thus plasmin inhibits thrombin-evoked platelet activation by cleaving the thrombin receptor, but the plasmin-induced cytosolic Ca2+ response is not due to the generation of the tethered peptide of the thrombin receptor.

The human anion transport protein, band 3, contains a CD36-like binding domain forPlasmodium falciparum-infected erythrocytes

Parasitology ◽  
1996 ◽  
Vol 112 (3) ◽  
pp. 261-267 ◽  
Author(s):  
I. Crandall ◽  
I. W. Sherman
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Blood Cells ◽  
Synthetic Peptide ◽  
Epitope Mapping ◽  
Protein Band ◽  
Band 3 ◽  
Anion Transport ◽  
Transport Protein ◽  
Amino Acid Residues

SUMMARYEpitope mapping of a murine monoclonal antibody (mAb), 5H12, prepared against livePlasmodium falciparum-intected red blood cells indicated that the epitope consisted of amino acid residues 474–487 of the human anion transport protein, band 3. mAb 5H12 enhanced cytoadherence, but inhibited the CD36-like mediated resetting. A synthetic peptide based on the sequence of the epitope (FSFCETNGLE) blocked both resetting and cytoadherence, suggesting that this amino acid sequence may form the CD36-like receptor. The CD36-like region of band 3 was antigenically distinct from platelet or endothelial CD36.

Immunization with human thyrotrophin receptor peptide induces an increase in thyroid hormone in rabbits

1992 ◽  
Vol 135 (3) ◽  
pp. 479-484 ◽  
Author(s):  
M. Ohmori ◽  
T. Endo ◽  
M. Ikeda ◽  
T. Onaya
Keyword(s):  
Amino Acid ◽  
Thyroid Hormone ◽  
Western Blot ◽  
Synthetic Peptide ◽  
Matched Control ◽  
Tsh Receptor ◽  
Amino Acid Residues ◽  
Normal Range ◽  
Tsh Receptor Antibody ◽  
Peptide Antibodies

ABSTRACT Eight rabbits were immunized with a synthetic peptide corresponding to the unique N-terminal region (termed N peptide; amino acid residues 29–57) in the extracellular domain of the human thyrotrophin (TSH) receptor. After 10 weeks, all of the eight rabbits produced anti-N peptide antibodies. Western blot analysis revealed that the antibodies recognized rabbit TSH receptor as an approximately 100 kDa protein. We compared the level of thyroid hormone in serum taken before immunization (preimmune sera) with that of serum taken after immunization (postimmune sera) in these immunized rabbits. Postimmune sera from the eight rabbits had higher mean (± s.d.) levels of tri-iodothyronine (T3) and thyroxine (T4) than did preimmune sera (T3, preimmune 0·82 ± 0·26 μg/l vs postimmune 1·33 ± 0·35, P < 0·01; T4, preimmune 33·7 ± 10·0 μg/l vs postimmune 41·0 ± 6·0, P < 0·05). T3 levels in four rabbits and T4 levels in four rabbits after immunization were over the normal range obtained from six age-matched control rabbits. Seven rabbits exhibited thyroid-stimulating antibody (TSAb) activity with various degrees (241–545%). The concentration of T3 and T4 did not increase over 10 weeks in either non-immunized rabbits (T3, preimmune 0·89 ± 0·34 μg/l vs postimmune 0·82 ± 0·22; T4, preimmune 31·1 ± 7·3 μg/l vs postimmune 30·3 ± 5·1) or other peptide-immunized rabbits (T3, preimmune 0·68 μg/l (n = 2) vs postimmune 0·69; T4, preimmune 33·1 μg/l vs postimmune 26·4). These results indicate that experimentally produced anti-TSH receptor antibody with TSAb activity induces an increase in thyroid hormone in rabbits. Journal of Endocrinology (1992) 135, 479–484

scholarly journals The amino acid sequence of troponin I from rabbit skeletal muscle

1975 ◽  
Vol 149 (2) ◽  
pp. 493-496 ◽  
Author(s):  
J M Wilkinson ◽  
R J A. Grand
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Troponin I ◽  
Rabbit Skeletal Muscle ◽  
British Library ◽  
Amino Acid Residues ◽  
N Terminus

The complete amino acid sequence of rabbit skeletal muscle troponin I was determined by the isolation of the cyanogen bromide fragments and the tryptic methionine-containing peptides. Troponin I contains 179 amino acid residues and has a molecular weight of 20864. Its N-terminus is acetylated. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50055 (23 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

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