An inhibitor of collagen-induced platelet aggregation from the saliva of Triatoma pallidipennis

• Published in: The Journal of biological chemistry 1994-02, Vol.269 (7), p.5050-5053
• Main Authors: Noeske-Jungblut, C, Kratzschmar, J, Haendler, B, Alagon, A, Possani, L, Verhallen, P, Donner, P, Schleuning, W.D
• Format: Article
• Language: English
• Subjects: 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid; Adenosine Diphosphate - pharmacology; Adenosine Triphosphate - blood; Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Blood coagulation. Blood cells; Blood Platelets - drug effects; Blood Platelets - metabolism; Cell Line; COAGULACION SANGUINEA; COAGULATION SANGUINE; COLAGENOS; Collagen - pharmacology; COLLAGENE; Cricetinae; Fundamental and applied biological sciences. Psychology; Gene Expression; GENERO HUMANO; GENRE HUMAIN; Hemiptera; Humans; Kidney; Kinetics; Molecular and cellular biology; Molecular Sequence Data; Molecular Weight; Phorbol Esters - pharmacology; Platelet; Platelet Adhesiveness - drug effects; Platelet Aggregation - drug effects; Platelet Aggregation Inhibitors - isolation & purification; Platelet Aggregation Inhibitors - pharmacology; PROPIEDADES MECANICAS; PROPRIETE MECANIQUE; Prostaglandin Endoperoxides, Synthetic - pharmacology; PROTEINAS; PROTEINE; Recombinant Proteins - biosynthesis; Recombinant Proteins - isolation & purification; Recombinant Proteins - pharmacology; Reduviidae; Saliva; Salivary Proteins and Peptides - biosynthesis; Salivary Proteins and Peptides - isolation & purification; Salivary Proteins and Peptides - pharmacology; SECUENCIA NUCLEICA; SEQUENCE NUCLEIQUE; Thrombin - pharmacology; THROMBOCYTE; Thromboxane A2 - analogs & derivatives; Thromboxane A2 - pharmacology; Transfection; TRIATOMA; Triatominae - metabolism; TROMBOCITOS
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(17)37652-4

The saliva of Triatoma pallidipennis, a blood-sucking triatomine bug (Hemiptera, family Reduviidae, subfamily Triatominae) was found to contain a factor that specifically inhibits collagen-induced platelet aggregation. The 19-kDa protein was purified to homogeneity and named pallidipin. Collagen-mediated aggregation of platelets in plasma and of washed platelets was inhibited with the same efficacy. No inhibition of aggregation stimulated by other effectors (ADP, thrombin, thromboxane A2 mimetic U46619, phorbol ester) was detected. Pallidipin had no effect on platelet adhesion to collagen but inhibited ATP release from platelets. It interacted reversibly with platelets and may share with collagen a common target on them. The protein exhibits a unique primary structure (predicted from cDNA clones) with no significant similarity to other previously described sequences. The protein produced in recombinant baby hamster kidney cells had antiaggregatory effects similar to those of native pallidipin. Availability of recombinant pallidipin will allow further investigation of the precise mechanism of action