Dipyridamole-induced decrement of functional recovery of postischemic reperfused myocardium in conscious dogs with well-developed coronary collateral circulation

Kenny, Dermot; Wynsen, John C.; Brooks, Harold L.; Warltier, David C.

doi:10.1016/0002-8703(91)90136-6

Cited by 7 publications

(1 citation statement)

References 31 publications

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“…There are, however, technical limitations in physiological studies in the mouse, due to size. In contrast the vascular physiology of the dog is well understood and is similar in many respects to humans (14,15). Furthermore, several types of thrombotic models in the anesthetized (16), and conscious state (17,18) have been developed in the dog.…”

Section: Introductionmentioning

confidence: 99%

Cloning and Expression of Canine Glycoprotein Ibα

Morateck¹,

Fahs²,

Warltier³

et al. 1999

Thromb Haemost

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SummaryThe interaction of the glycoprotein (GP) Ib-IX-V complex with von Willebrand factor (vWF) is critical in initiation of haemostasis and thrombosis through platelet adhesion to damaged endothelium. The binding site for vWF resides within the GPIbα subunit of the complex. To further define the physiological function of platelet GPIbα we cloned and expressed the canine GPIbα cDNA. A canine platelet cDNA library was constructed and screened with a randomly primed 32P-labeled 1041-base-pair restriction fragment of the human GPIbα cDNA. Analysis of 23 clones demonstrated that the canine GPIbα cDNA is 2530 nucleotides in length and includes a short 5’ untranslated segment of 42 nucleotides followed by a signal peptide of 16 amino acids, a mature peptide of 645 amino acids and a 3’ noncoding region of 455 nucleotides. A single intron of 142 nucleotides, 6 nucleotides upstream from the ATG translation initiation codon was identified in the canine gene in a similar location to that present in the human gene.Chinese hamster ovary cells that stably express human GPIbα and GPIX were transfected with the canine GPIbα cDNA. Canine GPIbα was expressed on the surface of these cells and bound vWF in the presence of botrocetin. The binding of vWF was inhibited by an anti-vWF human monoclonal antibody known to inhibit vWF binding to GPIbα. The results of this investigation will allow the development of reagents to study the physiological function of GPIbα in an animal model.

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