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Adel Giaid

Researcher at McGill University

Publications -  105
Citations -  13513

Adel Giaid is an academic researcher from McGill University. The author has contributed to research in topics: Endothelin 1 & Lung. The author has an hindex of 52, co-authored 105 publications receiving 13213 citations. Previous affiliations of Adel Giaid include University of Oslo & Imperial College London.

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Expression of Endothelin-1 in the Lungs of Patients with Pulmonary Hypertension

TL;DR: Preliminary results suggest that pulmonary hypertension is associated with the increased expression of endothelin-1 in vascular endothelial cells, suggesting that the local production of endethelin- 1 may contribute to the vascular abnormalities associated with this disorder.
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Reduced Expression of Endothelial Nitric Oxide Synthase in the Lungs of Patients with Pulmonary Hypertension

TL;DR: It is possible that decreased expression of nitric oxide synthase may contribute to pulmonary vasoconstriction and to the excessive growth of the tunica media observed in this disease.
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Targeted and natural (piebald-lethal) mutations of endothelin-B receptor gene produce megacolon associated with spotted coat color in mice

TL;DR: Findings indicate an essential role for EDNRB in the development of two neural crest-derived cell lineages, myenteric ganglion neurons and epidermal melanocytes, and postulate that defects in the human ED NRB gene cause a hereditary form of Hirschsprung's disease that has recently been mapped to human chromosome 13.
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Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons

TL;DR: It is reported that a targeted disruption of the mouse endothelin-3 ligand (EDN3) gene produces a similar recessive phenotype of megacolon and coat color spotting, and postulate that defects in the human EDN3 gene may cause Hirschsprung's disease.
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ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1

TL;DR: The identification of ECE-1 is reported, a novel membrane-bound neutral metalloprotease that is expressed abundantly in endothelial cells in vivo and is structurally related to neutral endopeptidase 24.11 and Kell blood group protein.