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Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin - PubMed
Source: pubmed.ncbi.nlm.nih.gov
Article summary:
1. The C-terminal "cell-binding domain" (CBD) of thrombospondin-1 (TS1) is a binding site for many cell types.
2. Integrin-associated protein (IAP or CD47) associates with alpha v beta 3 and modulates the activity of several integrins.
3. Cells that express the 52-kDa protein bind strongly to TS1, the CBD, and its active cell-binding peptides while cells without it do not; this establishes that the 52-kDa protein is a receptor for the CBD of TS1.
Article analysis:
The article is generally reliable and trustworthy in its reporting of scientific findings. The authors provide evidence to support their claims, such as showing that cells expressing the 52-kDa protein bind strongly to TS1, the CBD, and its active cell-binding peptides while cells without it do not; this establishes that the 52-kDa protein is a receptor for the CBD of TS1. Furthermore, they provide evidence that endothelial cells exhibit chemotaxis toward TS1 and RFYVVM peptides which can be inhibited by a function blocking anti-IAP monoclonal antibody.
The article does not appear to have any biases or one sided reporting as it presents both sides equally and does not make any unsupported claims or omit any points of consideration. It also does not contain any promotional content or partiality towards either side of an argument. The article does note possible risks associated with its findings but does not explore them in depth. All in all, this article appears to be reliable and trustworthy in its reporting of scientific findings.