Biomedical subjects

D E McGrath

Publications and source records attributed to D E McGrath.

3 recordsLinked to original sources

PubMed1994

Ligand and cation binding are dual functions of a discrete segment of the integrin beta 3 subunit: cation displacement is involved in ligand binding.

The alpha IIb beta 3 integrin binds Arg-Gly-Asp-containing (RGD-containing) ligands in a cation-dependent interaction. A fourteen amino acid sequence, beta 3 (118-131), and an antibody to it, inhibited ligand binding functions of alpha IIb beta 3, and a 1:1 stoichiometric beta 3 (118-131)-RGD complex was detected by mass spectroscopy. Cation binding to beta 3 (118-131) was demonstrated by terbium luminescence and mass spectroscopy. Notably, ligand displaced cation from the beta 3(118-131) peptide and also from purified alpha IIb beta 3. Thus, beta 3 (118-131), a highly conserved region in integrin beta subunits, binds both ligand and cation. Formation of a ternary complex between cation, ligand, and receptor, with subsequent displacement of cation from beta 3 (118-131) and a second site within the receptor, may be central to the mechanism of ligand recognition by integrins.

Amino Acid Sequence↗

PubMed1994

A hookworm glycoprotein that inhibits neutrophil function is a ligand of the integrin CD11b/CD18.

The chronic survival of many endoparasites is dependent on the ability of these organisms to escape the host immune response. Identification of the molecular mechanisms by which these organisms evade this response may yield novel approaches in the development of anti-inflammatory agents. We describe here the discovery and characterization of a novel 41-kilodalton glycoprotein from the canine hookwork (Ancylostoma caninum) that potently inhibits CD11/CD18-dependent neutrophil function in vitro. Neutrophil inhibitory factor (NIF) blocks the adhesion of activated human neutrophils to vascular endothelial cells as well as the release of H2O2 from activated neutrophils, over a similar concentration range (IC50 10-20 nM). Studies aimed at determining the nature of the NIF binding site on neutrophils revealed selective, high affinity binding of this protein to the integrin CD11b/CD18. A cDNA encoding NIF was isolated from a canine hookworm cDNA library. NIF comprises a mature polypeptide of 257 amino acids, preceded by a 17-amino acid leader. The mature protein has 10 cysteines and has seven potential N-linked glycosylation sites. NIF has no significant sequence homologies to any previously reported protein. As such, NIF represents a prototype of a novel class of leukocyte function inhibitors.

Amino Acid Sequence↗

PubMed1986

A newsletter evaluation using the Title Rating Method.

The Title Rating Method is used to measure readership interests and predict readership topics for future issues, in message ideas. This methodology was used to plan types of articles in a newsletter published through the Cancer Communication Network contract. This article describes evaluation results of the newsletter for health professionals, North Carolina Cancergram. Retrospective and prospective titles were assigned to seven categories: psychosocial, treatment, drugs, nursing issues, rehabilitation, education, and detection. Interest in the titles in each category was evaluated according to five occupational groups: nurses, pharmacists, physicians, allied health, and others. The rank order of most popular to least popular categories was: drugs, treatment, education, psychosocial, rehabilitation, detection, and nursing issues. The most popular article overall across occupational groups was an article directed primarily to physicians, "Informing the patient requires honesty, sensitivity." The readership was primarily white, female, over 35 years of age with a college degree or higher. Most of the readership work in a health related setting although 67.6 percent of the respondents spent less than ten percent of their time working with cancer patients. This is in keeping with the intent of the publication to reach health professionals outside the Cancer Center.

Allied Health Personnel↗