Humanism or professionalism? The White Coat Ceremony and medical education.

In this article, the author challenges the widely held assumption that humanism and professionalism are necessarily complementary themes in medical education. He argues that humanism and professionalism are two very different value systems with different rationales, different goals, and different agendas. Whereas humanism is a universal, egalitarian ideology, professionalism represents the parochial, culturally determined practices of a particular professional group that may or may not conform to lay expectations. Distinguishing professionalism from humanism is crucial to understanding the divergent attitudes of providers and lay persons with regard to health care delivery and physician behavior. Moreover, it highlights the tension that medical students experience as they are tacitly asked to leave behind their lay, humanistic values and embrace a new professional identity, a transition that the common blurring of humanism and professionalism fails to recognize. In this context, the Arnold P. Gold Foundation's widely acclaimed White Coat Ceremony for entering medical students may actually be inhibiting, rather than encouraging, the genuine growth of humanism in medicine.

Angiopoietins have distinct modular domains essential for receptor binding, dimerization and superclustering.

Angiopoietins are a recently discovered family of angiogenic factors that interact with the endothelial receptor tyrosine kinase Tie2, either as agonists (angiopoietin-1) or as context-dependent agonists/antagonists (angiopoietin-2). Here we show that angiopoietin-1 has a modular structure unlike any previously characterized growth factor. This modular structure consists of a receptor-binding domain, a dimerization motif and a superclustering motif that forms variable-sized multimers. Genetic engineering of precise multimers of the receptor-binding domain of angiopoietin-1, using surrogate multimerization motifs, reveals that tetramers are the minimal size required for activating endothelial Tie2 receptors. In contrast, engineered dimers can antagonize endothelial Tie2 receptors. Surprisingly, angiopoietin-2 has a modular structure and multimerization state similar to that of angiopoietin-1, and its antagonist activity seems to be a subtle property encoded in its receptor-binding domain.