Pamela S. Steele

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PURPOSE Several mucins including MUC1, MUC2, MUC4, and MUC5AC have been identified at the ocular surface and in tears. The lacrimal gland, however, is not generally considered a source of ocular mucin. Because the lacrimal glands are similar to the salivary glands, we hypothesized that the lacrimal gland would express MUC7, a distinctive salivary mucin. We(More)
Mucins are highly glycosylated proteins that are vital to the maintenance of healthy epithelial surfaces including the ocular surface. Mucins act as lubricants, protectants, and mediators of signal transduction. The majority of the O-glycosylation sites on the transmembrane mucin MUC1 are found in a highly polymorphic core region containing a variable(More)
BACKGROUND The use of critical pathways for a variety of clinical conditions has grown rapidly in recent years, particularly pathways for patients with acute coronary syndromes (ACS). However, no systematic review exists regarding the value of critical pathways in this setting. METHODS The National Heart Attack Alert Program established a Working Group to(More)
The National Heart Attack Alert Program (NHAAP), which is coordinated by the National Heart, Lung, and Blood Institute (NHLBI), promotes the early detection and optimal treatment of patients with acute myocardial infarction and other acute coronary ischemic syndromes. The NHAAP, having observed the development and growth of chest pain centers in emergency(More)
The tear film is a complex mixture of secreted fluid, ions, proteins, glycoproteins, and lipids that lubricates and protects the ocular surface. Recently, several antimicrobial peptides have been described in the tear fluid. In this study, we describe the presence of the large secreted glycoprotein gp340 in the tear film. Western blot analysis showed that(More)
PURPOSE Mucins are highly glycosylated proteins that act as lubricants, protectants, and mediators of signal transduction. The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family members initiate mucin-type O-glycosylation. Because O-glycosylation provides mucins with the viscoelastic properties required for proper mucin function,(More)