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L. Skelton, M. Cooper, M. Murphy and A. Platt, “Human Immature Monocyte-Derived Dendritic Cells Express the G Protein-Coupled Receptor GPR105 (KIAA0001, P2Y14) and Increase Intracellular Calcium in Response to Its Agonist, Uridine Diphosphoglucose,” Journal of Immunology, Vol. 171, No. 4, 2003, pp. 1941-194.

has been cited by the following article:

• TITLE: Bacterial UDP-Glucose Hydrolases and P2 Receptor-Mediated Responses to Infection: A Commentary

  AUTHORS: Ifor R. Beacham, John P. Headrick

  KEYWORDS: UDP-Glucose Hydrolase; P2Y14 Receptor; Virulence Factor; Salmonella enterica; E. coli

  JOURNAL NAME: Advances in Infectious Diseases, Vol.3 No.2, June 5, 2013

  ABSTRACT: UDP-glucose hydrolases are a group of relatively little known membrane-bound or periplasmic enzymes found in Salmonella enterica and E. coli. UDP-glucose is an agonist for a specific P2 receptor (P2Y14) found on epithelial cells and cells associated with innate immunity. It is also recognised as a ‘danger signal’. Cells respond to mechanical damage by releasing UDP-glucose which activates P2Y14 to trigger an innate immune response; it is postulated that a similar response to bacterial infection may be protective against infection. However, the UDP-glucose hydrolases may constitute virulence factors able to abrogate this response by degradation of the released UDP-glucose.