J
John Prins
Researcher at University of Queensland
Publications - 34
Citations - 1394
John Prins is an academic researcher from University of Queensland. The author has contributed to research in topics: Adiponectin & Adipose tissue. The author has an hindex of 19, co-authored 34 publications receiving 1266 citations. Previous affiliations of John Prins include Princess Alexandra Hospital & University of Cambridge.
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Clinical review: Adiponectin biology and its role in inflammation and critical illness
TL;DR: This review discusses the history, biology and physiological role of adiponectin and explores its role in disease, with specific focus on adip onectin in inflammation and sepsis, and the various options for modulation of serum adiponECTin.
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Human adipose tissue endothelial cells promote preadipocyte proliferation
L Hutley,Adrian C. Herington,Wenda Shurety,Catherine Cheung,David A. Vesey,Donald P. Cameron,John Prins +6 more
TL;DR: In this paper, the role of endothelial cell-derived factors that influence the proliferation of human preadipocytes was examined, which indicated that adipose tissue endothelial cells secrete soluble adipogenic factor(s).
Journal ArticleDOI
Leptin and the risk of Barrett’s oesophagus
Bradley J. Kendall,Graeme A. Macdonald,Nicholas K. Hayward,John Prins,Ian L. Brown,Neal I. Walker,Nirmala Pandeya,Adèle C. Green,Penelope M. Webb,David C. Whiteman +9 more
TL;DR: High serum leptin is associated with an increased risk of Barrett’s oesophagus among men but not women, and this association is not explained simply by higher body mass or gastro-oesophageal reflux among cases.
Human adipose tissue endothelial cells promote preadipocyte proliferation
L Hutley,Adrian C. Herington,Wenda Shurety,Catherine Cheung,David A. Vesey,Donald P. Cameron,John Prins +6 more
TL;DR: Results indicate that adipose tissue endothelial cells secrete soluble adipogenic factor(s), and this work has examined the role of endothelial cell-derived factors that influence the proliferation of human preadipocytes.
Journal ArticleDOI
Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs
Fiona M. Keane,Fiona M. Keane,Tsun-Wen Yao,Tsun-Wen Yao,Stefanie Seelk,Margaret G. Gall,Margaret G. Gall,Sumaiya Chowdhury,Sumaiya Chowdhury,Sarah E. Poplawski,Jack H. Lai,Youhua Li,Wengen Wu,Penny Farrell,Ana Julia Vieira de Ribeiro,Ana Julia Vieira de Ribeiro,Brenna Osborne,Brenna Osborne,Denise M. T. Yu,Denise M. T. Yu,Devanshi Seth,Devanshi Seth,Khairunnessa Rahman,Paul S. Haber,Paul S. Haber,A. Kemal Topaloglu,Chuanmin Wang,Chuanmin Wang,Sally Thomson,Sally Thomson,Annemarie Hennessy,Annemarie Hennessy,John Prins,Stephen M. Twigg,Stephen M. Twigg,Susan V. McLennan,Susan V. McLennan,Geoffrey W. McCaughan,Geoffrey W. McCaughan,William W. Bachovchin,Mark D. Gorrell,Mark D. Gorrell +41 more
TL;DR: The new FAP enzyme assay is the first to be thoroughly characterised and shows that FAP activity is measurable in most organs and at high levels in some, particularly liver fibrosis.