Disease relevance of GPBP1

• Analysis of arteries displaying various stages of atherosclerosis indicated that the vasculin/SSH6-beta ratio increases throughout atherogenesis [1].

High impact information on GPBP1

• Normal human serum was found to contain a heat-stable protein which promoted the binding of granulocytes to timothy grass pollen (granulocyte/pollen-binding protein [GPBP]) [2].
• The apparent heterogeneity in the molecular size and charge of GPBP observed during progressive purification was minimal when GPBP was saturated with ferric ions before the separation procedures [2].
• Sequestering of GPBP present in HeLa cell nuclear extract by immunoabsorption completely and reversibly suppressed extract-dependent in vitro transcription from the murine Ada gene's G+C-rich promoter [3].
• Transferrin/GPBP did not bind to either neutrophils or pollen grains [4].
• Eosinophils, monocytes and lymphocytes did not appear to participate in GPBP-induced pollen binding reactions at concentrations up to 300 micrograms/ml [4].

Biological context of GPBP1

• Human granulocyte/pollen binding protein (GPBP), previously identified as serum transferrin, promoted prolonged firm adherence of neutrophils to Timothy grass pollen [4].

Anatomical context of GPBP1

• In the presence of GPBP, neutrophils adhered to a range of grass, weed and tree pollens [4].

Analytical, diagnostic and therapeutic context of GPBP1

• Western blot analysis indicated a ubiquitous 35-kDa protein (SSH6-beta), in addition to a 45-kDa protein (vasculin), detected in the vascular wall and in plasma [1].
• GPBP was purified by gel filtration, anion exchange, and affinity chromatography [2].

References