Crohn’s disease (colitis, usually of small intestine), Diarrhea, Abdominal pain Weight loss, Anemia, Inflammation Stomach Colon Small intestine Rectum Osmotin Injection Reduces Many Symptoms Of Colitis (Osmotin Mimics Adiponectin) Plasma Osmotin↑ Severity of Colitis ↓ Plasma Adiponectin↑ ↓ ↓↓↓ R. Arsenescu

VehicleAdiponectin 250 ng/ml TNFa 25ng/ml Osmotin 250 ng/ml Osmotin Reduces Proliferation Of Human Breast Cancer Cells Fold Change in Cell Number Osmotin mimics adiponectin T. Salameh et al.

New Functions Of PR-5/Thaumatin Like Proteins PR5L/TLP (PR-5/thaumatin Like) Antifungal Beta-glucanase αAI/Trypsin inhibitor Antifreeze Cytokinin-binding Xylanase inhibitor Actin binding Protein-Protein or/and Carbohydrate-Protein Interactions Leading To: Energy Metabolism/carbohydrate, FA catabolism Ion transport? Extracellular Matrix Structure? Cell-cell communication?

Diabetes Heart disease Cancer IBD/colitis Antifungal Rheumatoid Arthritis? Inflammation Autoimmune Implications- Uses Of PR-5 Proteins Human Health Prevention/cure Agriculture Benefits Disease protection Increase Yield

Acknowledgements EBNC Research Center, South Korea Kyeong Kyu Kim GNU, South Korea Dae-Jin Yun Purdue Cancer Center Therese Salameh Maxine Nichols Ignacio Camarillo Purdue University Ray Bressan Irina Sokolchik Matilde Paino D’Urzo Maria Coca Ignacio Ibeas Barbara Damsz Mike Hasegawa Jingbo Jin Yinhua Jin Instituto RNA Sevilla, Spain José Pardo University of Kentucky Medical School, Lexington, KY Razvan Arsenescu Violeta Arsenescu Willem de Villiers Pennington Biomedical Institute, Baton Rouge, LA Anthony Civiitarese Eric Ravussin University of Tokyo Medical School, Tokyo Toshimasa Yamauchi Takashi Kadowaki

Plant PR-5 And Mammalian gC1q Domains Have Similar Properties And Functions (Trimer) n Immunity Energy/C utilization Immunity Energy/C utilization C1qTNFαAdiponectinOsmotin/ PR-5 n=1 n=2 n=3 n=4 n=5 n=6 Oligomers LPS, bacterial OM, phospholipid, etc Phospho- mannan 1,3-β-glucan gC1q collagen gC1q-like gC1q collagen gC1q collagen C1qRTNFRAdipo R Adipo R like

Thaumatin 10 5 X sweeter than sucrose Approved for use as calorie-free sweetener Sold in Europe

Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. ‘Samsun’ and ‘Samsun NN’ II. Changes in protein constitution after infection with tobacco mosaic virus L. C. Van Loon and A. Van Kammen Laboratory of Virology, State Agricultural University, Wageningen, The Netherlands Accepted 14 August Available online 16 April Abstract Electrophoresis in 5, 7.5, and 10% acrylamide gels revealed that characteristic changes appear in the protein constitution of N. tabacum var. ‘Samsun,’ ‘Samsun NN,’ and N. glutinosa after infection with tobacco mosaic virus (TMV). Apart from significant quantitative changes, one new band was present in Samsun plants 4 weeks after infection. This band was characterized as TMV coat protein by coelectrophoresis and serology. A change in the electrophoretic mobility of the major band was recorded. In Samsun NN plants four new bands (I–IV) were present 1 week after infection. These bands are not related to TMV coat protein and are not new isozymes of peroxidase, polyphenoloxidase, acid phosphatase, glucose-6-phosphate dehydrogenase, or 6-phosphogluconate dehydrogenase. The bands first appear at the onset of necrosis and increase in intensity with time. Five days after infection band I ceases to increase, whereas bands II, III, and IV increase up to day 14. From day 7 onward, the four bands are also present in the noninoculated, young developing leaves, where they further increase with time. The amount of the four new protein components was related to lesion density and was reduced by treatment of the leaves with actinomycin D 2 days after infection. In N. glutinosa one new band was induced and two bands increased markedly after infection, while one had disappeared from the protein pattern. These changes relate to other protein components than those found in infected Samsun NN, but are also apparent in the noninoculated parts of the plants from day 7 after infection. The possible relation of the new protein components to the phenomenon of systemic acquired resistance is discussed. Virology Volume 40, Issue 2Virology Volume 40, Issue 2, February 1970, Pages