2006
DOI: 10.1016/j.peptides.2006.01.005
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Ghrelin in plants: What is the function of an appetite hormone in plants?

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Cited by 13 publications
(12 citation statements)
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“…It has been suggested that ghrelin-like molecules, i.e., those structurally related to the appetite-stimulating lipopeptide hormone which was first isolated from the gastrointestinal tract of rats (Kojima et al, 1999), are ubiquitously present in living organisms (Aydin et al, 2006). These molecules have been found in microorganisms (i.e., viruses, archaea, and phototrophic bacteria), animals and plants, where they fulfill different functions (e.g., inhibition of apoptosis), especially those connected with food intake and cell proliferation (Aydin, 2007).…”
Section: Communication Signals Through Different Biological Kingdomsmentioning
confidence: 99%
See 1 more Smart Citation
“…It has been suggested that ghrelin-like molecules, i.e., those structurally related to the appetite-stimulating lipopeptide hormone which was first isolated from the gastrointestinal tract of rats (Kojima et al, 1999), are ubiquitously present in living organisms (Aydin et al, 2006). These molecules have been found in microorganisms (i.e., viruses, archaea, and phototrophic bacteria), animals and plants, where they fulfill different functions (e.g., inhibition of apoptosis), especially those connected with food intake and cell proliferation (Aydin, 2007).…”
Section: Communication Signals Through Different Biological Kingdomsmentioning
confidence: 99%
“…These molecules have been found in microorganisms (i.e., viruses, archaea, and phototrophic bacteria), animals and plants, where they fulfill different functions (e.g., inhibition of apoptosis), especially those connected with food intake and cell proliferation (Aydin, 2007). For instance, a structural homolog ( N -octanoyl homoserine lactone) of ghrelin is produced by Gram-negative bacteria as a quorum sensing (QS) autoinducer and cell-to-cell communication molecule, which is also involved in food-searching (Aydin et al, 2006). …”
Section: Communication Signals Through Different Biological Kingdomsmentioning
confidence: 99%
“…ELISA (quantitative analysis) and a highly specific immunohistochemical analysis that utilized a human anti‐ghrelin antibody demonstrated that ghrelin‐like peptides were present in the flower bud of S. aromaticum but not in the tissues of the branch of S. persica . S. aromaticum contains ghrelin at concentrations higher than those in human salivary gland (Figure 1), rat kidney, human kidney, human stomach, P. x domestica L (common plum) and Morus alba (mulberry) (Aydin et al, 2006). From the calculated molecular mass of 3244.6 for the 28‐amino acid sequence of the peptide, these concentrations are significantly higher than the average ghrelin levels (150 fmol) found in the plasma of fasting humans (reviewed, Aydin, 2007).…”
Section: Resultsmentioning
confidence: 99%
“…IHC was carried out using the ABC (streptavidin—avidin–biotin—peroxidase complex) procedure with minor modifications (Hsu et al, 1981; Aydin et al, 2006). Sections (4 μm) were mounted on silanized slices, and the solutions utilized were freshly prepared before staining.…”
Section: Methodsmentioning
confidence: 99%
“…The presence of this hormone, however, has recently been reported in various other tissues, organs (Kojima and Kangawa, 2005;Aydin, 2007a) and body fluids such as saliva (Aydin et al, 2005;Groschl et al, 2005), milk (Aydin et al, 2006a;Ilcol and Hizli, 2007) and urine (Yoshimoto et al, 2002). Further, a recent study from this laboratory reported the expression of this hormone in various plants (Aydin et al, 2006b), indicating an evolutionary origin. The peptide is composed of 28 amino acid residues and acts as a growth hormone releaser and also an appetite stimulator.…”
Section: Introductionmentioning
confidence: 94%