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Journal of Dental Research
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Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein

C. Geetha1,2, S.G. Venkatesh1,*, L. Bingle3, C.D. Bingle3 and S.-U. Gorr1,4

1 Department of Periodontics, Endodontics and Dental Hygiene, Room 209C, and
4 Department of Biochemistry and Molecular Biology, University of Louisville Health Sciences Center, School of Dentistry, Louisville, KY 40292, USA;
3 Academic Unit of Respiratory Medicine, Division of Genomic Medicine, The University of Sheffield Medical School, Royal Hallamshire Hospital, Sheffield S10 2JF, UK;


Figure 1
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  		Figure 1. PLUNC and PSP expression in human tissues. Expression of PLUNC and PSP was investigated by the use of RT-PCR with exon-spanning primer pairs as described in MATERIALS & METHODS. The negative control was a reverse-transcription reaction performed in the absence of RT enzyme.

 

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  		Figure 2. Molecular modeling of human PSP. (A) Sequence alignment of hPSP, hPLUNC, and the N-terminal domain of BPI (BPI1). The PSP and PLUNC peptides and a peptide in the LPS-binding domain of BPI (Dankesreiter et al., 2000) are underlined. The putative signal peptides of PSP (20 residues) and BPI are not shown. (B) The PSP sequence was modeled with the 3D-PSSM package. The locations of the 3 PSP peptides are highlighted in black.

 

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  		Figure 3. Inhibition of TNF{alpha} secretion from RAW 264.7 cells. RAW 264.7 cells were incubated with lipopolysaccharide (LPS) and substance P, the PSP-derived peptides KN-11, KK-9, or GK-7, or with polymyxin B. The secretion media were assayed for TNF{alpha}. Values obtained were normalized to TNF{alpha} secretion in the presence of LPS alone (100%). Values presented are the mean ± SEM of 3 independent experiments. *Different from secretion in the presence of LPS and substance P. P < 0.05.

 

Journal of Dental Research, Vol. 84, No. 2, 149-153 (2005)
DOI: 10.1177/154405910508400208
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