Abstract
Peptides have been proposed to function in intracellular signaling within the cytosol. Although cytosolic peptides are considered to be highly unstable, a large number of peptides have been detected in mouse brain and other biological samples. In the present study, we evaluated the peptidome of three diverse cell lines: SH-SY5Y, MCF7, and HEK293 cells. A comparison of the peptidomes revealed considerable overlap in the identity of the peptides found in each cell line. The majority of the observed peptides are not derived from the most abundant or least stable proteins in the cell, and approximately half of the cellular peptides correspond to the N- or C- termini of the precursor proteins. Cleavage site analysis revealed a preference for hydrophobic residues in the P1 position. Quantitative peptidomic analysis indicated that the levels of most cellular peptides are not altered in response to elevated intracellular calcium, suggesting that calpain is not responsible for their production. The similarity of the peptidomes of the three cell lines and the lack of correlation with the predicted cellular degradome implies the selective formation or retention of these peptides, consistent with the hypothesis that they are functional in the cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1583-1592 |
| Number of pages | 10 |
| Journal | Journal of Proteome Research |
| Volume | 10 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 1 2011 |
Fingerprint
Keywords
- HEK293
- hemopressin
- MCF7
- peptides
- peptidomics
- SH-SY5Y
ASJC Scopus subject areas
- Biochemistry
- Chemistry(all)
Cite this
Peptidomic analysis of human cell lines. / Gelman, Julia S.; Sironi, Juan; Castro, Leandro M.; Ferro, Emer S.; Fricker, Lloyd D.
In: Journal of Proteome Research, Vol. 10, No. 4, 01.04.2011, p. 1583-1592.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Peptidomic analysis of human cell lines
AU - Gelman, Julia S.
AU - Sironi, Juan
AU - Castro, Leandro M.
AU - Ferro, Emer S.
AU - Fricker, Lloyd D.
PY - 2011/4/1
Y1 - 2011/4/1
N2 - Peptides have been proposed to function in intracellular signaling within the cytosol. Although cytosolic peptides are considered to be highly unstable, a large number of peptides have been detected in mouse brain and other biological samples. In the present study, we evaluated the peptidome of three diverse cell lines: SH-SY5Y, MCF7, and HEK293 cells. A comparison of the peptidomes revealed considerable overlap in the identity of the peptides found in each cell line. The majority of the observed peptides are not derived from the most abundant or least stable proteins in the cell, and approximately half of the cellular peptides correspond to the N- or C- termini of the precursor proteins. Cleavage site analysis revealed a preference for hydrophobic residues in the P1 position. Quantitative peptidomic analysis indicated that the levels of most cellular peptides are not altered in response to elevated intracellular calcium, suggesting that calpain is not responsible for their production. The similarity of the peptidomes of the three cell lines and the lack of correlation with the predicted cellular degradome implies the selective formation or retention of these peptides, consistent with the hypothesis that they are functional in the cells.
AB - Peptides have been proposed to function in intracellular signaling within the cytosol. Although cytosolic peptides are considered to be highly unstable, a large number of peptides have been detected in mouse brain and other biological samples. In the present study, we evaluated the peptidome of three diverse cell lines: SH-SY5Y, MCF7, and HEK293 cells. A comparison of the peptidomes revealed considerable overlap in the identity of the peptides found in each cell line. The majority of the observed peptides are not derived from the most abundant or least stable proteins in the cell, and approximately half of the cellular peptides correspond to the N- or C- termini of the precursor proteins. Cleavage site analysis revealed a preference for hydrophobic residues in the P1 position. Quantitative peptidomic analysis indicated that the levels of most cellular peptides are not altered in response to elevated intracellular calcium, suggesting that calpain is not responsible for their production. The similarity of the peptidomes of the three cell lines and the lack of correlation with the predicted cellular degradome implies the selective formation or retention of these peptides, consistent with the hypothesis that they are functional in the cells.
KW - HEK293
KW - hemopressin
KW - MCF7
KW - peptides
KW - peptidomics
KW - SH-SY5Y
UR - http://www.scopus.com/inward/record.url?scp=79953686243&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79953686243&partnerID=8YFLogxK
U2 - 10.1021/pr100952f
DO - 10.1021/pr100952f
M3 - Article
C2 - 21204522
AN - SCOPUS:79953686243
VL - 10
SP - 1583
EP - 1592
JO - Journal of Proteome Research
JF - Journal of Proteome Research
SN - 1535-3893
IS - 4
ER -