The S100 protein family

Kligman, Douglas; Hilt, Dana

doi:10.1016/0968-0004(88)90218-6

Cited by 512 publications

(396 citation statements)

References 31 publications

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“…Calcyclin is a member of a recently described family of Ca2+-binding proteins (for review see [4]). With one exception, all members of this family contain two functional EF-hands.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the cell‐cycle‐regulated protein calcyclin from Ehrlich ascites tumor cells

Filipek

Gerke

Weber

et al. 1991

European Journal of Biochemistry

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The nearly complete amino acid sequence obtained for murine calcyclin from Ehrlich ascites tumor cells reveals a very strong similarity with the rat and human sequences previously deduced from corresponding cDNA clones. While mouse and rat calcyclins are identical, the human protein shows at three positions a conservative amino acid replacement. Using a mouse calcyclin affinity matrix, two proteins with molecular masses of about 36 kDa have been purified from Ehrlich ascites tumor cells. The interaction between these two proteins and the immobilized calcyclin is strictly Ca2 +-dependent. Immunological criteria and partial sequence data identify the two calcyclinbinding proteins as the phospholipid-binding protein annexin I1 (p36) and the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. These observations suggest that calcyclin may exert its physiological function by a Ca''-dependent interaction with cellular targets, e. g. annexin I1 or glyceraldehyde-3-phosphate dehydrogenase.

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“…Calcyclin is a member of a recently described family of Ca2+-binding proteins (for review see [4]). With one exception, all members of this family contain two functional EF-hands.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the cell‐cycle‐regulated protein calcyclin from Ehrlich ascites tumor cells

Filipek

Gerke

Weber

et al. 1991

European Journal of Biochemistry

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“…The solution structure of reduced apo-SlOOB(PP) shows that two subunits associate tightly (KD < 500 pM) (Drohat et al, 1997) through extensive hydrophobic interactions to form a compact dimer with a highly charged surface (Amburgey et al, 1995;Drohat et al, 1996;Kilby et al, 1996). The general model for S 100-target protein interactions is similar to that of other CaZf-binding proteins, such as calmodulin and troponin C. As for these proteins, S100B(PP) undergoes a conformational change upon binding Ca2+ that promotes its interaction with a variety of target proteins (Kligman & Hilt, 1988;Drohat et al, 1996;Chaudhuri et al, 1997). For example, the Ca2+-dependent binding of SlOOB(PP) to microtubules (Bianchi et al, 1993), GFAP (Bianchi et al, 1994), and p53 (Baudier et al, 1992) prevents oligomerization for each of these proteins.…”

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confidence: 99%

“…A comparison of the Ca2+-dependent inhibition constant (CaICso = 29.3 f 17.6 pM; Fig. 2 (Baudier et al 1986;Kligman & Hilt, 1988;Zimmer et al, 1995)' indicates that at least the C-terminal EF-hand of each SlOOP subunit must be saturated to inhibit phosphorylation. As in PKM assays, low concentrations of S100B(PP) were able to inhibit full-length PKCa (s100BIC50 = 10 f 7 pM; Fig.…”

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confidence: 99%

S100B(ββ) inhibits the protein kinase C‐dependent phosphorylation of a peptide derived from p53 in a Ca²⁺‐dependent manner

et al. 1998

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S100B(PP) is a dimeric Ca2+-binding protein that is known to inhibit the protein kinase C (PKC)-dependent phosphorylation of several proteins. To further characterize this inhibition, we synthesized peptides based on the PKC phosphorylation domains of p53 (residues 367-388), neuromodulin (residues 37-53), and the regulatory domain of PKC (residues 19-31), and tested them as substrates for PKC. All three peptides were shown to be good substrates for the catalytic domain of PKC. As for full-length p53 (Baudier J, Delphin C, Grunwald D, Khochbin S, Lawrence JJ. 1992. Proc Nut1 Acud Sci USA 89:11627-11631), S100B(PP) binds the p53 peptide and inhibits its PKC-dependent phosphorylation (IC50 = 10 f 7 pM) in a Ca2+-dependent manner. Similarly, phosphorylation of the neuromodulin peptide and the PKC regulatory domain peptide were inhibited by SlOOB(PP) in the presence of Ca2+ (IC50 = 17 f 5 pM; IC50 = 1 + 0.5 pM, respectively).At a minimum, the C-terminal EF-hand Ca2+-binding domain (residues 61-72) of each Sloop subunit must be saturated to inhibit phosphorylation of the p53 peptide as determined by comparing the Ca2+ dependence of inhibition = 29.3 * 17.6 pM) to the dissociation of Ca2+ from the C-terminal EF-hand Ca2+-binding domain of SlOOB(PP).

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“…Non-covalent A8 homodimers were also observed using mass spectrometry [8]. Ca 2ϩ -binding induces structural changes within helices III and IV, exposing amino acids within the hinge and C-terminal domains that may be involved in binding target proteins [5,9]. Covalent oxidative modifications may regulate the functions of S100B, A8, and S100A2 [10 -12].…”

mentioning

confidence: 99%

Electrospray low energy CID and MALDI PSD fragmentations of protonated sulfinamide cross-linked peptides

Raftery

Geczy

2002

J. Am. Soc. Mass Spectrom.

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Murine S100A8 (A8) is a major cytoplasmic neutrophil protein and is converted to novel oxidation products containing Cys-amino-Lys sulfinamide cross-links and Met-sulfoxide by the neutrophil oxidant HOCl. Seven products were separated using RP-HPLC, with electrospray ionization mass spectrometry (ESI-MS) masses after deconvolution of 10,354, 10,388, Ϯ1, and 20,707, Ϯ3 Da, and all were resistant to reduction by dithiothreitol. The major products with masses of 10,354 Da contained Cys 41 -Lys 34/35 intramolecular cross-links. Additional isomeric products with identical masses (10,354 Da) were isolated and peptide mapping and ESI/MS indicated that Cys 41 forms covalent sulfinamide cross-links with either Lys 6 , Lys 76 , Lys 83 , or Lys 87 present in A8. Electrospray low energy collisionally induced (CID) spectra of multiply-charged AspN digest peptides with sulfinamide cross-links contained characteristic fragmentations that corresponded to simple cleavage of the nitrogen™sulfur bond with charge retention on either of the fragment ions, allowing conformation of cross-linked peptides. Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) post source decay spectra of [M ϩ H] ϩ ions of the same sulfinamide-containing cross-linked peptides fragment similarly, but additional facile fragmentation reactions corresponding to formation of a protonated peptide containing de-hydroalanine were attributed to cleavage of the carbon™sulfur bond. In addition, lose of methanesulfenic acid from Met-sulfoxide was observed. A sulfinamide-containing adduct was isolated after incubation of the A8/HOCl reaction mixture with Lys or ␣ N-acetyl Lys with masses of 10,500 or 10,542 Da. ESI/MS/MS and MALDI/ post decay source (PSD) analysis of A8 32-57 -sulfinamide showed the same characteristic fragmentations as those in the sulfinamide cross-linked peptides, confirming the Cys 41 -Lys sulfinamide cross-link and suggesting that peptide-peptide sulfinamides may all fragment similarly, allowing ready identification of these cross-links in proteins from more complex biological materials. (J Am Soc Mass Spectrom 2002, 13, 709 -718)

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The S100 protein family

Cited by 512 publications

References 31 publications

Characterization of the cell‐cycle‐regulated protein calcyclin from Ehrlich ascites tumor cells

Characterization of the cell‐cycle‐regulated protein calcyclin from Ehrlich ascites tumor cells

S100B(ββ) inhibits the protein kinase C‐dependent phosphorylation of a peptide derived from p53 in a Ca²⁺‐dependent manner

Electrospray low energy CID and MALDI PSD fragmentations of protonated sulfinamide cross-linked peptides

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The S100 protein family

Cited by 512 publications

References 31 publications

Characterization of the cell‐cycle‐regulated protein calcyclin from Ehrlich ascites tumor cells

Characterization of the cell‐cycle‐regulated protein calcyclin from Ehrlich ascites tumor cells

S100B(ββ) inhibits the protein kinase C‐dependent phosphorylation of a peptide derived from p53 in a Ca2+‐dependent manner

Electrospray low energy CID and MALDI PSD fragmentations of protonated sulfinamide cross-linked peptides

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S100B(ββ) inhibits the protein kinase C‐dependent phosphorylation of a peptide derived from p53 in a Ca²⁺‐dependent manner