Interaction of S-100 protein with cations and liposomes

Calissano, Pietro; Alemà, Stefano; Fasella, P.

doi:10.1021/bi00719a013

Cited by 99 publications

(32 citation statements)

References 19 publications

(25 reference statements)

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“…These substitutions might suggest different orientation of some residues serving as binding ligands within the loop. However, as seen in the calciumbinding protein of muscle (24) and in bovine S-100 protein (25) (35). In this regard, Mann et al (36) Based on our analysis of the amino acid sequence, we propose a possible model for osteonectin structure (Fig.…”

Section: Honologies Between Osteonectin From Bovine and Humanmentioning

confidence: 83%

“…A search of the NBRF protein data base (18) showed sequence homology between two regions of osteonectin, Asp-165 to Lys-17t0 in domain III and Asp-258 to Glu-269 in domain IV, and the central calcium-binding loop of "EF hand" structures found in bovine brain calmodulin (22,23), the calciumbinding protein of muscle (24), and both the a and 13 chains of bovine S-100 protein (25) (Fig. 3).…”

Section: Resultsmentioning

confidence: 99%

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Osteonectin cDNA sequence reveals potential binding regions for calcium and hydroxyapatite and shows homologies with both a basement membrane protein (SPARC) and a serine proteinase inhibitor (ovomucoid).

Bolander

Young

Fisher

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

170

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Osteonectin is a prominent noncollagenous protein of developing bone. A 2150-base-pair cDNA coding for osteonectin, isolated from a bovine bone cell Agtll expression library, was sequenced and identified by comparison with protein sequence data. The nucleotide sequence predicts that osteonectin contains 304 amino acids, including a 17-residue signal peptide. Analysis of the deduced protein sequence suggests that the secreted protein contains at least four distinct structural domains. An acidic region at the amino terminus of the protein appears to be a potential hydroxyapatite-binding site. This is followed by a second domain, rich in cysteine, that shows sequence homology with cysteine-rich domains in turkey ovomucoid and other serine proteinase inhibitors. Two sequences homologous with central calcium-binding loops of "EF hands" and thus having potential to be high-affinity calcium-binding sites are located in two other domains within the carboxyl-terminal half of the protein. Finally, the osteonectin sequence shows near identity (>90%) with another protein, SPARC (secreted protein, acidic and rich in cysteine), secreted by mouse parietal endoderm. These data suggest that osteonectin, a protein present in bone and other selected tissues, is a multifunctional protein.

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Section: Honologies Between Osteonectin From Bovine and Humanmentioning

confidence: 83%

Section: Resultsmentioning

confidence: 99%

Osteonectin cDNA sequence reveals potential binding regions for calcium and hydroxyapatite and shows homologies with both a basement membrane protein (SPARC) and a serine proteinase inhibitor (ovomucoid).

Bolander

Young

Fisher

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

170

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“…On binding of Ca2+-ions, S100 becomes hydrophobic (Calissano et al 1974;Kligman and Hilt 1988). In this state, S100 may bind to other hydrophobic domains in the tissue as discussed by Moore (1988) and become fixed subsequently; however, Ca2+-dependent hydrophobic interactions have been mainly shown for the a subunit of S100 and not for S100b (Baudier and G6rard 1986), which predominates in the rat brain (Kato et al 1990).…”

Section: Discussionmentioning

confidence: 98%

Modifications of S100-protein immunoreactivity in rat brain induced by tissue preparation

Rickmann¹,

Wolff²

1995

Histochem Cell Biol

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Immunocytochemistry using antibodies against various molecular forms of the Ca++ and Zn(++)-binding S100 proteins predominantly labelled astrocytes. However, especially in the neocortex the staining pattern is variable. Methods of tissue preparation have been evaluated with the aim to preserve as much S100 immunoreactivity as possible. Optimal results were obtained after perfusion fixation with 4-5% aldehydes, 0.1 M sodium cacodylate, 0.1% CaCl2, pH 7.3. In such preparations, astrocytes were completely labelled including their lamellar compartments in large parts of the central nervous system. Ca(++)-withdrawal had adverse affects on S100 immunoreactivity. Cryostat sections treated with EDTA-containing solutions before fixation showed that Ca(++)-free S100 can apparently not be fixed to the tissue. Perfusion fixatives containing EDTA resulted in inhomogeneous loss of S100 staining, indicating a differential susceptibility of astrocytic subpopulations. A different type of reduction in S100 immunoreactivity occurred around large neocortical blood vessels. Perivascular defects in immunostaining occasionally appeared even after optimal fixation, but could be regularly provoked by mildly acidic fixation (pH 6.6) or prolonged barbiturate anaesthesia. These defects might be based on S100 release into the cerebrospinal fluid. Presumably under none of the conditions studied can the immunoreactivity of all S100-forms and -fractions be completely preserved in the tissue. However, recommendations are presented for optimizing tissue preparation, to the extent that premortal modifications affecting the stainability of astrocytes may be detected by S100 immunohistochemistry in fixed brain tissue.

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“…UV difference spectroscopy also suggests that the single tryptophan and the tyrosine chromophores in S-100a are blue shifted (i.e., exposed to the solvent) in the presence of CaZ+, in contrast to the observed red shift noted with S-100b. protein is unknown; however, existing literature suggests a role for it in the function or development of the nervous system (Hyden & Lange, 1970;Calissano & Bangham, 1971;Calissano et al, 1974).…”

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confidence: 99%

Isolation and spectral studies on the calcium binding properties of bovine brain S-100a protein

Mani¹,

Kay²

1983

Biochemistry

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Interaction of S-100 protein with cations and liposomes

Cited by 99 publications

References 19 publications

Osteonectin cDNA sequence reveals potential binding regions for calcium and hydroxyapatite and shows homologies with both a basement membrane protein (SPARC) and a serine proteinase inhibitor (ovomucoid).

Osteonectin cDNA sequence reveals potential binding regions for calcium and hydroxyapatite and shows homologies with both a basement membrane protein (SPARC) and a serine proteinase inhibitor (ovomucoid).

Modifications of S100-protein immunoreactivity in rat brain induced by tissue preparation

Isolation and spectral studies on the calcium binding properties of bovine brain S-100a protein

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