30 S.P. to B. St. Michel

Pepys, Samuel; Heath, Helen Truesdell

doi:10.1093/oseo/instance.00005860

Cited by 5 publications

(7 citation statements)

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“…An interesting aspect of the acute phase response is the species specificity of individual acute phase proteins. For instance, af2-macroglobulin (a12-MG) is a major acute phase reactant in rats but not in mice or man (Kushner, 1982); SAP is induced several-fold during inflammation in mice but not in man; the reverse being true for CRP (Pepys and Baltz, 1983). Our results with the CRP gene suggest that the species specificity is exclusively due to the properties of the individual genes and to the way cis-acting regulatory sequences located in them are able to interact with widespread and evolutionary conserved trans-acting regulatory factors.…”

Section: Transcriptional Control Of Crp E-xpressionmentioning

confidence: 99%

“…One of the major acute phase reactants in man is C-reactive protein (CRP), which belongs to the pentraxin gene family together with the serum amyloid protein (SAP) and the female hamster protein (for a review, see Pepys and Baltz, 1983). Dur-ing acute inflammation the serum level of human CRP rises from <1 mg/l to 300 mg/l (Kushner and Feldman, 1978) and this 1000-fold increase in concentration corresponds with the availability of the specific mRNA in liver cells (Whitehead et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

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Inducible and tissue-specific expression of human C-reactive protein in transgenic mice.

Ciliberto¹,

Arcone²,

Wagner³

et al. 1987

The EMBO Journal

123

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C‐reactive protein (CRP) is a major acute phase reactant in man but not in mouse. It is synthesized in abundant quantities by human hepatocytes during the course of several diseases, mainly acute inflammations. To investigate the regulation of CRP expression, the human CRP gene was introduced into fertilized eggs by microinjection and transgenic mouse lines were derived. The CRP gene is exclusively transcribed in the liver and expression is strictly dependent on experimental inflammation. The kinetics of induction both for RNA and protein synthesis is very fast; RNA is first detectable after 2 h in the liver, the protein after 6 h in the serum. Human CRP levels in the sera of transgenic mice are comparable to those observed in human diseases. Nuclear run‐on experiments indicate that regulation is primarily at the transcriptional level.

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Section: Transcriptional Control Of Crp E-xpressionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Inducible and tissue-specific expression of human C-reactive protein in transgenic mice.

Ciliberto¹,

Arcone²,

Wagner³

et al. 1987

The EMBO Journal

123

View full text Add to dashboard Cite

show abstract

“…SAP is related in structure to C-reactive protein (CRP), which also belongs to the pentraxin protein family [33,34]. In humans CRP is a major acute phase reactant that is massively induced by in£ammation and provides enhanced protection against invading micro-organisms, limit tissue damage and promote a rapid return to homeostasis [29].…”

Section: Discussionmentioning

confidence: 99%

“…Although the physiological function of SAP is largely unknown, SAP has received considerable medical interest as it associates with all types of amyloid deposits, including those found in Alzheimer's disease [33,35]. SAP has a high tendency to undergo Ca 2 -dependent self-aggregation, which may be important for its deposition in amyloid.…”

Section: Discussionmentioning

confidence: 99%

Calumenin interacts with serum amyloid P component

2000

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“…Human serum amyloid P component (SAP) belongs to the family of pentraxins, defined by their characteristic pentameric organization of identical subunits [14]. In comparison to the structure of the human acute phase reactant C-reactive protein with its five promoters, native SAP is arranged as a planar, non-covalently linked face-to-face dimer of two disc-shaped pentamers, constituting a decameric complex [2][3][4][5][6][7]. Further aggregation can be mediated by increasing the Ca z+ concentration [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Effect of enzymatic desialylation of human serum amyloid P component on surface exposure of laser photo CIDNP (chemically induced dynamic nuclear polarization) ‐ reactive histidine, tryptophan and tyrosine residues

et al. 1995

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The human pentraxin serum amyioid P component (SAP) exhibits no microheterogeneity in its complex di-antennary glycan. To elucidate whether the removal of sialic acids from this glycoprotein might affect the accessibility of certain amino acid residues of the protein we employed the laser photo CIDNP approach as a sensitive tool. The CIDNP effect is created by the interaction of a photoexcited dye with reactive amino acids and results in enhanced absorption-or emission-signals which can be observed for the three aromatic amino acids histidine, tryptophan, and tyrosine if they are accessible to the dye. Therefore, this technique can be applied to explore surface exposure of these residues. The respective spectra of SAP and enzymatically desialylated SAP were determined. Six tryptophan/histidine signals and one tyrosine signal are present in the aromatic part of the CIDNP difference spectrum of SAP. The corresponding spectrum of desialylated SAP shows remarkable alterations. The chemical shift of one tryptophan/histidine-characteristic signal is decreased by 0.1 ppm. One tryptophan/histidine signal disappeared and a new one was formed in the CIDNP difference spectrum of desialylated SAP, while the other signals were unaffected. The tyrosine signal has a clearly enhanced intensity in desialylated SAP. Therefore, the removal of sialic acid moieties from the single N-glycan of each monomer apparently affects surface presentation of distinct ClDNP-reactive amino acids of SAP.Key words: Chemically induced dynamic nuclear polarization (CIDNP); Glycoprotein; Human serum amyloid P component (SAP); Sialic acid 3-sulfated derivatives of galactose, N-acetylgalactosamine and glucuronic acid, which are thought to influence the deposition of SAP to amyloid fibrils and bacterial surfaces [9][10][11][12]. The protein part of human SAP and its tissue form shown no disease-associated alterations, which is also true for threir glycosylation pattern [12]. SAP contains one invariant complex diantennary glycan Asn 3z, located on a fl-strand under the single c~-helix on the promoter surface opposite of the Ca 2+-and ligand-binding site [12][13][14][15]. This lack of microheterogeneity is unusual and may thus be structurally and/or functionally important.Enzymic removal of sialic acids provides a means to address the potential role(s) of this monosaccharide. With respect to catabolism, the desialylated form will be rapidly transported into hepacytes via asialoglycoprotein receptor-mediated endocytosi for lysosomal degradation [15]. Structurally, it retains its decameric state of aggregation and its full capacity to bind in vitro to amyloid fibrils and to DNA, whereas its interaction with agarose is reduced by 7% despite to opposite locations of the carbohydrate chain and the ligand-binding site [13,[15][16][17]. To answer the question, whether removal of the two sialic acid moieties from the single N-linked saccharide chain per promoter may cause a change in surface exposure of aromatic amino acids, a sensitive assay system is r...

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30 S.P. to B. St. Michel

Cited by 5 publications

References 0 publications

Inducible and tissue-specific expression of human C-reactive protein in transgenic mice.

Inducible and tissue-specific expression of human C-reactive protein in transgenic mice.

Calumenin interacts with serum amyloid P component

Effect of enzymatic desialylation of human serum amyloid P component on surface exposure of laser photo CIDNP (chemically induced dynamic nuclear polarization) ‐ reactive histidine, tryptophan and tyrosine residues

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