Identification of novel members of the serum amyloid A protein superfamily as constitutive apolipoproteins of high density lipoprotein. Funding Information This paper was supported by the following grants: Processing of X-ray diffraction data collected in oscillation mode. Saa transcript abundance was determined by Q-PCR. Serum amyloid A-luciferase transgenic mice:

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Please review our privacy policy. However, the identity of potential SAA ligand s remains unclear. However, it retains the hydrophobic amino acids that are predicted to line the hydrophobic binding pocket in SAA3. Processing of X-ray diffraction data collected in oscillation mode. First, SAAs are strongly induced by microbial exposure at sites of retinol uptake intestine and storage liverand are present at high mouee in the circulation following microbial challenge Chiba et al.

H-Antigen, dual oxidases, the NHE antiporter and the granzymes all have interesting disease associations. Secondary structure is based on the mSAA3 crystal structure and is indicated above the sequence.

These values are similar to binding affinities calculated for human serum retinol binding protein hRBP Cogan et al. Residues that make dimer kx-w103 are shown as green sticks while residues involved in tetramer stabilization are shown as yellow sticks.

A key question is whether there are tissue-specific effects of intestinal epithelial SAAs, or whether the intestinal SAAs enter the circulation with bound retinol acquired directly from the diet. Reviewers have the opportunity to discuss the decision lx-a103 the letter is sent see review process. Figure 3—figure supplement 1. The genes that show consistent expression differences include saa 1 and 2 please note that I assume that saa 3 should be substituted for one of the saa1 labels, which appear twice in Figure 1—figure supplement 1.


B Top view of the tetrameric mSAA3 structure. B A semi-transparent surface representation of mluse protein llx-w103 the same orientation as Figure 4Bwith a muse trace.

Refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol.

Retinoic acid lacks intrinsic fluorescence but can quench inherent protein fluorescence due to energy transfer from tryptophan residues Cogan et al. B Mose was detected in peak 1 by Western blot. Mouse and human SAAs bound retinol with nanomolar affinity, were associated with retinol in vivo, and limited the bacterial burden in tissues after acute infection.

SAA expression requires dietary vitamin A.


Introduction Retinol plays a vital role in the physiological response to microbial challenge. There are multiple probe sets representing Saa1 on the Affymetrix arrays and both of these probe sets showed a change in transcript abundance.

CMZ, Conception and design, Acquisition of data, Analysis and interpretation of data, Drafting or revising the article. Serum amyloid A-luciferase transgenic mice: We speculate that SAAs mediate retinol transport during such inflammatory states just as they do during infection, and plan to investigate this possibility in our future studies. All- trans -retinoic acid was titrated into mSAA3 and fluorescence quenching was monitored following excitation at nm.


Recombinant mSAA1 and 3 were expressed and purified as described below.

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mous Serum amyloid A SAA proteins are strongly induced in the liver by systemic infection and in the intestine by bacterial colonization, but their exact functions remain unclear. E K d s were calculated from the binding assay data plotted in B and D and were derived from three independent experiments. Finally, we provide structural insight into the binding interaction by solving the mouse SAA3 crystal structure, which reveals a tetrameric assembly with a hydrophobic binding moue that can accommodate retinol.

Mothers and pups were maintained on the diets until weaning, and pups stayed on the diet for two additional moue prior to sacrifice. Crystal structure data collection and refinement statistics are provided in Table 2 ; alignments of mouse and human SAAs are shown in Figure 4—figure supplement 1 ; parameters from the protein Interfaces, Surfaces, and Assemblies PISA analysis showing a tetrameric state are provided in Table 3. Open in a separate window. Immunofluorescence analysis Zinc-fixed, paraffin embedded tissue sections were stained with anti-SAA antiserum raised against purified recombinant mSAA1 and detected using a goat anti-rabbit IgG Cy3 conjugate Biomeda.

Single-wavelength anomalous dispersion SAD data moouse collected at the selenium K edge 0.