Climate Change, Growth, and California Wildfire

Large wildfire occurrence and burned area are modeled using hydroclimate and landsurface characteristics under a range of future climate and development scenarios. The range of uncertainty for future wildfire regimes is analyzed over two emissions pathways (the Special Report on Emissions Scenarios [SRES] A2 and B1 scenarios); three global climate models (Centre National de Recherches Météorologiques CM3, Geophysical Fluid Dynamics Laboratory CM21 and National Center for Atmospheric Research PCM2); a mid‐range scenario for future population growth and development footprint; two model specifications related to the uncertainty over the speed and timing with which vegetation characteristics will shift their spatial distributions in response to trends in climate and disturbance; and two thresholds for defining the wildland‐urban interface relative to housing density. Results were assessed for three 30‐year time periods centered on 2020, 2050, and 2085, relative to a 30‐year reference period centered on 1975. Substantial increases in wildfire are anticipated for most scenarios, although the range of outcomes is large and increases with time. The increase in wildfire area burned associated with the higher emissions pathway (SRES A2) is substantial, with increases statewide ranging from 57 percent to 169 percent by 2085, and increases exceeding 100 percent in most of the forest areas of Northern California in every SRES A2 scenario by 2085. The spatial patterns associated with increased fire occurrence vary according to the speed with which the distribution of vegetation types shifts on the landscape in response to climate and disturbance, with greater increases in fire area burned tending to occur in coastal southern California, the Monterey Bay area and northern California Coast ranges in scenarios where vegetation types shift more rapidly.National Oceanic and Atmospheric Administration (NOAA) Regional Integrated Science and Assessment Program for California, United StatesCalifornia Climate Change Center/[CEC-500-2009-046-F]//Estados UnidosUnited States Department of Agriculture (USDA) Forest Service Pacific Southwest Research Station///Estados UnidosNational Oceanic and Atmospheric Administration (NOAA) Regional Integrated Science and Assessment Program for California///Estados UnidosUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias Básicas::Centro de Investigaciones Geofísicas (CIGEFI

Affinity chromatography of non-modified and FITC-modified pIgG_mix on DNA-cellulose.

<p>(–) and (–), absorbance of IgGs at 280 nm before and after modification of IgGs with FITC, respectively; the bars correspond to the relative fluorescence of FITC-IgG_mix fractions (A). Analysis of a relative efficiency of specific-molecule exchange under different conditions between non-modified IgG_mix and FITC-IgG_mix having different affinity for DNA-cellulose (B–D). Before chromatography, the IgG_mix eluted from DNA-cellulose by 0.15 M NaCl (0.15 M-IgG_mix) were incubated with FITC-IgG_mix eluted by 1.5 M NaCl (1.5 M-FITC-IgG_mix) in the presence of TBS and GSH (B); 0.5 M-IgG_mix and 1.5 M-FITC-IgG_mix (C) or 0.5 M-FITC-IgG_mix +1.5 M-IgG_mix (D) were incubated in the presence of TBS containing GSH and human milk plasma.</p

Sequential affinity chromatography of sIgA-2 and sIgA-3 preparations on casein-Sepharose and lipid-resin.

<p>After chromatography of sIgA-2 and sIgA-3 preparations on ATP-Sepharose (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048756#pone-0048756-g003" target="_blank">Figs 3C and 3D</a>, respectively), fractions 10–18 having high affinity to ATP-Sepharose were combined and chromatographed on casein-Sepharose (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048756#pone-0048756-g004" target="_blank">Figs 4A and 4B</a>, respectively). Panel C demonstrates chromatography on lipid-resin of a mixture of fractions 9–17 corresponding to sIgA-2 and sIgA-3 eluted from casein-Sepharose (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048756#pone-0048756-g003" target="_blank">Figs 3C and 3D</a>): (–), absorbance at 280 nm; relative catalytic activities (RA) in the hydrolysis of DNA (▵), phosphorylation of casein (□) and lipids tightly bound with Abs (▪). Depending on the RA and reaction analyzed, the reaction mixtures were incubated for 0.5–2 h and then the RAs were normalized to the standard conditions and the RA of the fraction with the highest activity was taken for 100%. The average error in the initial rate determination from two experiments in every case did not exceed 7–10%. See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048756#s4" target="_blank">Materials and methods</a> for other details.</p

Affinity chromatography of milk pIgGs on two different resins.

<p>Various IgG fractions were separated using DNA-cellulose (A) and ATP-Sepharose (B): (–), absorbance at 280 nm; symbols correspond to the relative catalytic activities (RA) in the hydrolysis of DNA (▵), ATP (○), oligosaccharides (×); phosphorylation of lipids (▪) and polysaccharides (⋄) tightly bound with IgGs. Depending on the RA and reaction analyzed, the reaction mixtures were incubated for 0.5–2 h and then the RAs were normalized to the standard conditions and the RA of the fraction with the highest activity was taken for 100%. The average error in the initial rate determination from two experiments in each case did not exceed 7–10%.</p

The dependencies of the absorbance (A₄₅₀) on the concentration of tested IgG preparation.

<p>The analysis was performed using a direct (A) and sandwich (B) ELISA. For a direct analysis, the tested IgG preparations were adsorbed on ELISA strips, then mouse Abs against human kappa-IgGs or lambda-IgGs (anti-kappa-Abs and anti-lambda-Abs) were added, and finally the conjugate of polyclonal rabbit anti-mouse IgGs with horseradish peroxidase (HRP) was used (C). For a sandwich analysis, anti-kappa-Abs and anti-lambda-Abs were adsorbed on ELISA strips, then tested IgG preparations were added, and finally the conjugate of HRP with mouse Abs against human kappa-IgGs or lambda-IgGs (anti-x-Ab-HRP) were used (B). Anti-lambda-Abs (or anti-lambda-Abs and anti-lambda-Ab-HRP) were used for the analysis of the content of IgGs having affinity only for anti-lambda-Ab-Sepharose (▪), for anti-kappa-Ab-Sepharose (□), and for both of these Sepharoses (▴), while anti-kappa-Abs (or anti-kappa-Abs and anti-kappa-Ab-HDP) were used for the analysis of preparations having affinity only for anti-kappa-Ab-Sepharose (•), for anti-lambda-Ab-Sepharose (○), and for both of these Sepharoses (▾). (⋄), a control mixture containing no analyzed IgGs (A and B). The RAs of lambda-IgGs, kappa-IgGs, and kappa-lambda-IgGs in the catalysis of different chemical reactions (C). The RA of the preparation with the highest activity in each reaction analyzed was taken for 100%. See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042942#s4" target="_blank">Materials and Methods</a> for other details.</p

Affinity chromatography of milk sIgA-1 preparation from first donor on DNA-cellulose and ATP-Sepharose.

<p>sIgA-1 preparation was chromatographed on DNA-cellulose (A) and ATP-Sepharose (B) in standard conditions: (–), absorbance at 280 nm; symbols correspond to the relative catalytic activities (RA) in the hydrolysis of DNA (▵), ATP (○), oligosaccharides (×) as well as phosphorylation of lipids (▪) and polysaccharides (⋄) tightly bound with sIgAs. Depending on the RA and reaction analyzed, the reaction mixtures were incubated for 0.5–2 h and then the RAs were normalized to the standard conditions and the RA of the fraction with the highest activity was taken for 100%. The average error in the initial rate determination from two experiments in each case did not exceed 7–10%. See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048756#s4" target="_blank">Materials and methods</a> for other details.</p

Affinity chromatography of milk pIgGs on anti-kappa-L-Sepharose.

<p>The chromatography was performed under the conditions of over-saturation of the affinity capacity of the sorbent (A) and re-chromatography of the preparation eluted by acidic buffer (peak 2) on anti-lambda-L-Sepharose (B) under the conditions of the excess of the affinity sorbent. After incubation of a mixture of equal amounts of purified lambda- and kappa-IgGs for 24 h, lambda+kappa-IgG_mix was subjected to standard affinity chromatography on Protein G-Sepharose (C) and gel filtrated (data not shown). Then lambda- and kappa-IgGs were separated by affinity chromatography of lambda+kappa-IgG_mix on anti- lambda-L-Sepharose (D). The preparation of lambda-IgGs purified on anti-lambda-L-Sepharose was rechromatographed on anti-kappa-L-Sepharose (E), while kappa-IgGs on anti-lambda-L-Sepharose (F). In all cases: (–), absorbance at 280 nm (A₂₈₀).</p

Affinity chromatography of non-modified and FITC-modified sIgA_mix on DNA-cellulose:

<p>(–) and (- - -), absorbance of sIgA_mix at 280 nm before and after modification of sIgAs with FITC, respectively. Analysis of a relative efficiency of specific-molecule exchange under different conditions between non-modified sIgA_mix and FITC-sIgA_mix having different affinity for DNA-cellulose; relative fluorescence (RF) is shown by the bars (B–D). Before chromatography, the sIgA_mix eluted from DNA-cellulose by 0.6 M NaCl (0.6M-IgG_mix, Panel A) were incubated for 24 h with FITC-IgA_mix eluted by 8 M urea (8M-FITC-IgA_mix, Panel A) in the presence of TBS and GSH (B), TBS + human milk plasma (C), and with this buffer containing both GSH and human milk plasma (D). See <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048756#s4" target="_blank">Materials and methods</a> for other details.</p

SDS-PAGE analysis of FITC-modified pIgG_mix formation.

<p>The analysis was performed after non-labeled pIgG_mix incubation with preparations of separated FITC-modified heavy (A, B) and light chains (C, D) of Abs. The relative fluorescence of proteins (A and C) and their position on the gel (B and D; Coomassie staining) were analyzed. Before electrophoresis, FITC-heavy-chains were incubated alone (lanes 1, A and B), in the presence of the IgG_mix and GSH (lanes 2, A and B) or in the presence of the IgG_mix, GSH and human milk plasma (lanes 3, A and B). Lane 4 (B) corresponds to human milk plasma incubated alone. FITC-L-chains were incubated alone (lanes 1, C and D), in the presence of the IgG_mix and GSH (lanes 2, C and D) or in the presence of the IgG_mix, GSH, and human milk plasma (lane 3 C and D). The arrows (lane 4, D) indicate the positions of molecular mass markers. For details, see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0042942#s4" target="_blank">Materials and methods</a>.</p

Affinity chromatography of non-modified and ³²P-labeled pIgGs on DNA-cellulose.

<p>(–) and (–), absorbance of IgGs at 280 nm before and after phosphorylation using γ-[³²P]ATP, respectively; the bars correspond to the relative radioactivity (RR) of [³²P]IgG fractions (A). Analysis of a relative efficiency of half-molecule exchange under different conditions between non-modified pIgGs and [³²P]pIgGs having different affinity for DNA-cellulose (B–E). Before chromatography, the IgG preparations eluted from DNA-cellulose by 0.15 M NaCl (0.15 M-IgG_mix) were incubated with [³²P]pIgG_mix eluted by 0.6 M NaCl (0.6 M-[³²P]pIgG_mix) in the presence of TBS and GSH (B) or in the presence of TBS and milk plasma containing no Abs (C); 0.15 M-IgG_mix and 0.6 M-[³²P]pIgG_mix (D) or 0.15 M-[³²P]pIgG_mix and 0.6 M-IgG_mix (E) were incubated in the presence of TBS containing GSH and human milk plasma.</p