Secondary forest fragments offer important carbon and biodiversity cobenefits.

Tropical forests store large amounts of carbon and high biodiversity, but are being degraded at alarming rates. The emerging global Forest and Landscape Restoration (FLR) agenda seeks to limit global climate change by removing carbon dioxide from the atmosphere through the growth of trees. In doing so, it may also protect biodiversity as a free cobenefit, which is vital given the massive shortfall in funding for biodiversity conservation. We investigated whether natural forest regeneration on abandoned pastureland offers such cobenefits, focusing for the first time on the recovery of taxonomic diversity (TD), phylogenetic diversity (PD) and functional diversity (FD) of trees, including the recovery of threatened and endemic species richness, within isolated secondary forest (SF) fragments. We focused on the globally threatened Brazilian Atlantic Forest, where commitments have been made to restore 1 million hectares under FLR. Three decades after land abandonment, regenerating forests had recovered ~20% (72 Mg/ha) of the above-ground carbon stocks of a primary forest (PF), with cattle pasture containing just 3% of stocks relative to PFs. Over this period, SF recovered ~76% of TD, 84% of PD and 96% of FD found within PFs. In addition, SFs had on average recovered 65% of threatened and ~30% of endemic species richness of primary Atlantic forest. Finally, we find positive relationships between carbon stock and tree diversity recovery. Our results emphasize that SF fragments offer cobenefits under FLR and other carbon-based payments for ecosystem service schemes (e.g. carbon enhancements under REDD+). They also indicate that even isolated patches of SF could help to mitigate climate change and the biodiversity extinction crisis by recovering species of high conservation concern and improving landscape connectivity.

Productive performance of Holstein calves finished in feedlot or pasture

ABSTRACT The use of animals from dairy farms is an alternative to meat production since it provides an increment of total income for farmers. This study aims to evaluate the performance of Holstein calves finished in two feeding systems (feedlot or pasture). Forty-three animals with 58 days old and 57 kg were divided in two treatments: 23 animals finished in feedlot with corn silage plus concentrate based on corn and soybean meal (40:60); 20 animals kept in cultivated pastures according to the period of the year: Italian ryegrass (Lolium multiflorum) and pearl millet (Pennisetum americanum) with supplementation with the same feedlot-concentrate at 1% body weight. Animals were slaughtered with 200 kg. Dry matter and nutrient intake were determined, with the use of chromium oxide for estimating pasture intake. Feedlot animals had greater total intake and total digestible nutrients, resulting in higher average daily gain (0.949 vs 0.694 kg day-1). Crude protein intake, neutral detergent fiber and feed conversion did not show significant differences. Holstein calves have improved performance when finished in feedlot.

Productive performance of Holstein calves finished in feedlot or pasture.

The use of animals from dairy farms is an alternative to meat production since it provides an increment of total income for farmers. This study aims to evaluate the performance of Holstein calves finished in two feeding systems (feedlot or pasture). Forty-three animals with 58 days old and 57 kg were divided in two treatments: 23 animals finished in feedlot with corn silage plus concentrate based on corn and soybean meal (40:60); 20 animals kept in cultivated pastures according to the period of the year: Italian ryegrass (Lolium multiflorum) and pearl millet (Pennisetum americanum) with supplementation with the same feedlot-concentrate at 1% body weight. Animals were slaughtered with 200 kg. Dry matter and nutrient intake were determined, with the use of chromium oxide for estimating pasture intake. Feedlot animals had greater total intake and total digestible nutrients, resulting in higher average daily gain (0.949 vs 0.694 kg day-1). Crude protein intake, neutral detergent fiber and feed conversion did not show significant differences. Holstein calves have improved performance when finished in feedlot.

Pkd1 haploinsufficiency increases renal damage and induces microcyst formation following ischemia/reperfusion.

Mutations in PKD1 cause the majority of cases of autosomal dominant polycystic kidney disease (ADPKD). Because polycystin 1 modulates cell proliferation, cell differentiation, and apoptosis, its lower biologic activity observed in ADPKD might influence the degree of injury after renal ischemia/reperfusion. We induced renal ischemia/reperfusion in 10- to 12-wk-old male noncystic Pkd1(+/-) and wild-type mice. Compared with wild-type mice, heterozygous mice had higher fractional excretions of sodium and potassium and higher serum creatinine after 48 h. In addition, in heterozygous mice, also cortical damage, rates of apoptosis, and inflammatory infiltration into the interstitium at time points out to 14 d after injury all increased, as well as cell proliferation at 48 h and 7 d. The mRNA and protein expression of p21 was lower in heterozygous mice than wild-type mice at 48 h. After 6 wk, we observed dilated tubules, microcysts, and increased renal fibrosis in heterozygotes. The early mortality of heterozygotes was significantly higher than that of wild-type mice when we extended the duration of ischemia from 32 to 35 min. In conclusion, ischemia/reperfusion induces a more severe injury in kidneys of Pkd1-haploinsufficient mice, a process that apparently depends on a relative deficiency of p21 activity, tubular dilation, and microcyst formation. These data suggest the possibility that humans with ADPKD from PKD1 mutations may be at greater risk for damage from renal ischemia/reperfusion injury.

Polyductin, the PKHD1 gene product, comprises isoforms expressed in plasma membrane, primary cilium, and cytoplasm.

BACKGROUND: PKHD1, the autosomal-recessive polycystic kidney disease (ARPKD) gene, encodes multiple alternatively spliced transcripts predicted to generate membrane-bound and secreted proteins. The longest open reading frame encodes polyductin (fibrocystin), a putative 4074 amino acid protein with a single transmembrane domain and an intracellular C-terminus. METHODS: To characterize the PKHD1 products and their expression profile, we raised polyclonal antibodies against different portions of polyductin and analyzed different organs using various methods. RESULTS: Western blot analyses demonstrated specific bands of >440 kD in human adult kidney, liver, and pancreas and approximately 230 kD in kidney and liver, predominantly observed in membrane fractions. The >440-kD putative membrane protein was immunoprecipitated from kidney and subsequently detected by Western blotting using two distinct antisera. An additional product of approximately 140 kD was specifically recognized by affinity-purified antisera predominantly in soluble fractions. Immunohistochemistry studies revealed specific staining in cortical and medullary collecting ducts and thick ascending limbs of Henle (TALH). Serial sections were stained with antibodies against aquaporin-2 and Tamm-Horsfall protein to confirm the nephron segment localization. Positive staining was also detected in biliary and pancreatic duct epithelia. Analyses of mouse developing tissues showed specific staining in the ureteric bud branches, intra- and extrahepatic biliary ducts, pancreatic ducts, and salivary glands. Immunofluorescence studies in inner medullary collecting duct cultured cells and immunoelectron microscopy analysis of medullary collecting ducts demonstrated that the protein localizes to the primary cilium. Positive signal was also detected in the apical membrane and in cytoplasm. CONCLUSION: The results indicate that polyductin is part of the group of polycystic kidney disease (PKD)-related proteins expressed in primary apical cilia. Our data also suggest that, in addition to its likely involvement in cilia function, polyductin probably serves in other subcellular functional roles. The detection of three different products using two antisera, with evidence for distinct subcellular localizations, suggests that PKHD1 encodes membrane-bound and soluble isoforms.