Thrombomodulin (TM) is an endothelial anticoagulant cofactor that promotes thrombin-mediated formation of activated protein C (APC). We have found that the N-terminal lectin-like domain (D1) of TM has unique antiinflammatory properties. TM, via D1, binds high-mobility group-B1 DNA-binding protein (HMGB1), a factor closely associated with necrotic cell damage following its release from the nucleus, thereby preventing in vitro leukocyte activation, in vivo UV irradiation-induced cutaneous inflammation, and in vivo lipopolysaccharide-induced lethality. Our data also demonstrate antiinflammatory properties of a peptide spanning D1 of TM and suggest its therapeutic potential. These findings highlight a novel mechanism, i.e., sequestration of mediators, through which an endothelial cofactor, TM, suppresses inflammation quite distinctly from its anticoagulant cofactor activity, thereby preventing the interaction of these mediators with cell surface receptors on effector cells in the vasculature.

Thrombomodulin (TM) is an endothelial anticoagulant cofactor that promotes thrombin-mediated formation of activated protein C (APC). We have found that the N-terminal lectin-like domain (D1) of TM has unique antiinflammatory properties. TM, via D1, binds high-mobility group-B1 DNA-binding protein (HMGB1), a factor closely associated with necrotic cell damage following its release from the nucleus, thereby preventing in vitro leukocyte activation, in vivo UV irradiation-induced cutaneous inflammation, and in vivo lipopolysaccharide-induced lethality. Our data also demonstrate antiinflammatory properties of a peptide spanning D1 of TM and suggest its therapeutic potential. These findings highlight a novel mechanism, i.e., sequestration of mediators, through which an endothelial cofactor, TM, suppresses inflammation quite distinctly from its anticoagulant cofactor activity, thereby preventing the interaction of these mediators with cell surface receptors on effector cells in the vasculature.

Cereal Chem. 81(4):515-520The molecular structure and pasting properties of starches from eight buckwheat cultivars were examined. Rapid viscograms showed that buckwheat starches had similar pasting properties among cultivars. The actual amylose content was 16-18%, which was lower than the apparent amylose content (26-27%), due to the high iodine affinity (IA) of amylopectin (2.21-2.48 g/100 g). Amylopectins resembled each other in average chain-length (23-24) and chain-length distributions. The long-chains fraction (LC) was abundant (12-13% by weight) in all the amylopectins, which was consistent with high IA values. The amyloses were also similar among the cultivars in numberaverage DP 1,020-1,380 with 3.1-4.3 chains per molecule. The molar-based distribution indicated that all the amyloses comprised two molecular species differing in molecular size, although the weight-based distribution showed a single species. A comparison of molecular structures of buckwheat starches to cereal starches indicated buckwheat amylopectins had a larger amount of LC, and their distributions of amylose and short chains of amylopectin on molar basis were similar to those of wheat and barley starches.

The molecular structure and some physicochemical properties of starches from two high‐amylose cultivars of barley, high‐amylose Glacier A (HAG‐A) and N (HAG‐N), were examined and compared with those of a normal cultivar, Normal Glacier (NG). The true amylose contents of HAG‐A, HAG‐N, and NG were 41.0, 33.4, and 23.0%, respectively. Iodine affinities before and after defatting of starch, and thermograms of differential scanning calorimetry, indicated that HAG‐A and HAG‐N starches had a higher proportion of amylose‐lipid complex than did NG starch. The amylopectins from HAG‐A and HAG‐N were similar to NG amylopectin in average chain length (18–19), β‐amylolysis limit (β‐AL 56–57%), number‐average degrees of polymerization (DPn 6,000–7,500) and chain length distribution. Very long chains (1–2%) were found in amylopectins from all cultivars. HAG‐A amylopectin had a larger amount of phosphorus (214 ppm) than the others. The amyloses from HAG‐A and HAG‐N resembled NG amylose in DPn (950–1,080) and β‐AL (70–74%). However, HAG‐A and HAG‐N had a larger number of chains per molecule (NC 2.4–2.7) than NG amylose (1.8) and contained the branched amylose with a higher NC (9.5–10.6) than that of NG amylose (5.8), although molar fractions of the branched amylose (15–20%) were similar.

The nature and enzymic properties of starch-branching enzyme (SBE) are two of the dominant factors influencing the fine structure of starch. To understand the role of this enzyme's activity in the formation of starch in kidney bean (Phaseolus ulgaris L.), a study was undertaken to identify the major SBE sequences expressed during seed development and to characterize the enzymic properties of the coded recombinant enzymes. Two SBE cDNA species (designated p sbe2 and p sbe1) that displayed significant similarity (more than 70 %) to other family A and B SBEs respectively were isolated. Northern blot analysis revealed that p sbe1 and p sbe2 were differentially expressed during seed development. p sbe2 showed maximum steady-state transcript levels at the mid-stage of seed maturation, whereas p sbe1 reached peak levels at a later stage. Western blot analysis with antisera raised against both recombinant proteins (rPvSBE1 and rPvSBE2) showed that these two SBEs were located in different