The role of community review in evaluating the risks of human genetic variation research.

The practicality and moral value of community review of human genetic research has become a focus of debate. Examples from two Native American communities are used to address four aspects of that debate: (1) the value of community review in larger, geographically dispersed populations; (2) the identification of culturally specific risks; (3) the potential conflict between individual and group assessments of research-related risks; and (4) the confusion of social categories with biological categories. Our experiences working with these two communities suggest that: (1) successful community review may require the involvement of private social units (e.g., families); (2) culturally specific implications of genetic research may be identifiable only by community members and are of valid concern in their moral universes; (3) community concerns can be incorporated into existing review mechanisms without necessarily giving communities the power to veto research proposals; and (4) the conflation of social and biological categories presents recruitment problems for genetic studies. These conclusions argue for the use of community review to identify and minimize research-related risks posed by genetic studies. Community review also can assist in facilitating participant recruitment and retention, as well as in developing partnerships between researchers and communities.     

Expression of a Gene Specific for Iron Deficiency (Ids3) in the Roots of Hordeum vulgare

To clone genes required for the synthesis of mugineic acid (MA)or for the transport of Fe(III)-MA, a     

Human naive epiblast cells possess unrestricted lineage potential

1. Download : Download high-res image (172KB)
2. Download : Download full-size image

     

The complete amino acid sequence of α-neo-endorphin

After re-purification by reverse phase high performance liquid chromatography, α-neo-endorphin was submitted to structural analyses, performed by dansyl-Edman degradation, as well as by C-terminal analysis by ³H-labeling. The full sequence of α-neo-endorphin has been determined to be : Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys, in which the 8th residue previously reported as Arg is found to be Tyr. A synthetic decapeptide with the above sequence was verified to be identical with natural α-neo-endorphin. For further structural confirmation, tryptic and chymotryptic peptides were also identified. Thus, the complete sequence of α-neo-endorphin has been definitely established. Its potent opioid activity in the guinea-pig ileum assay is also discussed.     

Membrane Tension Gates ERK-Mediated Regulation of Pluripotent Cell Fate

1. Download : Download high-res image (121KB)
2. Download : Download full-size image

     

Unexpected racemization of proline or hydroxy-proline phenacyl ester during coupling reactions with Boc-amino acids.

When L-proline or O-benzyl-trans-4-hydroxy-L-proline phenacyl ester was coupled with Boc-amino acids in dimethylformamide using water-soluble carbodiimide (WSCI) in the presence of anhydrous 1-hydroxybenzotriazole (HOBt) as coupling reagents, extensive racemization was observed at the C alpha of the proline or hydroxy-proline residue. The extent of racemization was measured by HPLC after the coupling with Boc-L-Leu-OH in the presence or absence of HOBt. The extent of racemization increased when HOBt was added to the reaction mixture, but greatly decreased when it was not, indicating that HOBt was needed for inducing racemization. Almost no racemization was observed when the coupling reaction was carried out by the mixed anhydride procedure in tetrahydrofuran or by the carbodiimide method in dichloromethane without using HOBt. In the case of coupling reactions with ordinary L-amino acid phenacyl esters, no racemization was observed. Examination of some model systems yielded sufficient evidence to prove that HOBt is an efficient catalyst for racemizing proline or hydroxy-proline phenacyl ester not only in the stage of cyclic intermediate formation but also in the opening of the ring structure. Thus, the racemization reaction was found to be closely related to the formation of the cyclic carbinol-amine derivative.