Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Experimentally delayed mouse blastocysts were activated to implant by exogenous estradiol and after varying duration of estrogen influence, the blastocysts were flushed out from the uterine horns. Then they were incubated in the cold with different, 125I-conjugated proteins and the amount of protein bound to the blastocysts was determined by radioassay. Three radiolabelled proteins: human serum albumin (125I-HSA), human serum transferrin (125I-HST) and normal rabbit IgG (125I-RIgG) were tested and it was found that the uptake of each protein markedly increased between 14 and 24 hours of estrogen-activation. It was possible to partially block the binding of 125I-HSA and 125I-RIgG with the respective unlabelled protein. Unlabelled RIgG could also partially block the uptake of 125I-HSA whereas HSA did not impede the binding of 125I-RIgG. During delay of implantation the protein binding was low and approximately the same as after 14 hours of activation. However, at 18 and 24 hours of activation protein uptake increased gradually. Raising the incubation temperature from 0 to 37 degrees C did not significantly influence the protein binding capacity of the 24-hour-activated blastocyts. Whole blastocyst autoradiography indicated that the labelled protein was heavily bound in patches, preferentially located in the abembryonic half of the postattachment blastocysts. It is assumed that the binding of protein to abembryonic trophoblast cells of the implanting blastocyst can be attributed to the presence of protein receptors on the surface of these cells.
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PMID:Binding of proteins to mouse blastocysts after the attachment stage of implantation. 101 63

Almost a quarter of a century ago, the banding patterns of human and other higher primate chromosomes were compared, creating a barrage of speculation. Consequently, a number of approaches have been used to understand human descent. Chromosome modifications are believed to be important in the origin of species, and pericentric inversions account for the majority of evolutionary chromosomal alterations seen in Hominoidea. A comparative mapping fluorescence in situ hybridization technique, using locus-specific DNA probes as phylogenotic markers, was used to decipher the pericentric inversions of human chromosomes 11 and 12. Human-derived (Homo sapiens, HSA) DNA probes for GLI, HST and INT2 protooncogenes were used to identify their homologous locations in the chromosomes of chimpanzee (Pan troglodytes, PTR), gorilla (Gorilla gorilla, GGO) and orangutan (Pongo pygmaeus, PPY). The INT2 and HST loci mapping results confirm the earlier putative claim that a pericentric inversion took place in HSA chromosome 11 and its equivalent PTR and GGO chromosomes. In addition, these data provide additional information regarding the orangutan's position on the evolutionary tree of Pongidae and Hominidae. GLI mapping reveals that a pericentric inversion occurred in the HSA chromosome 12 equivalent in PTR and GGO, but was not seen in HSA or PPY. These pericentric inversions in PTR and GGO may have occurred at a period when both PTR and GGO had branched off from the Hominoidae trunk. The use of loci-specific probes to decipher pericentric inversions has proved to be a formidable approach in characterizing chromosome rearrangements and providing further evidence on human descent.
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PMID:Evolutionary divergence of the oncogenes GLI, HST and INT2. 972 Mar