Literature DB >> 2121273

Functional changes in cation-preferring amino acid transport during development of preimplantation mouse conceptuses.

L J Van Winkle1, A L Campione.   

Abstract

In a previous study, a Na(+)-independent, cation-preferring amino acid transport system was detected in preimplantation mouse blastocysts. The system resisted Na(+)-dependent inhibition by homoserine and so resembled the lysosomal system c more than it resembled the plasmalemmal system y+. We now report the presence of a cation-preferring system in unfertilized and fertilized eggs and cleavage-state conceptuses which also resists Na(+)-dependent inhibition by homoserine. The systems in 1-cell conceptuses and blastocysts are, however, insensitive to changes in pH in the interval of 6.0 to 8.0 and, thus, different from the pH-sensitive system c. Moreover, the relative strengths of the interactions of a variety of basic amino acids with the systems in conceptuses do not correspond well with the relative strengths of their interactions with either system c or system y+. Similarly, the system in 1-cell conceptuses can be distinguished from the system in blastocysts because L-arginine interacts about equally well with each of these systems, whereas the system in 1-cell conceptuses is inhibited more strongly than the system in blastocysts by most other basic amino acids. In addition, inhibition of the system in 1-cell conceptuses by some basic amino acids is Na(+)-stimulated, whereas Na+ does not affect inhibition of the system in blastocysts. Finally, L-tryptophan inhibits the system in blastocysts better than L-histidine or D-arginine do, but the reverse is true for the system in 1-cell conceptuses. Therefore, the relative activities of at least two forms of a novel, cation preferring amino acid transport process change during development of blastocysts from fertilized eggs. For convenience, the forms of the cation-preferring transport processes that seem to predominate at the 1-cell and blastocysts stages are provisionally designated systems b+1 and b+2, respectively, although these two systems need not represent entirely different gene products.

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Year:  1990        PMID: 2121273     DOI: 10.1016/0005-2736(90)90151-d

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  CATs, a family of three distinct mammalian cationic amino acid transporters.

Authors:  E I Closs
Journal:  Amino Acids       Date:  1996-06       Impact factor: 3.520

2.  L-Arginine currents in rat cardiac ventricular myocytes.

Authors:  R Daniel Peluffo
Journal:  J Physiol       Date:  2007-02-15       Impact factor: 5.182

3.  Amino Acid transport mechanisms in mouse oocytes during growth and meiotic maturation.

Authors:  Amélie M D Pelland; Hannah E Corbett; Jay M Baltz
Journal:  Biol Reprod       Date:  2009-07-15       Impact factor: 4.285

4.  The glycine neurotransmitter transporter GLYT1 is an organic osmolyte transporter regulating cell volume in cleavage-stage embryos.

Authors:  Candace L Steeves; Mary-Anne Hammer; Glenn B Walker; Duncan Rae; Nicolas A Stewart; Jay M Baltz
Journal:  Proc Natl Acad Sci U S A       Date:  2003-11-13       Impact factor: 11.205

Review 5.  Amino Acid Transport and Metabolism Regulate Early Embryo Development: Species Differences, Clinical Significance, and Evolutionary Implications.

Authors:  Lon J Van Winkle
Journal:  Cells       Date:  2021-11-13       Impact factor: 6.600

  5 in total

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