Literature DB >> 2422074

Synthesis of plasma proteins in fetal, adult, and neoplastic human brain tissue.

K M Dziegielewska, N R Saunders, E J Schejter, H Zakut, D Zevin-Sonkin, R Zisling, H Soreq.   

Abstract

The synthesis of plasma proteins directed by mRNA from human brain tissues was studied by combining in vitro or in ovo translation of mRNAs with crossed immunoelectrophoresis of the mRNA-directed labeled polypeptides, followed by autoradiography of the washed plates. Poly(A)-containing mRNA was prepared from different developmental stages of fetal and postnatal human brain and also from primary glioblastomas and meningiomas. Several plasma protein-like polypeptides were identified in the autoradiographs by their migration coordinates in the two-dimensional gels, compared with immunoprecipitates formed by mature, unlabeled, stainable proteins. These included polypeptides migrating like Gc globulin, haptoglobin, fibrinogen, alpha-fetoprotein, transferrin, cholinesterase, and alpha 2-macroglobulin; other, yet unidentified plasma proteins, were also observed. In general, the synthesis of these plasma proteins appeared to be more pronounced in fetal and neoplastic brain tissues than in postnatal tissues. However, clear immunoprecipitates for some of these plasma proteins could also be detected in products directed by mRNA from particular regions of mature, normal brains, indicating that some synthesis of plasma proteins takes place in the human brain even as late as 40 years of age. mRNAs for several proteins were also identified in samples of neoplastic brain. mRNA for transferrin was identified in normal fetal and adult brain but not in either the glioblastomas or meningiomas studied. Microinjected Xenopus oocytes, in which post-translational processing occurs as well, were also used to translate fetal brain mRNA. Several plasma proteins could be detected in the translation products which were induced and stored in the oocytes. These included hemopexin, which could not be detected in the in vitro system. Others, such as cholinesterase, were found to be secreted by the oocytes. These findings indicate that different cell types in the human brain may produce and either store or secrete particular plasma proteins at defined stages in their development.

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Year:  1986        PMID: 2422074     DOI: 10.1016/0012-1606(86)90231-9

Source DB:  PubMed          Journal:  Dev Biol        ISSN: 0012-1606            Impact factor:   3.582


  14 in total

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5.  The use of mRNA translation in vitro and in ovo followed by crossed immunoelectrophoretic autoradiography to study the biosynthesis of human cholinesterases.

Authors:  H Soreq; K M Dziegielewska; D Zevin-Sonkin; H Zakut
Journal:  Cell Mol Neurobiol       Date:  1986-09       Impact factor: 5.046

6.  Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues.

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Journal:  Proc Natl Acad Sci U S A       Date:  1987-06       Impact factor: 11.205

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