Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027819 (neuroblastoma)
27,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Plasmolipin is an hydrophobic plasma membrane proteolipid present in both kidney and brain. The protein consists of two subunits of 17-18.5 kD, which together form K+ selective voltage-dependent channels. In this report, we define the embryonic and postnatal expression of plasmolipin in the developing rat brain. Plasmolipin was found to be essentially restricted to the postnatal period increasing eight-fold between the first to fourth week after birth. A fetal plasmolipin immunoreactive protein (FPIP) was identified in embryonic brain and also during the early postnatal development of the cerebellum. The expression of FPIP was biphasic with an initial transient increase between E15-E20 followed by a decrease in its levels. FPIP was not detected in the developed rat CNS. FPIP was found in a variety of dividing and immature cells including cultured astrocytes and embryonic neurons, neuroblastoma cells, and rat thymus. In contrast, plasmolipin was restricted to oligodendrocytes of the neural cells tested and to renal tubular epithelial cells.
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PMID:Expression of plasmolipin in the developing rat brain. 153 79

We have examined the regulation of plasma membrane proteolipid (PM-PLP) synthesis and steady-state levels in mouse NB2a/d1 neuroblastoma cells during differentiation with dibutyryl cyclic AMP (dbcAMP) and retinoic acid (RA), agents which have been previously shown to induce the elaboration of exclusively axonal or dendritic neurites, respectively. We report that a PM-PLP-immunoreactive species is expressed by this neuroblastoma cell line, and that its expression is regulated by specific states of differentiation. Differentiation of cells with dbcAMP was accompanied by an initial 2-fold increase in this PM-PLP immunoreactive species at 24 h after treatment, which returned to control levels by 96 h after treatment. By contrast, no significant increase in synthesis was detected when cells were treated with RA. Protein blot analysis of PM-PLP in dbcAMP-treated cells indicated that there was little change in its steady-state level until 96 h following treatment, at which time a reduction of 40% was observed. Throughout induced differentiation with dbcAMP, NB2a/d1 cells continued to express a PM-PLP-immunoreactive species which comigrated on immunoblot analysis with PM-PLP form characteristic of embryonic brain (14-16 kDa), and apparently did not express the PM-PLP form characteristic of adult brain (18 kDa).
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PMID:Expression of the plasma membrane proteolipid in mouse neuroblastoma cells: transient increase in synthesis during differentiation with N6,O2-dibutyryl adenosine 3',5'-cyclic monophosphate. 255 Feb 93