Characterization of rat brain NCAM mRNA using DNA oligonucleotide probes

Andersson, Anna‐Maria; Gaardsvoll, Henrik; Giladi, Eliezer; Dahl, Britta Mynster; Bock, Elisabeth

doi:10.1016/0014-5793(90)81420-s

Cited by 18 publications

(13 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is possibly due to a very low turnover of this polypeptide in BT4C cells or, alternatively, due to a higher sensitivity of the blotting technique. In some Northern blots we observed a low amount of the 7.4-kb NCAM mRNA, which encodes the 190,000 (NCAM-A) polypeptide (Barthels et al, 1988;Anderson et al, 1990). There have been doubts whether astroglial cells produce the 190,000 (NCAM-A) form or not.…”

Section: Discussionmentioning

confidence: 88%

Characterization of NCAM expression and function in BT4C and BT4C_n glioma cells

Andersson

Moran

Gaardsvoll

et al. 1991

Intl Journal of Cancer

View full text Add to dashboard Cite

The neural cell adhesion molecule, NCAM, plays an important role in cell-cell adhesion. Therefore, we have studied NCAM expression in the glioma cell lines BT4C and BT4Cn. We demonstrate that the 2 cell lines differ in their metastatic ability; while BT4C cells have a very low capacity for producing experimental metastases, that of BT4Cn cells is high. In BT4C cells NCAM is synthesized as 4 polypeptides with Mr's of 190,000, 140,000, 115,000 and 97,000. The 140,000, 115,000 and 97,000 polypeptides are glycosylated and for the 140,000 and 115,000 polypeptides sulfatation is observed. Conversely, no NCAM protein synthesis is observed in BT4Cn cells, even though NCAM mRNA is expressed. Thus, development of an increased metastatic capacity is accompanied by the disappearance of NCAM protein expression in this model system. The functional importance of NCAM expression was studied by a cell-substratum binding assay in which the binding of BT4C and BT4Cn cells to NCAM immobilized to glass was assessed. We found that BT4C cells adhere specifically to NCAM, and that adhesion is inhibited by anti-NCAM Fab'-fragments, while no specific binding of BT4Cn cells to NCAM was observed. The BT4C and BT4Cn cell lines thus constitute an important new model system for the study of tumor invasion and metastasis and of the role of cell adhesion molecules in these processes.

show abstract

Section: Discussionmentioning

confidence: 88%

Characterization of NCAM expression and function in BT4C and BT4C_n glioma cells

Andersson

Moran

Gaardsvoll

et al. 1991

Intl Journal of Cancer

View full text Add to dashboard Cite

show abstract

“…Hence, a direct action of PIPLC may be prevented by steric hindrance, e.g., due to clustering of GPI-linked molecules at the prostasome membrane surface, or their sequestration in invaginated membrane regions [24], or their modification through acylation of an inositol hydroxy-group by a fatty acid as has been reported for the ectoenzyme acetylcholinesterase of human erythrocytes [25]. Another possibility might be that the prostasome membrane-associated protein exists in two forms, one is GPI-anchored and the other is not as demonstrated for neural cell adhesion molecule [26] and the IgG receptor, F, , RIII (CD16) [27]. It has been reported that GPI-anchored proteins are poorly solubilized by nonionic detergents like Triton X-100 [8,28].…”

Section: Discussionmentioning

confidence: 99%

Association of some hydrolytic enzymes with the prostasome membrane and their differential responses to detergent and PIPLC treatment

Fabiani¹,

Ronquist²

1995

The Prostate

View full text Add to dashboard Cite

Prostasomes are human prostate derived organelles that were isolated from both prostatic fluid and seminal plasma for the present study. Specific activities were determined for prostasome membrane-associated enzymes, alkaline phosphatase (ALP), 5'-nucleotidase (5'NT), and alkaline phosphodiesterase I (APD). The mode of their membranous anchoring was studied by treatment of prostasomes with phosphoinositol-specific phospholipase C (PIPLC) and different detergents. A substantial amount of ALP (50%) and 5'NT (31%) was released by incubation of prostasomes with 2 U/ml of PIPLC contrary to the small amount of APD (12%) released by the same treatment. After PIPLC treatment, the enzymes were recovered in the aqueous phase after phase repartition in Triton X-114 indicating that PIPLC removed the hydrophobic domain converting the enzymes from membrane-linked to aqueous soluble forms. Octyl glycoside was the most efficient one among different detergents to solubilize the enzymes from the prostasome membrane. Both ALP and 5'NT were resistant to the treatment with Triton X-100 and Triton X-114. These results suggest that ALP, 5'NT, and APD are more or less extensively linked to the prostasome membrane via a glycophosphoinositide anchor.

show abstract

“…ST8Sia II, and NCAM in postnatal rat brain development Northern blot analysis was carried out with poly (A) + RNA isolated from whole brains of postnatal rats at the age of 2 days [postnatal day (P) 2], P21, and 6 months. The NCAM probe developed the known hybridization pattern with bands of 7.4, 6.7, 5.2, and 2.9 kb (Andersson et al, 1990;Linnemann et al, 1993) (Fig. 1).…”

Section: Changes In Expression Level Of St8sia IVmentioning

confidence: 99%

Heterogeneous Expression of the Polysialyltransferases ST8Sia II and ST8Sia IV During Postnatal Rat Brain Development

Hildebrandt

Becker

Mürau

et al. 1998

Journal of Neurochemistry

100

View full text Add to dashboard Cite

Polysialic acid on the neural cell adhesion molecule is developmentally regulated and has been implicated in the plasticity of cell‐cell interactions. The sialyltransferases ST8Sia II and ST8Sia IV are able to catalyze the synthesis of polysialic acid. This study compares the expression of ST8Sia II and ST8Sia IV mRNA during postnatal rat brain development. Northern blot analysis indicated a substantial down‐regulation of ST8Sia II from high expression at postnatal day 2 to almost undetectable levels at the age of 6 months. In contrast, the decline of ST8Sia IV content was moderate. In the mature brain, ST8Sia IV is the predominant polysialyltransferase. In situ hybridization of selected brain regions at postnatal days 2, 11, and 21 confirmed the decline of ST8Sia II level in isocortex, hippocampus, and cerebellum. ST8Sia II was not detectable at any time point in the subependymal layer and the layers of the olfactory bulb. Persistent ST8Sia IV expression was localized in the subependymal layer, the glomerular layer of the olfactory bulb, and the granule cell layer of the dentate gyrus and in some widely dispersed cells of the isocortex. The distinct expression patterns of ST8Sia II and ST8Sia IV suggest their differential regulation. As discussed with regard to the persistent polysialic acid expression, ST8Sia IV should receive particular attention in the mature brain.

show abstract

Characterization of rat brain NCAM mRNA using DNA oligonucleotide probes

Cited by 18 publications

References 19 publications

Characterization of NCAM expression and function in BT4C and BT4C_n glioma cells

Characterization of NCAM expression and function in BT4C and BT4C_n glioma cells

Association of some hydrolytic enzymes with the prostasome membrane and their differential responses to detergent and PIPLC treatment

Heterogeneous Expression of the Polysialyltransferases ST8Sia II and ST8Sia IV During Postnatal Rat Brain Development

Contact Info

Product

Resources

About

Characterization of rat brain NCAM mRNA using DNA oligonucleotide probes

Cited by 18 publications

References 19 publications

Characterization of NCAM expression and function in BT4C and BT4Cn glioma cells

Characterization of NCAM expression and function in BT4C and BT4Cn glioma cells

Association of some hydrolytic enzymes with the prostasome membrane and their differential responses to detergent and PIPLC treatment

Heterogeneous Expression of the Polysialyltransferases ST8Sia II and ST8Sia IV During Postnatal Rat Brain Development

Contact Info

Product

Resources

About

Characterization of NCAM expression and function in BT4C and BT4C_n glioma cells

Characterization of NCAM expression and function in BT4C and BT4C_n glioma cells