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Literature DB >> 9030206

Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain.

S Maekawa¹, H Kumanogoh, N Funatsu, N Takei, K Inoue, Y Endo, K Hamada, Y Sokawa.

Abstract

NAP-22 is a membrane-localized brain enriched acidic protein having a Ca(2+)-dependent calmodulin binding activity. Further fractionation of the NAP-22 containing membrane showed the localization of NAP-22 in a Triton insoluble fraction of low density. Besides NAP-22, this fraction was found to contain GAP-43 (neuromodulin), trimeric G proteins, and some GPI-anchored proteins such as Thy-1 and N-CAM-120. Presence of some protein tyrosine kinases, such as src and fyn, was also shown.

Entities: Chemical Gene Species

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Year: 1997 PMID： 9030206 DOI： 10.1016/s0005-2736(96)00222-2

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

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Cited

6 in total

1. Local accumulations of B-50/GAP-43 evoke excessive bleb formation in PC12 cells.

Authors: L H Aarts; P Verkade; L H Schrama; A B Oestreicher; W H Gispen; P Schotman
Journal: Mol Neurobiol Date: 1999-08 Impact factor: 5.590

2. Myelin protein zero is one of the components of the detergent-resistant membrane microdomain fraction prepared from rat pituitary.

Authors: Katsutoshi Taguchi; Haruko Kumanogoh; Shun Nakamura; Seiji Miyata; Shohei Maekawa
Journal: J Mol Histol Date: 2007-02-21 Impact factor: 2.611

3. Morphological analysis on the distribution of membrane lipids and a membrane protein, NAP-22, during neuronal development in vitro.

Authors: Ryoko Tsuda; Haruko Kumanogoh; Masato Umeda; Shohei Maekawa
Journal: J Mol Histol Date: 2008-06-03 Impact factor: 2.611

Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain.

1. Local accumulations of B-50/GAP-43 evoke excessive bleb formation in PC12 cells.

2. Myelin protein zero is one of the components of the detergent-resistant membrane microdomain fraction prepared from rat pituitary.

3. Morphological analysis on the distribution of membrane lipids and a membrane protein, NAP-22, during neuronal development in vitro.

Review 4. Functional roles of glycosphingolipids in signal transduction via lipid rafts.

5. Association of membrane rafts and postsynaptic density: proteomics, biochemical, and ultrastructural analyses.

Review 6. A Unique Family of Neuronal Signaling Proteins Implicated in Oncogenesis and Tumor Suppression.