Isolation and sequence determination of cDNA encoding P2 protein of human peripheral myelin

Hayasaka, Kiyoshi; Nanao, Kenji; Tahara, Marie; Sato, Wataru; Takada, Goro; Miura, Masayuki; Uyemura, Keiichi

doi:10.1016/s0006-291x(05)81402-0

Cited by 17 publications

(6 citation statements)

References 7 publications

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“…Interestingly, an immunohistochemical analysis of MDGI and H-FABP expression shows immunoreactivity exclusively in postmitotic, terminally differentiated cells of the myocard, skeletal muscle, and surface epithelial cells of intestinal and respiratory tracts (Zschiesche, W., A. Kleine, J. H. Veerkamp, and J. Glatz, manuscript submitted for publication). The developmental, cell and tissue specific expression of various other FABPs (14,15,28,30) indeed seems to support a more general role for these proteins in growth and differentiation similarly to that described here for MDGI.…”

Section: Discussionsupporting

confidence: 75%

Members of the fatty acid binding protein family are differentiation factors for the mammary gland.

Yang

Spitzer

Kenney

et al. 1994

The Journal of Cell Biology

103

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Abstract. Mammary gland development is controlled by systemic hormones and by growth factors that might complement or mediate hormonal action. Peptides that locally signal growth cessation and stimulate differentiation of the developing epithelium have not been described. Here, we report that recombinant and wild-type forms of mammary-derived growth inhibitor (MDGI) and heart-fatty acid binding protein (FABP), which belong to the FABP family, specifically inhibit growth of normal mouse mammary epithelial cells (MEC), while growth of stromal cells is not suppressed. In mammary gland organ culture, inhibition of ductal growth is associated with the appearance of bulbous alveolar end buds and formation of fully developed lobuloalveolar structures. In parallel, MDGI stimulates its own expression and promotes milk protein synthesis. Selective inhibition of endogenous MDGI expression in MEC by antisense phosphorothioate oligonucleotides suppresses appearance of alveolar end buds and lowers the ~-casein level in organ cultures. Furthermore, MDGI suppresses the mitogenic effects of epidermal growth factor, and epidermal growth factor antagonizes the activities of MDGI. Finally, the regulatory properties of MDGI can be fully mimicked by an l 1-amino acid sequence, represented in the COOH terminus of MDGI and a subfamily of structurally related FABPs. This peptide does not bind fatty acids. To our knowledge, this is the first report about a growth inhibitor promoting mammary gland differentiation.ROWTH development, and differentiation of epithelial tissues are multistage processes that are driven by a combination of paracrine and autocrine signaling factors and interactions of a cell with its extracellular matrix (reviewed in 51, 60, 62). In the mammary gland, these complex interactions are regulated by various steroid and peptide hormones (29,32,46,60). Development of the mouse mammary gland at puberty is characterized by sparsely branching ducts which invade the stroma, followed by the development of lobuloalveolar structures and functional differentiation, i.e., synthesis of milk constituents at pregnancy (1,17,32). By use of endocrine ablation (44), organ culture systems (1,35,54,65) and mammary cells (MEC) ~ growing on a

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Section: Discussionsupporting

confidence: 75%

Members of the fatty acid binding protein family are differentiation factors for the mammary gland.

Yang

Spitzer

Kenney

et al. 1994

The Journal of Cell Biology

103

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“…PMP2 is a peripheral myelin protein gene that encodes a small basic P2 protein. P2 is also called M-FABP/FABP8 and is a member of a family of fatty acid binding proteins with maximal specificity of expression in the peripheral myelin [ 11 – 13 ]. P2 enhances myelin membrane stability and lipid dynamics [ 14 ].…”

Section: Discussionmentioning

confidence: 99%

A Mutation in PMP2 Causes Dominant Demyelinating Charcot-Marie-Tooth Neuropathy

et al. 2016

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Charcot-Marie-Tooth disease (CMT) is a heterogeneous group of peripheral neuropathies with diverse genetic causes. In this study, we identified p.I43N mutation in PMP2 from a family exhibiting autosomal dominant demyelinating CMT neuropathy by whole exome sequencing and characterized the clinical features. The age at onset was the first to second decades and muscle atrophy started in the distal portion of the leg. Predominant fatty replacement in the anterior and lateral compartment was similar to that in CMT1A caused by PMP22 duplication. Sural nerve biopsy showed onion bulbs and degenerating fibers with various myelin abnormalities. The relevance of PMP2 mutation as a genetic cause of dominant CMT1 was assessed using transgenic mouse models. Transgenic mice expressing wild type or mutant (p.I43N) PMP2 exhibited abnormal motor function. Electrophysiological data revealed that both mice had reduced motor nerve conduction velocities (MNCV). Electron microscopy revealed that demyelinating fibers and internodal lengths were shortened in both transgenic mice. These data imply that overexpression of wild type as well as mutant PMP2 also causes the CMT1 phenotype, which has been documented in the PMP22. This report might expand the genetic and clinical features of CMT and a further mechanism study will enhance our understanding of PMP2-associated peripheral neuropathy.

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“…intestine [4], stomach [5] and kidney [6,7], supports this hypothesis. Since the first isolation of an FABP cDNA, the rat liver FABP cDNA [8], cDNAs of all five FABP types have been obtained [9][10][11][12][13][14][15][16].…”

Section: Methodsmentioning

confidence: 99%

Molecular identification of the liver- and the heart-type fatty acid-binding proteins in human and rat kidney. Use of the reverse transcriptase polymerase chain reaction

Maatman

Westerlo

Kuppevelt

et al. 1992

Biochemical Journal

129

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The cDNAs of two types of fatty acid-binding protein (FABP) present in human kidney, previously described as types A and B, were isolated using reverse transcriptase-PCR (RT-PCR) with human kidney mRNA and various sets of primers. The cDNA fragments were cloned and sequenced. Renal FABP type A and B cDNAs appeared to be completely identical to human liver- and heart-type FABP cDNAs respectively. In the second part of this study we demonstrated the presence of liver-type FABP in rat kidney by chromatography, e.l.i.s.a. and immunocytochemistry. The ratio and cellular distribution of the two FABP types varies markedly in human and rat kidney. Using RT-PCR we were also able to prepare and identify liver- and heart-type FABP cDNAs with mRNA from both male and female rat kidney.

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Isolation and sequence determination of cDNA encoding P2 protein of human peripheral myelin

Cited by 17 publications

References 7 publications

Members of the fatty acid binding protein family are differentiation factors for the mammary gland.

Members of the fatty acid binding protein family are differentiation factors for the mammary gland.

A Mutation in PMP2 Causes Dominant Demyelinating Charcot-Marie-Tooth Neuropathy

Molecular identification of the liver- and the heart-type fatty acid-binding proteins in human and rat kidney. Use of the reverse transcriptase polymerase chain reaction

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