Isolation of cDNA clones encoding RICH: a protein induced during goldfish optic nerve regeneration with homology to mammalian 2',3'-cyclic-nucleotide 3'-phosphodiesterases.

Ballestero, Rafael P.; Wilmot, George; Leski, Michael; Uhler, Michael D.; Agranoff, Bernard W.

doi:10.1073/pnas.92.19.8621

Cited by 24 publications

(30 citation statements)

References 36 publications

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“…Nevertheless, a CNPase analog has been cloned from the goldfish retina (Ballestero et al 1995). Expression of this protein was upregulated in regenerating retinal ganglion cells after optic nerve injury, and hence, it was called RICH (for regeneration-induced CNPase homolog).…”

Section: Cnpasementioning

confidence: 99%

Features and Functions of Oligodendrocytes and Myelin Proteins of Lower Vertebrate Species

2008

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The myelin-forming cells in the central nervous system (CNS) of lower vertebrate species, in particular those of fish, profoundly differ from their mammalian counterparts in their biochemical phenotype in that they express Po-like glycoproteins as major myelin protein constituents instead of proteolipid protein, while in their overall cellular structure and their cell lineage relationships, they closely resemble mammalian oligodendrocytes. While molecular biology in the past has allowed to appropriately classify the major myelin proteins synthesized by fish oligodendrocytes, heterologous expression studies are expected to give a deeper insight into the particular features and the conserved functions of these proteins required for myelin formation and maintenance in fish. It is hoped that this approach will also help to improve our understanding of the molecular processes underlying the unique capacity of fish oligodendrocytes for remyelination after injury in the CNS. This survey may stimulate neuroscientists to engage into this exciting field.

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Section: Cnpasementioning

confidence: 99%

Features and Functions of Oligodendrocytes and Myelin Proteins of Lower Vertebrate Species

2008

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“…terminal, a number of phosphorylation sites [Ser-7; -12; -56; -110; -115; -151; -165 and Thr-34; 98] [131][132][133][134][135][136][137], two carbohydrate acceptor sites [Thr-95; -98] of Nacetylgalactosamine (GalNAc), a methylated Arg residue which occurs in both the mono-and di-methylated form, two likely deamidation sites [Gln-103; 147] and a possible Cterminal modification (i.e., loss of Arg). It also, contains an unusual tri-proline region [residues [99][100][101], which has been highlighted as an important structural feature similar to that contained in immunoglobulin G (IgG), and sequences homologous to cholera toxin A and B subunits [residues 102-118 and 67-77 in human MBP], which may possibly be involved in GM 1 ganglioside and GTP binding, as well as ADP ribosylation of MBP.…”

Section: C) Myelin Oligodendrocytic Basic Protein (Mobp)mentioning

confidence: 99%

Structure and Function of the Myelin Proteins: Current Status and Perspectives in Relation to Multiple Sclerosis

Tzakos¹,

Kursula²,

Troganis³

et al. 2005

CMC

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Multiple sclerosis (MS) is a chronic inflammatory disease of the central nervous system (CNS) characterized by demyelination and loss of neurological function, local macrophage infiltrate and neuroantigenspecific CD4 + T cells. MS arises from complex interactions between genetic, immunological, infective and biochemical mechanisms. Although the circumstances of MS etiology remain hypothetical, one persistent theme involves immune system recognition of myelin-specific antigens derived from myelin basic protein, the most abundant extrinsic myelin membrane protein, and/or another equally suitable myelin protein or lipid. Knowledge of the biochemical and physico-chemical properties of myelin proteins and lipids, particularly their composition, organization, structure and accessibility with respect to the compacted myelin multilayers, becomes central to understanding how and why myelin-specific antigens become selected during the development of MS. This review focuses on the current understanding of the molecular basis of MS with emphasis: (i) on the physical-chemical properties, organization, morphology, and accessibility of the proteins and lipids within the myelin multilayers; (ii) on the structure-function relationships and characterization of the myelin proteins relevant to the manifestation and evolution of MS; (iii) on conformational relationships between myelin epitopes which might become selected during the development of MS; (iv) on the structure of MHC/HLA in complex with MBP peptides as well as with TCR, which is crucial to the understanding of the pathogenesis of MS with the ultimate goal of designed antigen-specific treatments.

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“…RNase-protection analysis procedures were essentially as described previously [26]. pGEM-T-mLKB1 was digested with BamHI and BglII.…”

Section: Rnase-protection Analysismentioning

confidence: 99%

LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo

Collins

Reoma

Gamm

et al. 2000

Biochemical Journal

165

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Peutz-Jeghers syndrome (PJS) is an autosomal dominant disease characterized by melanocytic macules, hamartomatous polyps and an increased risk for numerous cancers. The human LKB1 (hLKB1) gene encodes a serine/threonine protein kinase that is deficient in the majority of patients with PJS. The murine LKB1 (mLKB1) cDNA was isolated, sequenced and shown to produce a 2.4-kb transcript encoding a 436 amino acid protein with 90% identity with hLKB1. RNA blot and RNase-protection analysis revealed that mLKB1 mRNA is expressed in all tissues and cell lines examined. The widespread expression of LKB1 transcripts is consistent with the elevated risk of multiple cancer types in PJS patients. The predicted LKB1 protein sequence terminates with a conserved prenylation motif (Cys433-Lys-Gln-Gln436) directly downstream from a consensus cAMP-dependent protein kinase (PKA) phosphorylation site (Arg428-Arg-Leu-Ser431). The expression of enhanced green fluorescent protein (EGFP)-mLKB1 chimaeras demonstrated that LKB1 possesses a functional prenylation motif that is capable of targeting EGFP to cellular membranes. Mutation of Cys433 to an alanine residue, but not phosphorylation by PKA, blocked membrane localization. These findings suggest that PKA does phosphorylate LKB1, although this phosphorylation does not alter the cellular localization of LKB1.

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Isolation of cDNA clones encoding RICH: a protein induced during goldfish optic nerve regeneration with homology to mammalian 2',3'-cyclic-nucleotide 3'-phosphodiesterases.

Cited by 24 publications

References 36 publications

Features and Functions of Oligodendrocytes and Myelin Proteins of Lower Vertebrate Species

Features and Functions of Oligodendrocytes and Myelin Proteins of Lower Vertebrate Species

Structure and Function of the Myelin Proteins: Current Status and Perspectives in Relation to Multiple Sclerosis

LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo

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