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Biomedical subjects

H Bourbon

Publications and source records attributed to H Bourbon.

7 recordsLinked to original sources
PubMed2004

[Fluoroscopy guided L5-S1 transforaminal injection as a treatement for s1 radiculopathy].

OBJECTIVE: To assess the efficacy of fluoroscopy guided L5-S1 transforaminal steroid injections for the treatment of S1 radiculopathy secondary to intervertebral disk disorder. METHOD: 41 patients were included: prospective study (20 patients) and retrospective study (21 patients). All patients suffered from S1 radiculopathy secondary to nerve root compression by intervertebral disk material, as demonstrated by lumbar spine CT. The patients underwent 2 fluoroscopy guided L5-S1 transforaminal injections of steroid (Hydrocotancyl 125 mg), at 8 days interval. RESULTS: 60% of patients showed significant improvement of their painful radiculopathy at day 8 (n:41), 60-67% at day 30 (n:41) and 67% at day 90 (n:18). CONCLUSION: Fluoroscopy guided L5-S1 transforaminal injection showed good efficacy in the treatment of S1 radiculopathy.

Adrenal Cortex Hormones↗
PubMed1995

hemipterous encodes a novel Drosophila MAP kinase kinase, required for epithelial cell sheet movement.

During Drosophila embryogenesis, a cell sheet movement, dorsal closure, allows establishment of the dorsal epidermis. In this morphogenetic process, lateral epithelia undergo a dramatic movement toward the dorsal midline. In the mutant hemipterous (hep), spreading of the epithelia is blocked; in genetically sensitized hep embryos, cell sheet movement can be arrested at any time, indicating hep requirement in maintaining this morphogenetic activity. Further, hep is required for expression in the dorsal epithelium edges of another dorsal closure gene, puckered. The HEP protein is homologous to the Jun kinase kinase (JNKK) group of mitogen-activated protein kinase kinases (MAPKKs). These data suggest that hep functions in a novel Drosophila MAPK pathway, controlling puckered expression and morphogenetic activity of the dorsal epidermis.

Amino Acid Sequence↗
PubMed1988

Sequence and secondary structure of the 5' external transcribed spacer of mouse pre-rRNA.

We report the sequence of the 4006-nucleotide 5' external transcribed spacer (5'ETS) of the mouse ribosomal primary transcript. These data complete the sequence of the 13.4-kb mouse rRNA gene, thus providing a mammalian rRNA gene structure, in addition to yeast and Xenopus. The mouse 5'ETS displays a highly biased base content (very high in GC and particularly low in A), closely similar to the other transcribed spacers of the mouse ribosomal gene. This region seems to have accumulated sequence variation relatively rapidly during vertebrate evolution, with the possible insertion in rodents of sequences structurally similar to retroposons. About half the length of the mouse 5'ETS can fold into a giant and highly stable secondary structure, which is probably evolutionarily conserved in mammals and which could play an important role in the higher-order organization of mammalian pre-ribosomes.

Animals↗
PubMed1987

RNA binding fragments from nucleolin contain the ribonucleoprotein consensus sequence.

Nucleolin (C23 or 100 kDa) is a major nucleolar phosphoprotein whose primary structure has recently been determined (Lapeyre, B., Bourbon, H., and Amalric, F. (1987) Proc. Natl. Acad. Sci. U. S. A. 84, 1472-1476) and found to be associated with preribosomal RNA (Herrera, A. H., and Olson, M. O. J. (1986) Biochemistry 25, 6258-6263). To identify the RNA binding region of the molecule, cyanogen bromide fragments were tested for binding of 18 S and 28 S ribosomal RNA by a "Western blotting" technique. Fragments with apparent molecular masses of 13, 33, and 47 kDa bound RNA with no preference for either 18 S or 28 S RNA. By protein sequencing, these fragments were localized in the carboxyl-terminal two-thirds of the molecule. The nucleolin sequence was searched for the ribonucleoprotein consensus sequence found in other RNA binding proteins. Four copies of a closely related 11-residue sequence were found within 80-90 residue repeats in the RNA binding region between residues 285 and 629. These results suggest that a highly conserved structure for the binding of different classes of RNA is utilized by several proteins.

Amino Acid Sequence↗
PubMed1987

Nucleolin, the major nucleolar protein of growing eukaryotic cells: an unusual protein structure revealed by the nucleotide sequence.

Nucleolin (also called C23) is the major nucleolar protein of exponentially growing eukaryotic cells. It is found associated with intranucleolar chromatin and preribosomal particles. Through use of a polyclonal antiserum, nucleolin cDNA clones were isolated from a Chinese hamster ovary cell library constructed in the expression vector lambda gt11. The isolated cDNAs encoded a polypeptide containing 679 residues of the 713 amino acids of nucleolin. The amino acid sequence presents several unusual features: in particular, repetitive sequences are found at both ends of the molecule. A repeat, Hy-Thr-Pro-Hy-Lys-Lys-Hy-Hy, in which Hy is a nonpolar residue, is found six times in the NH2-end proximal portion, followed by three acidic stretches containing 25, 25, and 33 glutamic acid or aspartic acid residues. Four potential phosphorylation sites (serines) are also observed in this region. The COOH-terminal proximal portion of the protein carries a glycine-rich region with fairly regularly interspersed phenylalanine and dimethylarginine residues. The two terminal portions of the molecule exhibit unique potential secondary structures: alpha-helix (NH2 terminus) and extended (COOH terminus). The central region exhibits alternating hydrophobic and hydrophilic stretches. Five potential N glycosylation sites are detected. The structure of this protein may reflect two functions in preribosome biogenesis: interaction with chromatin (NH2 terminus) and with preribosomes (COOH terminus).

Amino Acid Sequence↗
PubMed1982

Detection and localization of a class of proteins immunologically related to a 100-kDa nucleolar protein.

A high-molecular-mass nucleolar protein (100-kDa protein) is associated with nascent pre-rRNA and pre-ribosomes in Chinese hamster ovary cells. We have prepared antiserum against the 100-kDa protein and we have used it to study the intracellular localization and the possible processing of this protein. Serologically related proteins were detected in the nucleolus and in ribosomes. Proteins of various subcellular fractions were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, transferred to nitrocellulose filters, reacted with serum and the protein-immunoglobulin complexes were revealed by 125I-labeled protein A. In the nucleolus, four proteins with molecular masses of 100 kDa, 95 kDa, 76 kDa and 70 kDa were thus visualized. In the ribosomes, two proteins (of 100 kDa and 76 kDa) gave a strong reaction while six others (of 70 kDa, 60 kDa, 50 kDa, 30 kDa, 21 kDa, 18 kDa) reacted slightly. By immunological precipitation of total cell extracts, we have shown that the 100-kDa protein antiserum cross-reacts with five proteins with molecular masses of 120 kDa, 100 kDa, 95 kDa, 70 kDa and 60 kDa. Specific degradation of the 100-kDa protein into similar peptides with molecular masses of 95 kDa, 76 kDa, 70 kDa, 60 kDa and 50 kDa can be achieved by incubation of isolated nucleoli or of purified 100-kDa protein in vitro. Cleavage of the protein is due to a thiol endoprotease which is tightly bound to the 100-kDa protein. Possible relations between the maturation of this preribosomal protein into ribosomal proteins and the processing of preribosomal RNA into mature ribosomal RNA are discussed.

Animals↗