ABSTRACT
A cDNA which encodes a specific member of the NADP-dependent isocitrate dehydrogenase (ICDH) multi-isoenzyme family has been isolated from a tobacco cell suspension library, and the expression pattern of ICDH transcripts examined in various plant tissues. To assign this cDNA to a specific ICDH isoenzyme, the major, cytosolic ICDH isoenzyme of tobacco leaves (ICDH1) was purified to homogeneity and its N-terminus as well as several tryptic peptides, representing 30% of the protein, were sequenced. The comparison of these amino acid sequences with the deduced protein sequence of the cDNA confirmed that this clone encodes for ICDH1. The total ICDH specific activity and protein content were higher in vascular-enriched tobacco leaf tissue than in deveined (depleted in midrib and first-order veins) leaves. Taking advantage of antibodies raised against either ICDH1 or the chloroplastic ICDH2 isoenzyme from tobacco cell suspensions, an immuno-cytochemical approach indicated that the ICDH1 isoenzyme, located in the cytosolic compartment of tobacco leaf cells, is responsible for this expression pattern. This observation was confirmed by northern blot analyses, using a specific probe obtained from the 3' non-coding region of the ICDH1 cDNA. A comparison of ICDH protein sequences shows a large degree of similarity between eukaryotes (> 60%) but a poor homology is observed when compared to Escherichia coli ICDH (< 20%). However, it was found that the amino acids implicated in substrate binding, deduced from the 3-dimensional structure of the E. coli NADP-ICDH, appear to be conserved in all the deduced eukaryotic ICDH proteins reported until now.
Subject(s)
Cytosol/enzymology , Isocitrate Dehydrogenase/genetics , Isoenzymes/genetics , Nicotiana/genetics , Plants, Toxic , Amino Acid Sequence , Base Sequence , Blotting, Northern , Blotting, Western , Cell Compartmentation , Cloning, Molecular , Conserved Sequence , DNA, Complementary/genetics , Immunohistochemistry , Isocitrate Dehydrogenase/isolation & purification , Molecular Sequence Data , Plant Leaves/enzymology , Plant Leaves/ultrastructure , RNA, Messenger/genetics , RNA, Plant/genetics , Sequence Analysis , Sequence Homology, Amino Acid , Species Specificity , Tissue Distribution , Nicotiana/enzymologyABSTRACT
The authors report the case of a woman operated for multiple dorsal nodes of the fingers with a lytic appearance on X-rays of the distal joints. The histopathology concluded on multicentric reticulohistiocytosis which is a very rare disease (fewer than 100 cases) affecting the hand (90%), skin and joints, and other organ systems. The prognosis is not good as the disease is disabling to the hand and malignant diseases may occur in 15 to 25% of cases. No treatment, even very aggressive, has been shown to be truly effective.
Subject(s)
Fingers , Histiocytosis, Non-Langerhans-Cell/diagnostic imaging , Adult , Biopsy , Female , Histiocytosis, Non-Langerhans-Cell/pathology , Histiocytosis, Non-Langerhans-Cell/surgery , Humans , Prognosis , Radiography , Terminology as TopicSubject(s)
Arthritis/surgery , Arthroplasty/standards , Carpal Bones/surgery , Osteotomy/standards , Adult , Aged , Arthritis/pathology , Arthritis/physiopathology , Arthroplasty/methods , Arthroplasty/psychology , Consumer Behavior , Female , Follow-Up Studies , Humans , Joint Prosthesis , Male , Middle Aged , Multicenter Studies as Topic , Osteotomy/methods , Tendon Transfer/methods , Tendon Transfer/standardsABSTRACT
Four cases of osteoid osteoma of the distal phalanx are described. The difficulty of diagnosis is stressed. Complete removal of the nidus is essential for surgical cure. Other modes of treatment are discussed and our series compared to other similar cases described in the literature.
Subject(s)
Bone Neoplasms , Osteoma, Osteoid , Adolescent , Adult , Female , Fingers , Humans , Male , Middle AgedSubject(s)
Ambulatory Surgical Procedures , Dupuytren Contracture/surgery , Absenteeism , Adult , Aged , Female , Humans , Male , Methods , Middle Aged , Wound HealingABSTRACT
The hypothesis of a vitamin K hydroquinone hemicarbonate as intermediate of vitamin K-dependent carboxylation of glutamic residues, has been examined, by testing several vitamin K hydroquinone esters as inhibitors of the reaction. Among the esters that have been synthetized, a monoacetate proved to be an inhibitor. Kinetic analysis shows that the inhibition is no competitive with respect to vitamin K.
