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504 results on '"David, J.S."'

201. Procollagen C-proteinase enhancer-1 (PCPE-1) interacts with β2-microglobulin (β2-m) and may help initiate β2-m amyloid fibril formation in connective tissues

Author

Morimoto, Hisanori, primary, Wada, Jun, additional, Font, Bernard, additional, Mott, Joni D., additional, Hulmes, David J.S., additional, Ookoshi, Tadakazu, additional, Naiki, Hironobu, additional, Yasuhara, Akihiro, additional, Nakatsuka, Atsuko, additional, Fukuoka, Kousuke, additional, Takatori, Yuji, additional, Ichikawa, Haruo, additional, Akagi, Shigeru, additional, Nakao, Kazushi, additional, and Makino, Hirofumi, additional

Published
2008
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202. BOOK REVIEW

Author

David J.S. Montagnes

Subjects
Aquatic Science, Oceanography, Water Science and Technology
Published
2009
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206. Developmental changes in the type I procollagen processing pathway in chick-embryo cornea

Author

Gordon L. Atkins, David J.S. Hulmes, S J Mellor, and Deleage, Gilbert

Subjects
Gel electrophoresis, Models, Molecular, Chemistry, Alpha (ethology), Embryo, Cell Biology, Metabolism, Chick Embryo, Fibril, Biochemistry, Pepsin A, Cornea, Procollagen peptidase, Kinetics, Biophysics, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Collagen, Densitometry, Molecular Biology, Flux (metabolism), Protein Processing, Post-Translational, Procollagen, Research Article
Abstract

Type I procollagen processing in chick-embryo corneas was studied at days 12, 14 and 17 of development. Pulse-chase experiments and electrophoretic analysis of salt-soluble extracts showed developmental changes in the processing pathway. A kinetic model was fitted to the data to determine rate constants for processing of both N- and C-propeptides. Data for pro alpha 1(I)-chain processing and pro alpha 2(I)-chain processing were fitted separately (where pro means procollagen). Between days 12 and 17 the relative flux through the pC-collagen (procollagen chain lacking the N-propeptide) and pN-collagen (procollagen chain lacking the C-propeptide) pathways increased approx. 4-fold. Pro alpha 1(I) chains and pro alpha 2(I) chains were processed by slightly different routes. Variations in the rate constants were compared with electron-microscopic measurements of collagen fibril diameters at each stage of development. Diameters increased by less than 10% over the period from 12 to 17 days. It was concluded that fibril diameters are relatively insensitive to the pathway of procollagen processing in the salt-soluble pool.Type I procollagen processing in chick-embryo corneas was studied at days 12, 14 and 17 of development. Pulse-chase experiments and electrophoretic analysis of salt-soluble extracts showed developmental changes in the processing pathway. A kinetic model was fitted to the data to determine rate constants for processing of both N- and C-propeptides. Data for pro alpha 1(I)-chain processing and pro alpha 2(I)-chain processing were fitted separately (where pro means procollagen). Between days 12 and 17 the relative flux through the pC-collagen (procollagen chain lacking the N-propeptide) and pN-collagen (procollagen chain lacking the C-propeptide) pathways increased approx. 4-fold. Pro alpha 1(I) chains and pro alpha 2(I) chains were processed by slightly different routes. Variations in the rate constants were compared with electron-microscopic measurements of collagen fibril diameters at each stage of development. Diameters increased by less than 10% over the period from 12 to 17 days. It was concluded that fibril diameters are relatively insensitive to the pathway of procollagen processing in the salt-soluble pool.

Published
1991

207. D-periodic assemblies of type I procollagen

Author

A. Paul Mould, David J.S. Hulmes, David F. Holmes, John A. Chapman, Christopher H.J. Sear, Christine Cummings, Institut de biologie et chimie des protéines [Lyon] (IBCP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), and Deleage, Gilbert

Subjects
Type I Procollagen, Macromolecular Substances, Size-exclusion chromatography, Chick Embryo, Biology, In Vitro Techniques, Collagen fibril, 03 medical and health sciences, Overlap zone, Structural Biology, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Solubility, Protein precursor, Molecular Biology, 030304 developmental biology, 0303 health sciences, 030302 biochemistry & molecular biology, Immunohistochemistry, Procollagen peptidase, Crystallography, Microscopy, Electron, Transmission electron microscopy, Chromatography, Gel, Collagen, Protein Processing, Post-Translational, Procollagen, Protein Binding
Abstract

International audience; The solubility limit of purified chick type I procollagen, incubated at 37 degrees C in phosphate-buffered saline, was found to be in the range 1 to 1.5 mg/ml. At higher concentrations large aggregates formed. These comprised: (1) D-periodic assemblies; (2) narrow filaments with no apparent periodicity; and (3) segment-long-spacing-like aggregates. The D-periodic assemblies, which predominated at high concentrations, were separated from the other types of aggregate and found to be ribbon-like. Ribbons were uniform in thickness (approximately 8 nm) and up to 1 micron wide. Staining patterns showed features similar to those in native-type collagen fibrils. Immunolabelling indicated that the carboxyl-terminal propeptide domains were close to the carboxyl-terminal gap-overlap junction, and that the amino-terminal propeptide domains were folded over into the amino-terminal side of the overlap zone. Both propeptide domains appeared to be located on the surface of the assemblies. These observations show that intact propeptide domains hinder, but do not prevent, the formation of D-periodic assemblies. The presence of the propeptide domains on the surface of a growing assembly could restrict its lateral growth and limit its final thickness.The solubility limit of purified chick type I procollagen, incubated at 37 degrees C in phosphate-buffered saline, was found to be in the range 1 to 1.5 mg/ml. At higher concentrations large aggregates formed. These comprised: (1) D-periodic assemblies; (2) narrow filaments with no apparent periodicity; and (3) segment-long-spacing-like aggregates. The D-periodic assemblies, which predominated at high concentrations, were separated from the other types of aggregate and found to be ribbon-like. Ribbons were uniform in thickness (approximately 8 nm) and up to 1 micron wide. Staining patterns showed features similar to those in native-type collagen fibrils. Immunolabelling indicated that the carboxyl-terminal propeptide domains were close to the carboxyl-terminal gap-overlap junction, and that the amino-terminal propeptide domains were folded over into the amino-terminal side of the overlap zone. Both propeptide domains appeared to be located on the surface of the assemblies. These observations show that intact propeptide domains hinder, but do not prevent, the formation of D-periodic assemblies. The presence of the propeptide domains on the surface of a growing assembly could restrict its lateral growth and limit its final thickness.

Published
1990

209. Substrate-specific Modulation of a Multisubstrate Proteinase

Author

Moali, Catherine, primary, Font, Bernard, additional, Ruggiero, Florence, additional, Eichenberger, Denise, additional, Rousselle, Patricia, additional, François, Vincent, additional, Oldberg, Åke, additional, Bruckner-Tuderman, Leena, additional, and Hulmes, David J.S., additional

Published
2005
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221. Lysyl Oxidase-like Protein from Bovine Aorta

Author

Borel, Agnes, primary, Eichenberger, Denise, additional, Farjanel, Jean, additional, Kessler, Efrat, additional, Gleyzal, Claudine, additional, Hulmes, David J.S., additional, Sommer, Pascal, additional, and Font, Bernard, additional

Published
2001
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240. On molecular packing in pN-collagen sheets

Author

David J.S. Hulmes and Deleage, Gilbert

Subjects
Materials science, Molecular Structure, genetic structures, Self association, General Medicine, Biochemistry, Crystallography, Procollagen peptidase, Structural Biology, Transmission electron microscopy, Scanning transmission electron microscopy, Microscopy, Electron, Scanning, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Ultrastructure, Collagen, Self-assembly, Molecular Biology
Abstract

Recent data from scanning transmission electron microscopy of pN-collagen sheets are shown to be consistent with a model based on quasi-hexagonal molecular packing

Published
1992
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247. A Drop of Blood

Author

David, J.S.

Abstract

More than two months ago, I stuck myself with an H.I.V.-tainted scalpel. I didn't wake up that morning expecting it to happen, of course. I'm always careful: double gloves, a […]

Published
1993

248. Treatment of menorrhagia by endometrial ablation

Author

David J.S. Hill and Peter Maher

Subjects
medicine.medical_specialty, medicine.diagnostic_test, business.industry, medicine.medical_treatment, Uterus, Hysteroscopy, General Medicine, Endometrium, Resection, Surgery, medicine.anatomical_structure, Electrocoagulation, medicine, Cauterization, Endometrial ablation, Humans, Female, Laser Therapy, business, Menorrhagia
Published
1990
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