scholarly journals Developmental changes in the type I procollagen processing pathway in chick-embryo cornea

1991 ◽  
Vol 276 (3) ◽  
pp. 777-784 ◽  
Author(s):  
S J Mellor ◽  
G L Atkins ◽  
D J S Hulmes
Keyword(s):  
Chick Embryo ◽  
Kinetic Model ◽  
Rate Constants ◽  
Collagen Fibril ◽  
Electrophoretic Analysis ◽  
Developmental Changes ◽  
Type I ◽  
Electron Microscopic ◽  
Type I Procollagen ◽  
Stage Of Development

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.

scholarly journals Type I Procollagen N-proteinase from Chick Embryo Tendons

1989 ◽  
Vol 264 (19) ◽  
pp. 11336-11345 ◽  
Author(s):  
Y Hojima ◽  
J A McKenzie ◽  
M van der Rest ◽  
D J Prockop
Keyword(s):  
Chick Embryo ◽  
Type I ◽  
Type I Procollagen

A Kinetic Analysis of Type I Procollagen Processing in Developing Chick Embryo Cornea

1990 ◽  
Vol 580 (1 Structure, Mo) ◽  
pp. 484-488
Author(s):  
SALLY J. MELLOR ◽  
GORDON L. ATKINS ◽  
DAVID J. S. HULMES
Keyword(s):  
Chick Embryo ◽  
Kinetic Analysis ◽  
Type I ◽  
Type I Procollagen

scholarly journals Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta.

2003 ◽  
Vol 50 (2) ◽  
pp. 481-488 ◽  
Author(s):  
Anna Galicka ◽  
Sławomir Wołczyński ◽  
Andrzej Gindzieński
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Direct Sequencing ◽  
Electrophoretic Analysis ◽  
Skin Fibroblasts ◽  
Collagen Molecule ◽  
Molecular Defect ◽  
Type I ◽  
Single Nucleotide Change ◽  
Type I Procollagen

Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by L-[5-(3)H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy infant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular defect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30 degrees C for 5 min generated a shorter than normal alpha2 chain which melted at 36 degrees C. Direct sequencing of an asymmetric PCR product revealed a heterozygous single nucleotide change C-->G causing a substitution of histidine by aspartic acid in the alpha2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-alpha1(I) form as compared with control cells.

scholarly journals Cleavage of Type I Procollagen by Human Mast Cell Chymase Initiates Collagen Fibril Formation and Generates a Unique Carboxyl-terminal Propeptide

1997 ◽  
Vol 272 (11) ◽  
pp. 7127-7131 ◽  
Author(s):  
Mark W. Kofford ◽  
Lawrence B. Schwartz ◽  
Norman M. Schechter ◽  
Dorne R. Yager ◽  
Robert F. Diegelmann ◽  
...  
Keyword(s):  
Mast Cell ◽  
Collagen Fibril ◽  
Fibril Formation ◽  
Human Mast Cell ◽  
Type I ◽  
Type I Procollagen ◽  
Carboxyl Terminal ◽  
Mast Cell Chymase

scholarly journals OBSERVATIONS ON FIBRILLOGENESIS IN THE CONNECTIVE TISSUE OF THE CHICK EMBRYO WITH THE AID OF SILVER IMPREGNATION

1956 ◽  
Vol 2 (4) ◽  
pp. 67-70 ◽  
Author(s):  
F. Wassermann ◽  
L. Kubota
Keyword(s):  
Chick Embryo ◽  
Connective Tissue ◽  
Silver Impregnation ◽  
The Body ◽  
Electron Microscopic ◽  
Stage Of Development ◽  
Impregnation Technique ◽  
Microscopic Demonstration ◽  
Neutral Formalin ◽  
Electron Microscopic Demonstration

A technique is described which combines silver impregnation and ultrathin sectioning for the electron microscopic demonstration of fibrils in the connective tissue of the chick embryo. The electron micrographs presented in this paper provide evidence for the specificity and completeness of the silver-impregnation technique. It has been shown that, in this particular tissue after fixation in neutral formalin and at the stage of development represented by our material, the argyrophil fibers are embedded in a material which is continuous with the body of the fibroblasts.

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

Scanning electron microscopic study of collagen fibrillogenesis and extracellular compartmentalization in the chick embryo tendon

1986 ◽  
Vol 44 ◽  
pp. 208-209
Author(s):  
Grace C.H. Yang
Keyword(s):  
Chick Embryo ◽  
Extracellular Space ◽  
Fibroblast Cell ◽  
Collagen Fibrils ◽  
Electron Microscopic ◽  
Voltage Electron ◽  
Scanning Electron Microscopic Study ◽  
Microscopic Studies ◽  
And Function

The size and organization of collagen fibrils in the extracellular matrix is an important determinant of tissue structure and function. The synthesis and deposition of collagen involves multiple steps which begin within the cell and continue in the extracellular space. High-voltage electron microscopic studies of the chick embryo cornea and tendon suggested that the extracellular space is compartmentalized by the fibroblasts for the regulation of collagen fibril, bundle, and tissue specific macroaggregate formation. The purpose of this study is to gather direct evidence regarding the association of the fibroblast cell surface with newly formed collagen fibrils, and to define the role of the fibroblast in the control and the precise positioning of collagen fibrils, bundles, and macroaggregates during chick tendon development.

Structural Studies on the Eukaryotic Ribosome

1990 ◽  
Vol 48 (1) ◽  
pp. 256-257
Author(s):  
Adriana Verschoor ◽  
Ronald Milligan ◽  
Suman Srivastava ◽  
Joachim Frank
Keyword(s):  
Chick Embryo ◽  
3D Reconstruction ◽  
Single Particle ◽  
Mass Density ◽  
Particle Surface ◽  
Uranyl Acetate ◽  
Electron Microscopic ◽  
Eukaryotic Ribosome ◽  
Negative Stain ◽  
Reconstruction Methods

We have studied the eukaryotic ribosome from two vertebrate species (rabbit reticulocyte and chick embryo ribosomes) in several different electron microscopic preparations (Fig. 1a-d), and we have applied image processing methods to two of the types of images. Reticulocyte ribosomes were examined in both negative stain (0.5% uranyl acetate, in a double-carbon preparation) and frozen hydrated preparation as single-particle specimens. In addition, chick embryo ribosomes in tetrameric and crystalline assemblies in frozen hydrated preparation have been examined. 2D averaging, multivariate statistical analysis, and classification methods have been applied to the negatively stained single-particle micrographs and the frozen hydrated tetramer micrographs to obtain statistically well defined projection images of the ribosome (Fig. 2a,c). 3D reconstruction methods, the random conical reconstruction scheme and weighted back projection, were applied to the negative-stain data, and several closely related reconstructions were obtained. The principal 3D reconstruction (Fig. 2b), which has a resolution of 3.7 nm according to the differential phase residual criterion, can be compared to the images of individual ribosomes in a 2D tetramer average (Fig. 2c) at a similar resolution, and a good agreement of the general morphology and of many of the characteristic features is seen.Both data sets show the ribosome in roughly the same ’view’ or orientation, with respect to the adsorptive surface in the electron microscopic preparation, as judged by the agreement in both the projected form and the distribution of characteristic density features. The negative-stain reconstruction reveals details of the ribosome morphology; the 2D frozen-hydrated average provides projection information on the native mass-density distribution within the structure. The 40S subunit appears to have an elongate core of higher density, while the 60S subunit shows a more complex pattern of dense features, comprising a rather globular core, locally extending close to the particle surface.

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