Molecular mobility in the gap regions of type 1 collagen fibrils

1986 ◽  
Vol 6 (2) ◽  
pp. 221-226 ◽  
Author(s):  
R. D. B. Fraser ◽  
B. L. Trus
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Collagen Molecule ◽  
Type I ◽  
Amino Acid Residues ◽  
Linear Distribution ◽  
Uniform Distributions ◽  
Imino Acid ◽  
Hydropathy Index

Recent studies of the structure of Type I collagen fibrils (Piez and Trus, Biosci. Rep.1:801–810, 1981; Fraser, MacRae, Miller and Suzuki, J. Mol. Biol.167:497–521, 1983) suggest that the segments of the collagen molecule which comprise the gap region are more mobile than those which comprise the overlap region. We have analyzed the distribution of amino acid residues and triplet types between the two regions, and find significantly non-uniform distributions for Ala, Gln, His, Hyp, Leu, Phe, and Tyr, and for triplets containing two imino acid residues. Taken together with the lower packing density in the gap region these observations provide a basis for understanding the greater mobility of the molecular segments in the gap region. In addition, we have examined the linear distribution of residue types in the two regions and also the hydropathy profile (Kyte and Doolittle, J. Mol. Biol.157: 105–113, 1982). These reveal a segment of the gap region comprising helical residues 165–173, 399–407, 633–641 and 867–975 which has the highest hydropathy index, is devoid of charged residues, and contains very high proportions of Ala, Hyp and Phe.

scholarly journals Embryonic avian cornea contains layers of collagen with greater than average stability.

1986 ◽  
Vol 103 (4) ◽  
pp. 1587-1593 ◽  
Author(s):  
T F Linsenmayer ◽  
E Gibney ◽  
J M Fitch
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Collagen Molecule ◽  
Type I ◽  
Corneal Tissue ◽  
Tissue Sections ◽  
Triple Helical Domain ◽  
Thermal Stability Of

A unique morphological feature of the embryonic avian cornea is the uniformity of its complement of striated collagen fibrils, each of which has a diameter of 25 nm. We have asked whether this apparent morphological uniformity also reflects an inherent uniformity of the structural and physical properties of these fibrils. For this we have examined the in situ thermal stability of the type I collagen within these fibrils. Corneal tissue sections were reacted at progressively higher temperatures with conformation-dependent monoclonal antibodies directed against the triple-helical domain of the type I collagen molecule. These studies show that the cornea contains layers of collagen fibrils with greater than average stability. The two most prominent of these extend uninterrupted across the entire width of the cornea, and then appear to insert into thick bundles of scleral collagen, which in turn appear to insert into the scleral ossicles, a ring of bony plates which circumscribe the sclera of the avian eye. Once formed, the bands may act to stabilize the shape of the cornea or, conversely, to alter it during accommodation.

scholarly journals Thermal (In)Stability of Type I Collagen Fibrils

2009 ◽  
Vol 102 (4) ◽  
Author(s):  
S. G. Gevorkian ◽  
A. E. Allahverdyan ◽  
D. S. Gevorgyan ◽  
A. L. Simonian
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

Detection of type I collagen fibrils formation and dissociation by a fluorescence method based on thioflavin T

2016 ◽  
Vol 92 ◽  
pp. 1175-1182 ◽  
Author(s):  
Meilian Zou ◽  
Huan Yang ◽  
Haibo Wang ◽  
Haiyin Wang ◽  
Juntao Zhang ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Fluorescence Method ◽  
Thioflavin T ◽  
Type I

scholarly journals Mechanical Properties of Native and Cross-linked Type I Collagen Fibrils

2008 ◽  
Vol 94 (6) ◽  
pp. 2204-2211 ◽  
Author(s):  
Lanti Yang ◽  
Kees O. van der Werf ◽  
Carel F.C. Fitié ◽  
Martin L. Bennink ◽  
Pieter J. Dijkstra ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I

The ultrastructure of type I collagen at nanoscale: large or small D-spacing distribution?

Nanoscale ◽  
2014 ◽  
Vol 6 (14) ◽  
pp. 8134-8139 ◽  
Author(s):  
Hai-Nan Su ◽  
Li-Yuan Ran ◽  
Zhi-Hua Chen ◽  
Qi-Long Qin ◽  
Mei Shi ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Spacing Distribution ◽  
Large Distribution

The large distribution ofD-spacing values of type I collagen fibrils was due to image drift during measurement, and theD-spacing values were nearly identical both within a single fibril bundle and in different fibril bundles, exhibiting only a narrow distribution of 2.5 nm.

Has collagen a role in muscle pattern formation in the developing chick wing?

Development ◽  
1980 ◽  
Vol 60 (1) ◽  
pp. 245-254
Author(s):  
G. B. Shellswell ◽  
A. J. Bailey ◽  
V. C. Duance ◽  
D. J. Restall
Keyword(s):  
Type I Collagen ◽  
Immunofluorescence Microscopy ◽  
Microscopy Study ◽  
Type Iii Collagen ◽  
Type I ◽  
Embryonic Chick ◽  
Collagen Types ◽  
Developing Muscle ◽  
Ventral Muscle

We have used antibodies to three of the isomorphic forms of collagen, types I, III and V, in an immunofluorescence microscopy study of myogenesis in the embryonic chick wing, concentrating on the period between stages 27 and 30 (5 to 7·5 days incubation) which is when the dorsal and ventral muscle masses separate into discrete muscles. We have demonstrated the presence of all three collagen types at the ectoderm-mesenchyme junction from stage 27 onwards. Type I collagen and then type III collagen are found in progressively deeper layers of the dermis at the later stages. Both types I and V collagen are initially present in the cartilage elements, but type 1 collagen becomes restricted to the periphery of these structures at later stages. The developing muscle areas show a lack of staining at all stages and it is only at the latest stages that types I and III collagen first appear in the surrounding epimysium. We discuss possible mechanisms for the division of the muscle masses in the light of this information on the distribution of collagen types.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter

1990 ◽  
Vol 95 (4) ◽  
pp. 649-657 ◽  
Author(s):  
D.E. Birk ◽  
J.M. Fitch ◽  
J.P. Babiarz ◽  
K.J. Doane ◽  
T.F. Linsenmayer
Keyword(s):  
Type I Collagen ◽  
Small Diameter ◽  
Collagen Molecule ◽  
Type I ◽  
Collagen Types ◽  
Type V Collagen ◽  
Amino Terminal ◽  
Type V ◽  
Fibril Diameter

The small-diameter fibrils of the chick corneal stroma are heterotypic, composed of both collagen types I and V. This tissue has a high concentration of type V collagen relative to other type I-containing tissues with larger-diameter fibrils, suggesting that heterotypic interactions may have a regulatory role in the control of fibril diameter. The interactions of collagen types I and V were studied using an in vitro self-assembly system. Collagens were purified from lathyritic chick embryos in the presence of protease inhibitors. The type V collagen preparations contained higher molecular weight forms of the alpha 1(V) and alpha 2(V) chains constituting 60–70% of the total. Rotary-shadow electron micrographs showed a persistence of a small, pepsin-sensitive terminal region in an amount consistent with that seen by electrophoresis. In vitro, this purified type V collagen formed thin fibrils with no apparent periodicity, while type I collagen fibrils had a broad distribution of large diameters. However, when type I collagen was mixed with increasing amounts of type V collagen a progressive and significant decrease in both the mean fibril diameter and the variance was observed for D periodic fibrils. The amino-terminal domain of the type V collagen molecule was required for this regulatory effect and in its absence little diameter reducing activity was observed. Electron microscopy using collagen type-specific monoclonal antibodies demonstrated that the fibrils formed were heterotypic, containing both collagen types I and V. These data indicate that the interaction of type V with type I collagen is one mechanism modulating fibril diameter and is at least partially responsible for the regulation of collagen fibril formation.

Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation

1993 ◽  
Vol 39 (4) ◽  
pp. 635-640 ◽  
Author(s):  
J Risteli ◽  
I Elomaa ◽  
S Niemi ◽  
A Novamo ◽  
L Risteli
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Type I ◽  
Serum Samples ◽  
Amino Terminal ◽  
Wide Range ◽  
Carboxy Terminal

Abstract We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.

scholarly journals Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang
Keyword(s):  
Type I Collagen ◽  
Structural Characteristics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dry Weight ◽  
Collagen Fibrils ◽  
Type I ◽  
X Ray Diffraction ◽  
Aggregation Structure ◽  
Native Collagen

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

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