The collagen molecule

2022 ◽  
pp. 29-54
Author(s):  
Béla Suki
Keyword(s):  
Collagen Molecule

scholarly journals Native cross-links in collagen fibrils induce resistance to human synovial collagenase

1979 ◽  
Vol 181 (3) ◽  
pp. 639-645 ◽  
Author(s):  
C A Vater ◽  
E D Harris ◽  
R C Siegel
Keyword(s):  
Lysyl Oxidase ◽  
Collagen Fibrils ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Cross Linking ◽  
Pathological Conditions ◽  
Insoluble Material ◽  
Induce Resistance ◽  
Cross Links

A model system consisting of highly purified lysyl oxidase and reconstituted lathyritic chick bone collagen fibrils was used to study the effect of collagen cross-linking on collagen degradation by mammalian collagenase. The results indicate that synthesis of approx. 0.1 Schiff-base cross-link per collagen molecule results in a 2–3-fold resistance to human synovial collagenase when compared with un-cross-linked controls or samples incubated in the presence of beta-aminopropionitrile to inhibit cross-linking. These results confirm previous studies utilizing artificially cross-linked collagens, or collagens isolated as insoluble material after cross-linking in vivo, and suggest that increased resistance to collagenase may be one of the earliest effects of cross-linking in vivo. The extent of intermolecular cross-linking among collagen fibrils may provide a mechanism for regulating the rate of collagen catabolism relative to synthesis in normal and pathological conditions.

Estimation of the binding force of the collagen molecule-decorin core protein complex in collagen fibril

2005 ◽  
Vol 38 (3) ◽  
pp. 433-443 ◽  
Author(s):  
Simone Vesentini ◽  
Alberto Redaelli ◽  
Franco M. Montevecchi
Keyword(s):  
Protein Complex ◽  
Collagen Fibril ◽  
Core Protein ◽  
Collagen Molecule ◽  
Binding Force

scholarly journals Monoclonal antibodies against chicken type IV and V collagens: electron microscopic mapping of the epitopes after rotary shadowing.

1984 ◽  
Vol 98 (5) ◽  
pp. 1637-1644 ◽  
Author(s):  
R Mayne ◽  
H Wiedemann ◽  
M H Irwin ◽  
R D Sanderson ◽  
J M Fitch ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cleavage Site ◽  
Type Iv Collagen ◽  
Collagen Molecule ◽  
Electron Microscopic ◽  
Type V Collagen ◽  
Type Iv ◽  
Type V ◽  
Rotary Shadowing

The location of the epitopes for monoclonal antibodies against chicken type IV and type V collagens were directly determined in the electron microscope after rotary shadowing of antibody/collagen mixtures. Three monoclonal antibodies against type IV collagen were examined, each one of which was previously demonstrated to be specific for only one of the three pepsin-resistant fragments of the molecule. The three native fragments were designated (F1)2F2, F3, and 7S, and the antibodies that specifically recognize each fragment were called, respectively, IA8 , IIB12 , and ID2 . By electron microscopy, monoclonal antibody IA8 recognized an epitope located in the center of fragment (F1)2F2 and in tetramers of type IV collagen at a distance of 288 nm from the 7S domain, the region of overlap of four type IV molecules. Monoclonal antibody IIB12 , in contrast, recognized an epitope located only 73 nm from the 7S domain. This result therefore provides direct visual evidence that the F3 fragment is located closest to the 7S domain and the order of the fragments must be 7S-F3-(F1)2F2. The epitope for antibody ID2 was located in the overlap region of the 7S domain, and often several antibody molecules were observed to binding to a single 7S domain. The high frequency with which antibody molecules were observed to bind to fragments of type IV collagen suggests that there is a single population of type IV molecules of chain organization [alpha 1(IV)]2 alpha 2(IV), and that four identical molecules must form a tetramer that is joined in an antiparallel manner at the 7S domain. The monoclonal antibodies against type V collagen, called AB12 and DH2 , were both found to recognize epitopes close to one another, the epitopes being located 45-48 nm from one end of the type V collagen molecule. The significance of this result still remains uncertain, but suggests that this site is probably highly immunoreactive. It may also be related to the specific cleavage site of type V collagen by selected metalloproteinases and by alpha-thrombin. This cleavage site is also known to be located close to one end of the type V molecule.

scholarly journals Characterization of Collagen from Sakhalin Taimen Skin as Useful Biomass

2020 ◽  
Vol 58 (4) ◽  
Author(s):  
Takeshi Nagai ◽  
Masataka Saito ◽  
Yasuhiro Tanoue ◽  
Norihisa Kai ◽  
Nobutaka Suzuki
Keyword(s):  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
High Yield ◽  
Collagen Molecule ◽  
Edible Portion ◽  
Sakhalin Taimen ◽  
Skin Collagen ◽  
Modification Technique ◽  
Cold Acetone ◽  
Α Helix

Research background. Animal collagen has been widely utilized in foods, cosmetics, and biomedical fields. The non-edible portion, such as fish skins and bones, are generated during cooking processes. Most of them are currently discarded as wastes, although the nutritional values of the skins and bones are high. It needs to utilize the non-edible portion for the reduction of environmental impact, as it may be one of source of environmental pollution. Experimental approach. Collagen was prepared from Sakhalin taimen skins as wastes generated during cooking processes. Next, the color, SDS-polyacrylamide gel electrophoresis, ultraviolet absorption, subunit composition, amino acid composition, denaturation temperature, and attenuated total reflectance-Fourier transform infrared spectroscopy analysis were conducted to explore the properties of the collagen. Lastly, it tried to improve the functional properties of the collagen using chemical modification technique for future applications. Results and conclusions. Cold acetone treatment made it possible to easily remove the fats and pigments from skins. The odorless and pure-white collagen was obtained with high-yield. The α3 chain did not exist in the collagen. Sakhalin taimen skin collagen had rich α-helix and low β-sheet structures. Succinylation caused the secondary structural changes of the collagen molecule. Moreover, succinylation made it possible not only to increase the viscosity of collagen solution and but also to improve the solubility of collagen in the physiological conditions around pH=6. Novelty and scientific contribution. This finding was the first report on the absence of the α3 chain in Salmonid fish skin collagens. The succinylated collagen from Sakhalin taimen skins as useful biomass has potential to utilize in foods, cosmetics, and its related industries.

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.

Conformational Changes and the Collagen Molecule

1967 ◽  
pp. 533-544
Author(s):  
KLAUS KÜHN ◽  
BODO ZIMMERMANN ◽  
CHRISTIAN TKOCZ
Keyword(s):  
Conformational Changes ◽  
Collagen Molecule

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.

In Vitro Platelet Reaction with Isolated Glomerular Basement Membrane

1971 ◽  
Vol 25 (03) ◽  
pp. 507-516 ◽  
Author(s):  
Chung-Hsin Ts'ao
Keyword(s):  
Platelet Aggregation ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Platelet Rich Plasma ◽  
Collagen Molecule ◽  
High Concentration ◽  
Platelet Reaction ◽  
Collagen Suspension

SummaryPurified canine glomerular basement membrane (BM) induced platelet aggregation when added to heparinized platelet-rich plasma (PRP) of the rat. Platelet aggregation induced by BM suspension was compared with that induced by collagen submicroscopically. When aliquots of BM or collagen suspension of the same concentration (2 mg/ml saline) was incubated with PRP, platelet-BM reaction was far less pronounced than platelet-collagen reaction. Platelet-BM reaction was slow and aggregates were small; swelling and pseudopod formation were obvious but platelet degranulation was limited. With high concentration (5 mg/ml saline) of BM suspension, the aggregation time was shortened and aggregates were generally composed of larger number of platelets. Treatment of BM with collagenase abolished the platelet-BM reaction. It is postulated that similar “platelet aggregating” elements in collagen are present in BM; but the quantity of these elements is less in a BM than in a collagen molecule.

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