On the length and molecular weight of tropocollagen from calf skin

Rice, Robert V.; Casassa, Edward F.; Kerwin, R. E.; Maser, Morton D.

doi:10.1016/0003-9861(64)90025-6

Cited by 55 publications

(19 citation statements)

References 28 publications

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“…Both substrates were resistant to pepsin, neither would precipitate when centrifuged at 100,000 X g for 2 hr at 240, and both sedimented at approximately 3.2 S (Fig. 4), corresponding to values previously reported for soluble collagen (23,24). …”

Section: Resultsmentioning

confidence: 48%

“…All collagenase assays were performed using labeled soluble native collagen substrates prepared from confluent monolayers of either newborn rabbit lung fibroblasts (NB-6) or fetal human lung fibroblasts (HFL-1) in subeultivation 15 (NB-6) or 10 (HFL-1). The cells were incubated in serum-free modified Eagle's medium with [3H] proline (31 Ci/mmol, 50,uCi/ml), j-aminopropionitrile (0.5 mM), and ascorbic acid (0.3 mM) for 24 (20). Following electrophoresis, the gels were dried and fluororadiograms were prepared.…”

Section: Introductionmentioning

confidence: 99%

“…and the cells were plated as previously described (18). Medium (modified Eagle's medium without serum) between 24 and 48 hr in culture was collected, concentrated by dialysis against Aquacide II, and dialyzed against buffer for the collagenase-assay.…”

Section: Introductionmentioning

confidence: 99%

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Granulocyte collagenase: selective digestion of type I relative to type III collagen.

Horwitz¹,

Hance²,

Crystal³

1977

Proc. Natl. Acad. Sci. U.S.A.

175

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Collagenases produced by human polymorphonuclear leukocytes, human lung fibroblasts, and rabbit pulmonary alveolar macrophages were compared in their ability to digest soluble native type I and type III collagens. While the fibroblast and macrophage collagenases attacked the two substrates at approximately equal rates, the leukocyte collagenase attacked type I collagen preferentially (15:1) in comparison to type III collagen. This was true with human or rabbit collagen substrates. Thus, proteolysis of collagen, particularly in acute inflammation, may have a significant role in controlling the types of collagen present in connective tissue.

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Section: Resultsmentioning

confidence: 48%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Granulocyte collagenase: selective digestion of type I relative to type III collagen.

Horwitz¹,

Hance²,

Crystal³

1977

Proc. Natl. Acad. Sci. U.S.A.

175

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“…The amino acid sequences constitute a left-handed polypeptide helix, three of which assemble in parallel into a right-handed supercoil producing the tropocollagen (TC) molecule. A TC molecule is approximately 300 nm long, 1-2 nm in diameter and weighs 300 kDa (Rice et al 1964;Parry 1988;Kadler et al 1996;Ottani et al 2002;Buehler 2006b). The detailed molecular topography of short peptide fragments that model certain aspects of the naturally occurring fibrillar collagen molecules has been determined from X-ray diffraction experiments (Bella et al 1994;Kramer et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Deformation micromechanisms of collagen fibrils under uniaxial tension

Tang

Ballarini

Buehler

et al. 2009

J. R. Soc. Interface.

120

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Collagen, an essential building block of connective tissues, possesses useful mechanical properties due to its hierarchical structure. However, little is known about the mechanical properties of collagen fibril, an intermediate structure between the collagen molecule and connective tissue. Here, we report the results of systematic molecular dynamics simulations to probe the mechanical response of initially unflawed finite size collagen fibrils subjected to uniaxial tension. The observed deformation mechanisms, associated with rupture and sliding of tropocollagen molecules, are strongly influenced by fibril length, width and cross-linking density. Fibrils containing more than approximately 10 molecules along their length and across their width behave as representative volume elements and exhibit brittle fracture. Shorter fibrils experience a more graceful ductile-like failure. An analytical model is constructed and the results of the molecular modelling are used to find curve-fitted expressions for yield stress, yield strain and fracture strain as functions of fibril structural parameters. Our results for the first time elucidate the size dependence of mechanical failure properties of collagen fibrils. The associated molecular deformation mechanisms allow the full power of traditional material and structural engineering theory to be applied to our understanding of the normal and pathological mechanical behaviours of collagenous tissues under load.

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“…The fiber formation seems to be influenced by the extent of cross-linking of the tropocollagen molecule [8,9] For studies in vitro, under physiological conditions, of fiber formation from tropocollagen as well as of interactions between tropocollagen and glycosaminoglycans it is desirable to use tropocollagen in monomeric form. The isolation of native tropocollagen in monomeric form is, however, cumbersome and has so far only been successful a t acid pH [2,6,17]. When studied in neutral salt solutions, the tropocollagen molecules have invariably been aggregated [17,18] and light scattering measurements have given molecular weights corresponding to polymeric forms of tropocollagen, in spite of previous strenuous centrifugation [17,18].…”

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confidence: 99%

Non‐Aggregated Tropocollagen at Physiological pH and Ionic Strength

Öbrink

1972

European Journal of Biochemistry

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Collagen was isolated from the skins of normal and lathyritic rats. Amino acid analysis, sugar analysis and analysis of the subunit composition indicated that the two types of collagen differed only with regard to the degree of cross-linking. Investigations by physical chemical methods showed that the lathyritic collagen preparations behaved as free monomers below 15 "C a t physiological ionic conditions with the following characteristics: s :~,~ = 2.92 S, D:,,w = 0.78x lo-' cm2/sec, [rj ] = 11.1 dl/g. Mr from light scattering, sedimentation equilibrium and sedimentation-diffusion was 310000-320000. Light scattering data agreed with a rod-like structure and the molecular length from light scattering, frictional ratio and intrinsic viscosity was 300 nm. Preparations of normal collagen were aggregated under physiological ionic conditions and different reasons for the aggregation are discussed. It is suggested that lathyritic collagen should be a good model substance in studies a t the molecular level of fibrillogenesis and interactions between collagen and other macromolecules. Tropocollagen, which can be isolated by various extraction procedures [6] from different types of tissues, has the inherent ability to form fibers of native type, when the temperature is raised to 37 "C and the pH is near 7 [7]. The fiber formation seems to be influenced by the extent of cross-linking of the tropocollagen molecule [8,9] For studies in vitro, under physiological conditions, of fiber formation from tropocollagen as well as of interactions between tropocollagen and glycosaminoglycans it is desirable to use tropocollagen in monomeric form. The isolation of native tropocollagen in monomeric form is, however, cumbersome and has so far only been successful a t acid pH [2,6,17]. When studied in neutral salt solutions, the tropocollagen molecules have invariably been aggregated [17,18] and light scattering measurements have given molecular weights corresponding to polymeric forms of tropocollagen, in spite of previous strenuous centrifugation [17,18]. The lower molecular weights obtained by sedimentation equilibrium techniques [ 171 have probably been due to a removal of aggregated material from the solution. I n the present investigation, lathyritic collagen has for the first time been characterized in solution by physical chemical methods. The results show, that this collagen occurs in monomeric form a t physiological pH and ionic strength a t temperatures ranging between 4 and 15 "C. For comparison, neutral saltsoluble and citrate-soluble collagens from the skin of normal rats have been partly characterized. EXPERIMENTAL PROCEDURE Materials3-Amino-propionitrile was supplied by AB Pharmacia, Uppsala and 3-amino-propionitrile fumarate was supplied by Schuchardt (Munich).All chemicals were reagent grade or the highest quality available. Isolation and Purification of CollagenCollagen was isolated from the skins of normal and lathyritic male Sprague-Dawley rats, ranging in weight from 50-150 g. Animals were made lathyritic by feeding ...

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On the length and molecular weight of tropocollagen from calf skin

Cited by 55 publications

References 28 publications

Granulocyte collagenase: selective digestion of type I relative to type III collagen.

Granulocyte collagenase: selective digestion of type I relative to type III collagen.

Deformation micromechanisms of collagen fibrils under uniaxial tension

Non‐Aggregated Tropocollagen at Physiological pH and Ionic Strength

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