Purification and amino acid composition of monomeric and polymeric collagens

Steven, F. S.; Jackson, David S.

doi:10.1042/bj1040534

Cited by 90 publications

(22 citation statements)

References 13 publications

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“…Previously, both enzymatic and acid extraction methods have been used to obtain solubilized collagen for studies on collagen aging (6, 34). A number of studies have demonstrated that enzymatic extraction gives rise to subtle changes in the subsequent collagen products, although the gross physical characteristics of the molecules were not altered (35, 36). In this study, we used an acid extraction protocol, which ensures to prepare a native, nonpepsined, and fibrillar type I collagen.…”

Section: Discussionmentioning

confidence: 99%

A microscopic and macroscopic study of aging collagen on its molecular structure, mechanical properties, and cellular response

et al. 2013

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During aging, collagen structure changes, detrimentally affecting tissues' biophysical and biomechanical properties due to an accumulation of advanced glycation end-products (AGEs). In this investigation, we conducted a parallel study of microscopic and macroscopic properties of different-aged collagens from newborn to 2-yr-old rats, to examine the effect of aging on fibrillogenesis, mechanical and contractile properties of reconstituted hydrogels from these collagens seeded with or without fibroblasts. In addition to fibrillogenesis of collagen under the conventional conditions, some fibrillogenesis was conducted alongside a 12-T magnetic field, and gelation rate and AGE content were measured. A nondestructive indentation technique and optical coherence tomography were used to determine the elastic modulus and dimensional changes, respectively. It was revealed that in comparison to younger specimens, older collagens exhibited higher viscosity, faster gelation rates, and a higher AGE-specific fluorescence. Exceptionally, only young collagens formed highly aligned fibrils under magnetic fields. The youngest collagen demonstrated a higher elastic modulus and contraction in comparison to the older collagen. We conclude that aging changes collagen monomer structure, which considerably affects the fibrillogenesis process, the architecture of the resulting collagen fibers and the global network, and the macroscopic properties of the formed constructs.

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Section: Discussionmentioning

confidence: 99%

A microscopic and macroscopic study of aging collagen on its molecular structure, mechanical properties, and cellular response

et al. 2013

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“…This preparation is referred to as "soluble collagen." (c) Acid-dispersible polymerized human adult skin collagen was extracted from cadaver skin by the Nishihara method as modified by Steven and Jackson (11,29). The term Nishihara collagen is used to refer to this preparation.…”

Section: Methodsmentioning

confidence: 99%

Activation of hageman factor by collagen

Wilner¹,

Nossel²,

Leroy³

1968

J. Clin. Invest.

204

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A B S T R A C T Purified acid-soluble and insoluble human collagen accelerated the clotting of plateletpoor plasma in silicone-treated tubes. The clotpromoting effect did not appear to be due to thromboplastic activity since the collagen preparations did not activate factor X in the presence of factor VII and calcium. Instead, collagen appeared to accelerate clotting by activating Hageman factor (factor XII) on the basis of the following findings: collagen increased the clot-promoting activity of partially purified Hageman factor but exerted no further effect in the presence of kaolin, a known activator of Hageman factor; clot-promoting eluates were obtained from collagen exposed to normal, hemophilic, or PTC-deficient plasma but not from collagen exposed to Hageman or PTA-deficient plasma. The collagen molecule itself appeared to be required for the clot-promoting activity since digestion with collagenase or thermal denaturation at pH 2.5 (about 350C) resulted in very marked reduction in clot-promoting activity. Since thermal denaturation is associated with transformation of collagen structure from triple helical to random coil form, it is suggested that the native form of collagen is essential for the ability to activate Hageman factor.Blockage of the free amino groups by treatment with nitrous acid or dinitrofluorobenzene only slightly reduced the clot-promoting activity of collagen. In contrast, since addition of cationic proteins to collagen markedly reduced pro-coagulant activity it is suggested that negatively charged sites on the collagen molecule are critical for Hageman factor activation. This suggestion is supported by

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“…The samples were further extracted 3 times with 1.0M NaCl and 3 times with 0.1 M acetic acid using analogous volumes and procedure. The residue was dialyzed against a phosphate buffer (0.01 M) and fibrils were collected and purified from the insoluble material using the technique of Steven and Jackson [8]. The extracts obtained a t each salt and acid fractionation were separately pooled and centrifuged a t 65 000 x g for 60 min.…”

Section: Preparation Of Collagenmentioning

confidence: 99%

Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic Calves

Lenaers¹,

Nusgens²,

Lapière³

et al. 1971

Eur J Biochem

291

105

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Collagen has been extracted from the skin of dermatosparaxic calves and fractionated by acrylamide-gel electrophoresis and CM-cellulose chromatography. This collagen contains in large proportion two additional types of a-chains, p-a, and p-a,. The first, p-a,, ressembles a, of a collagen extracted from the skin of a normal calf in its amino-acid composition but its molecular weight is loo/, larger. The second, p-a,, is similar to a normal a, in its amino-acid composition but its molecular weight i s increased by 5O/,. The abnormal a-chains contain six to eight half cystine residues in p-a1 and one in pa,. As seen under the electron microscope on segment long spacing, the dermatosparaxic collagen is 25 nm larger than the normal collagen and the increased length results from an extension of the polypeptide chain at the N-terminal extremity of the molecules. Although the collagen is less extractable from the dermatosparaxic skin than from the normal skin and dimers and other polymers of the abnormal a-chains are observed, the dermatosparaxic collagen does not, in vitro, form fibrils of normal stability.Since an enzyme activity which can excise the N-terminal extension peptide of the dermatosparaxic collagen has been identified in extracts of normal skin but is absent in the dermatosparaxic animals, it is suggested that the dermatosparaxic collagen is a form of "procollagen)', from which all or a part of these peptides have not been removed and that such peptides function as coordinators in the post synthesis assembly of the collagen a-chains.Inbreeding and selection in the cattle population of Central and High Belgium has resulted in the disclosure of an unwanted recessive anomaly of the connective tissue. This inheritable disorder, characterized by an extreme fragility of the skin, was described in 1967 and was called dermatosparaxis [1,2]. As seen under the electron microscope [3,4], the dermis of these animals contained disorganized collagen bundles. The parallel packing of individual collagen filaments within the collagen fibers seemed to be impaired and the individual filaments displayed a weakly staining cross striation.I n the present report, the collagen extracted from the skin of dermatosparaxic animals is shown to contain a significant quantity of abnormal polypeptides The isolation and characterization of these polypeptides (a-chains) are described and data are presented which demonstrate that the abnormal polypeptides are a-chains prolongated by an extra peptide at their N-terminal extremity. The suggestion is made that these peptides are involved in the post synthesis registration of the a-chains. The hypothesis is pre- sented that the resultant association product is a precursor of the collagen normally found in the extracellular space, i.e. a normal collagen precursor or "procollagen') from which coordination peptides are not removed.Speakman [6] has recently proposed the existence of such peptides that would be required for the initiation of the collagen triple helix. He suggested that an enzyme cle...

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Purification and amino acid composition of monomeric and polymeric collagens

Cited by 90 publications

References 13 publications

A microscopic and macroscopic study of aging collagen on its molecular structure, mechanical properties, and cellular response

A microscopic and macroscopic study of aging collagen on its molecular structure, mechanical properties, and cellular response

Activation of hageman factor by collagen

Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic Calves

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