Isolation and characterization of the cyanogen bromide peptides from the α(III)chain of human collagen

Chung, Endy; Keele, Elizabeth M.; Miller, Edward J.

doi:10.1021/bi00714a006

Cited by 164 publications

(51 citation statements)

References 25 publications

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“…After reduction, 2 smaller fractions were obtained corresponding to molecular weights of 180,000 and 95,000. These results are identical with collagens of normal human skin (21) and lung (12), including the occurrence of disulfide bonds in…”

Section: Discussionsupporting

confidence: 80%

Investigation of type i and type iii collagens of the lung in progressive systemic sclerosis

Seyer

Kang²,

Rodnan³

1981

Arthritis & Rheumatism

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The interstitial collagens, type I and type 111, were investigated in lung tissue from patients with progressive systemic sclerosis (PSS) with pulmonary involvement. By use of CNBr digestion of whole tissue, the relative content of type I versus type I11 collagen was unchanged. This contrasts with idiopathic pulmonary fibrosis. Limited pepsin digestion released greater amounts of collagen (55%) than normal (16%), but the individual collagen chains were chemically indistinguishable. A reduced amount of the more stable collagen crosslink, hydroxylysinonorleucine, was observed which was consistent with the relatively greater degree of solubilization.Progressive systemic sclerosis (PSS) or systemic scleroderma is characterized by extensive fibrotic destruction of several organs associated with increased accumulation of collagen and other extracellular macromolecules in the involved tissues. Most commonly involved in the process is skin, but certain internal organs such as the lung, heart, kidney, and gastrointestinal tract are also frequently affected. The etiology and pathogenesis of this disorder are not completely understood.Theoretically, the increased accumulation of col- ~~From the Veterans Administration Medical Center and the

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Section: Discussionsupporting

confidence: 80%

Investigation of type i and type iii collagens of the lung in progressive systemic sclerosis

Seyer

Kang²,

Rodnan³

1981

Arthritis & Rheumatism

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“…Type I collagen was prepared in the laboratory from Sprague Dawley rat (Depre, St. Doulchard, France) tail tendons by 0.5 M acetic acid extraction (9) and used as native acid-soluble collagen or after pepsin digestion to remove telopeptides (10). Type I acid-soluble and pepsinized collagens used in this study were denatured by heating at 60°C for 30 min.…”

Section: Reagentsmentioning

confidence: 99%

Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

Garnotel

Rittié

Poitevin

et al. 2000

The Journal of Immunology

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“…These studies established that type I and type III collagen molecules are about the same length and have, except for three regions, a similar distribution of their charged polar amino acids. Recently, the peptides produced by CNBr cleavage of the a1(III) chains from humans (12,15) and calves (16) have been isolated and their molecular weights and compositions established. Nine peptides were isolated from the human protein and ten from the calf.…”

mentioning

confidence: 99%

“…EXPERIMENTAL Preparation of type III collagen from calf skin and the isolation of its CNBr peptides has been described in detail (16). Preparation of type III collagen, al(III-CB3, and al(III)CB8 from human skin followed the published procedure (15).…”

mentioning

confidence: 99%

Ordering of cyanogen bromide peptides of type III collagen based on their homology to type I collagen: preservation of sites for crosslink formation during evolution.

Fietzek¹,

Allmann²,

Rauterberg³

et al. 1977

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

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The order of the cyanogen-bromide-derived peptides from al(III) chains of pepsin-solubiliied calf skin collagen was found to be 3A-3B-3-74-61,8,24-9A-9B. The amino-acid sequences of the NHrterminal region of all peptides were determined by Edman's automated degradation procedure. The alignment of the peptides along the peptide chain was established by searching for the best homology between the partial sequences of the cyanogen bromide peptides from the al(III) chain and the completely known sequence of the al(I) chain. Characterization of three cyanogen-bromide-derived double peptides provided confirmation of the deduced order. A sequence Gly-Met-Hyl-Gly-His-Arg-Gly-Phe-was established near the NHrterminus and a sequence Gly-Ile-Hyl-Gly-HisArg-Gly-Phe near the COOH-terminus of the al(III) chain. Identical sequences have been found in the corresponding regions of the al(I) chain. They include hydroxylysine, a site for intermolecular crosslink formation. Because these sequences are conserved during evolution of the collagen molecule, they are probably important for collagen structure and function. Determination of the primary structure of the chains of various types of collagen is a formidable undertaking since each chain contains more than 1000 amino acids (1). However, the complete sequence of amino acids in the al chain of type I collagen is known (2), and about two-thirds of the sequence of amino acids in the a2 chain is also established (3). In such studies the chains are digested with cyanogen bromide (CNBr), the order of the peptides along the chain is deduced, and the detailed sequence analysis of the various peptides is carried through to completion.Work is now in progress to determine the sequence of al(III) chains. Type III collagen was first detected in fetal skin (4), but since then it has been found in a variety of tissues from humans, calves, chickens, and rabbits (4)(5)(6)(7)(8)(9)(10)(11)(12)

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Isolation and characterization of the cyanogen bromide peptides from the α(III)chain of human collagen

Cited by 164 publications

References 25 publications

Investigation of type i and type iii collagens of the lung in progressive systemic sclerosis

Investigation of type i and type iii collagens of the lung in progressive systemic sclerosis

Human Blood Monocytes Interact with Type I Collagen Through αxβ2 Integrin (CD11c-CD18, gp150-95)

Ordering of cyanogen bromide peptides of type III collagen based on their homology to type I collagen: preservation of sites for crosslink formation during evolution.

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