Quantitation of type I, III, and V collagens in human tissue samples by high-performance liquid chromatography of selected cyanogen bromide peptides

Miller, Edward J.; Furuto, Donald K.; Narkates, A. J.

doi:10.1016/0003-2697(91)90116-b

Cited by 30 publications

(7 citation statements)

References 31 publications

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“…In an early study of HPH in rats, the mRNA level of proα1(I) collagen in extralobar PAs was found to peak at 3 days after the onset of hypoxia (Poiani et al 1990b), suggesting an increase in type I collagen during HPH development; but the type III collagen mRNA was not examined. The ratio of type I to III collagen was quite consistent (2.3:1) between exposures (normoxia, hypoxia or hypoxia+BAPN) in Col1a1 +/+ mice, which agrees with our previous observation in mouse main PAs (Estrada and Chesler 2009) and other reports on systemic arteries (Halme et al 1986; Leushner and Haust 1986; Miller et al 1991). Because of the smaller percentage of type III collagen in PAs, the changes in collagen content and cross-linking with HPH only reached statistical significance for type I collagen in these mice (Fig 1).…”

Section: Discussionsupporting

confidence: 92%

Effects of collagen deposition on passive and active mechanical properties of large pulmonary arteries in hypoxic pulmonary hypertension

Wang

Lakes

Eickhoff

et al. 2013

Biomech Model Mechanobiol

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Proximal pulmonary artery (PA) stiffening is a strong predictor of mortality in pulmonary hypertension. Collagen accumulation is mainly responsible for PA stiffening in hypoxia-induced pulmonary hypertension (HPH) in mouse models. We hypothesized that collagen cross-linking and the type I isoform are the main determinants of large PA mechanical changes during HPH, which we tested by exposing mice that resist type I collagen degradation (Col1a1R/R) and littermate controls (Col1a1+/+) to hypoxia for 10 days with or without β-aminopropionitrile (BAPN) treatment to prevent cross-link formation. Static and dynamic mechanical tests were performed on isolated PAs with smooth muscle cells (SMC) in passive and active states. Percentages of type I and III collagen were quantified by histology; total collagen content and cross-linking were measured biochemically. In the SMC passive state, for both genotypes, hypoxia tended to increase PA stiffness and damping capacity, and BAPN treatment limited these increases. These changes were correlated with collagen cross-linking (p<0.05). In the SMC active state, hypoxia increased PA dynamic stiffness and BAPN had no effect in Col1a1+/+ mice (p<0.05). PA stiffness did not change in Col1a1R/R mice. Similarly, damping capacity did not change for either genotype. Type I collagen accumulated more in Col1a1+/+ mice whereas type III collagen increased more in Col1a1R/R mice during HPH. In summary, PA passive mechanical properties (both static and dynamic) are related to collagen cross-linking. Type I collagen turnover is critical to large PA remodeling during HPH when collagen metabolism is not mutated and type III collagen may serve as a reserve.

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Section: Discussionsupporting

confidence: 92%

Effects of collagen deposition on passive and active mechanical properties of large pulmonary arteries in hypoxic pulmonary hypertension

Wang

Lakes

Eickhoff

et al. 2013

Biomech Model Mechanobiol

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“…It is generally less abundant than collagen I, except in the walls of distensible organs and blood vessels [10], but its fibril cross-links and proteoglycan-rich matrix contribute mechanical strength and distensibility [11]. Collagen III also participates in a variety of biological functions.…”

Section: Introductionmentioning

confidence: 99%

The collαgen III fibril has a “flexi-rod” structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

et al. 2017

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Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a “flexi-rod” structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule’s prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.

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“…To this solution approximately 0.5 mg of CNBr was added (21). Reaction times of 1, 3, and 72 h were tested simultaneously to achieve complete and selective cleavage at methionine.…”

Section: Methodsmentioning

confidence: 99%

Biochemical Structural Analysis of the Lantibiotic Mutacin II

Krull¹,

Chen²,

Novák³

et al. 2000

Journal of Biological Chemistry

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Mutacin II is a post-translationally modified lantibiotic peptide secreted by Streptococcus mutans T8, which inhibits the energy metabolism of sensitive cells. The deduced amino acid sequence of promutacin II is NRW-WQGVVPTVSYECRMNSWQHVFTCC, which is capable of forming three thioether bridges. It was not obvious, however, how the three thioether bridges are organized. To examine the bridging, the cyanogen bromide cleavage products of mutacin II and its variants generated by protein engineering, C15A, C26A, and C15A/C26A, were analyzed by mass spectrometry. Analysis of the wild type molecule and the C15A variant excluded several possibilities and also indicated a high fidelity of formation of the thioether bridges. This allowed us to further resolve the structure by analysis (mass spectrometry and tandem mass spectrometry) of the cyanogen bromide cleavage fragments of the C26A and C15A/C26A mutants. Nuclear magnetic resonance analysis established the presence of one and two dehydrobutyrine residues in mutacin II and the C15A variant, respectively, thus yielding the final structure. The results of this investigation showed that the C-terminal part contains three thioether bridges connecting Cys residues 15, 26, and 27 to Ser/Thr residues 10, 12 and 19, respectively, with Thr 25 being modified to dehydrobutyrine.

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Quantitation of type I, III, and V collagens in human tissue samples by high-performance liquid chromatography of selected cyanogen bromide peptides

Cited by 30 publications

References 31 publications

Effects of collagen deposition on passive and active mechanical properties of large pulmonary arteries in hypoxic pulmonary hypertension

Effects of collagen deposition on passive and active mechanical properties of large pulmonary arteries in hypoxic pulmonary hypertension

The collαgen III fibril has a “flexi-rod” structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles

Biochemical Structural Analysis of the Lantibiotic Mutacin II

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