The Family of Collagen Genes

Vuorio, Eero; Crombrugghe, Benoít de

doi:10.1146/annurev.bi.59.070190.004201

Cited by 485 publications

(283 citation statements)

References 2 publications

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“…The amount of the type I collagen in an artery is regulated by the activities of matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (35). COL1A1 is the gene that encodes for the ␣1 chains of the triple helix type I collagen molecules (46). The homozygous collagenase-resistant Col1a1 mouse (Col1a1 R/R ) synthesizes collagen type I that is resistant to collagenase cleavage between Gly775 and Ile776 sites of the ␣1 chains, which is the site of action of human MMPs (28).…”

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confidence: 99%

The role of collagen in extralobar pulmonary artery stiffening in response to hypoxia-induced pulmonary hypertension

Ooi¹,

Wang²,

Tabima³

et al. 2010

American Journal of Physiology-Heart and Circulatory Physiology

113

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Chesler NC. The role of collagen in extralobar pulmonary artery stiffening in response to hypoxia-induced pulmonary hypertension. Am J Physiol Heart Circ Physiol 299: H1823-H1831, 2010. First published September 17, 2010 doi:10.1152/ajpheart.00493.2009.-Hypoxic pulmonary hypertension (HPH) causes extralobar pulmonary artery (PA) stiffening, which potentially impairs right ventricular systolic function. Changes in the extracellular matrix proteins collagen and elastin have been suggested to contribute to this arterial stiffening. We hypothesized that vascular collagen accumulation is a major cause of extralobar PA stiffening in HPH and tested our hypothesis with transgenic mice that synthesize collagen type I resistant to collagenase degradation (Col1a1 R/R ). These mice and littermate controls that have normal collagen degradation (Col1a1 ϩ/ϩ ) were exposed to hypoxia for 10 days; some were allowed to recover for 32 days. In vivo PA pressure and isolated PA mechanical properties and collagen and elastin content were measured for all groups. Vasoactive studies were also performed with U-46619, Y-27632, or calcium-and magnesium-free medium. Pulmonary hypertension occurred in both mouse strains due to chronic hypoxia and resolved with recovery. HPH caused significant PA mechanical changes in both mouse strains: circumferential stretch decreased, and mid-to-high-strain circumferential elastic modulus increased (P Ͻ 0.05 for both). Impaired collagen type I degradation prevented a return to baseline mechanical properties with recovery and, in fact, led to an increase in the low and mid-to-highstrain moduli compared with hypoxia (P Ͻ 0.05 for both). Significant changes in collagen content were found, which tended to follow changes in mid-to-high-strain elastic modulus. No significant changes in elastin content or vasoactivity were observed. Our results demonstrate that collagen content is important to extralobar PA stiffening caused by chronic hypoxia. biomechanics; mechanobiology; elastin; hydroxyproline; recovery HYPOXIC PULMONARY HYPERTENSION (HPH) is caused by living at high altitudes and is a complication of many lung diseases, including chronic obstructive pulmonary disease (1, 13, 16), cystic fibrosis (10), and obstructive sleep apnea (13), which contributes significantly to morbidity and mortality. Pulmonary vascular remodeling due to chronic HPH increases conduit pulmonary artery (PA) stiffness (4,20,21,23,34,42). Conduit PA stiffening likely increases wave reflections to impair right ventricular systolic function, much like aortic stiffening impairs left ventricular systolic function (18,29,33). Our laboratory has previously shown that HPH increases wave reflections in the mouse pulmonary circulation (44). Recent evidence showing that conduit PA stiffness is a strong predictor of mortality in PA hypertension (12, 30) further supports the importance of PA stiffness to pulmonary and right ventricular function.The dominant morphological changes in conduit PAs in response to HPH are accumulation of collagen and ...

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confidence: 99%

The role of collagen in extralobar pulmonary artery stiffening in response to hypoxia-induced pulmonary hypertension

Ooi¹,

Wang²,

Tabima³

et al. 2010

American Journal of Physiology-Heart and Circulatory Physiology

113

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“…Type I collagen is the most abundant protein of the extracellular matrix and is an important structural component in blood vessels, skin, tendons, ligaments, and bone (1). Accordingly, the synthesis and degradation of type I collagen is tightly regulated.…”

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Collagen Binding Properties of the Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Hemopexin C Domain

Tam

Butler

et al. 2002

Journal of Biological Chemistry

128

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“…The aminoterminal domain is largely responsible for the heparin binding properties of thrombospondins (4,5). The procollagen region contains a region homologous to a cysteine-rich domain in the NH 2 -terminal propeptide of the ␣ 1 -chain of type 1 procollagen (6). The type 1 repeats are homologous to sequences in a variety of proteins found in protozoans (7)(8)(9), invertebrates (10), and mammals (11)(12)(13)(14)(15)(16).…”

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Thrombospondin Type 1 Repeats Interact with Matrix Metalloproteinase 2

Bein

Simons

2000

Journal of Biological Chemistry

231

167

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Thrombospondins are thought to function as inhibitors of angiogenesis. However, the mechanism(s) of this activity is not well understood. In this study, we have used the yeast two-hybrid system to identify proteins that interact with the thrombospondins 1 (TSP1) and 2 (TSP2) properdin-like type 1 repeats (TSR). One of the proteins identified that interacted with both TSR was matrix metalloproteinase 2 (MMP2). The isolated MMP2 cDNA clone encoded amino acid residues 237-633, which include the fibronectin-like gelatin binding region flanking the catalytic center and the carboxyl hemopexin-like region. Further testing of this clone demonstrated that the TSR interacted with the NH 2 -terminal region of the MMP2 that contains the catalytic domain. The protein interaction observed in yeast was further demonstrated by immunoprecipitation and Western blotting using purified intact TSP1, TSP2, MMP2, and MMP9. Although MMP2 interacted with TSP1 and TSP2 via its gelatin-binding domain or a closely mapping site, neither TSP1 nor TSP2 was degraded by MMP2 in vitro. Tissue culture and in vitro assays demonstrated that the presence of purified TSR and intact TSP1 resulted in inhibition of MMP activity. The ability of TSP1 to inhibit MMP3-dependent activation of pro-MMP9 and thrombin-induced activation of pro-MMP2 suggests that the TSPs may inhibit MMP activity by preventing activation of the MMP2 and MMP9 zymogens.The thrombospondin (TSP) 1 family of proteins includes at least five related extracellular matrix glycoproteins encoded by separate genes (1). Each thrombospondin contains NH 2 -and COOH-terminal globular domains flanking different structural modules ( Ref. 2; Fig. 1A). The modules common to all TSP proteins include epidermal growth factor-like type 2 and Ca 2ϩ -binding type 3 repeats. In addition to these common features, TSP1 and TSP2 share two additional modules: a procollagen homology region and three properdin-like type 1 repeats (TSR).The NH 2 and COOH termini contain regions that are low in cysteine content, do not possess internal repeating motifs, and do not show homology with other proteins (3). The aminoterminal domain is largely responsible for the heparin binding properties of thrombospondins (4, 5). The procollagen region contains a region homologous to a cysteine-rich domain in the NH 2 -terminal propeptide of the ␣ 1 -chain of type 1 procollagen (6). The type 1 repeats are homologous to sequences in a variety of proteins found in protozoans (7-9), invertebrates (10), and mammals (11-16).Thrombospondin 1 has been the most extensively studied TSP protein to date. TSP1 contains a growing number of sites that have been implicated in interactions with more than 30 cell surface and matrix proteins, including structural proteins (e.g. collagen and fibronectin), cell surface receptors (e.g. integrins, syndecans, and CD36), enzymes (e.g. elastase and plasmin), and cytokines (e.g. transforming growth factor-␤1) (17). Because of its ability to interact with such a wide variety of proteins, TSP1 has been implicat...

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The Family of Collagen Genes

Cited by 485 publications

References 2 publications

The role of collagen in extralobar pulmonary artery stiffening in response to hypoxia-induced pulmonary hypertension

The role of collagen in extralobar pulmonary artery stiffening in response to hypoxia-induced pulmonary hypertension

Collagen Binding Properties of the Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Hemopexin C Domain

Thrombospondin Type 1 Repeats Interact with Matrix Metalloproteinase 2

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