Collagens

Gordon, Marion K.; Hahn, Rita A.

doi:10.1007/s00441-009-0844-4

Cited by 489 publications

(387 citation statements)

References 77 publications

(77 reference statements)

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“…Collagen fibrils regulate mineral deposition and growth (Murshed et al, 2005). FACIT collagens, including type XII collagen, play a role in collagen fibril formation by providing specific molecular bridges between fibrils and other matrix components (Gordon and Olsen, 1990;van der Rest and Garrone, 1991;Gordon and Hahn, 2010;Birk and Brückner, 2011). In this study, although the expression of type I collagen did not change, the absence of type XII collagen decreased bone matrix proteins such as osteocalcin and osteopontin.…”

Section: Discussionmentioning

confidence: 53%

Type XII collagen regulates osteoblast polarity and communication during bone formation

Izu¹,

Sun²,

Zwolanek³

et al. 2011

J Exp Med

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Abbreviations used in this paper: CT, computed tomography; FACIT, fibrilassociated collagen with interrupted triple helices; HA, hydroxyapatite; H&E, hematoxylin and eosin; HU, Hounsfield unit; shRNA, short hairpin RNA; TMDn, tissue mineral density; TRAP, tartrate resistance acid phosphatase. IntroductionOsteoblast differentiation and maturation are crucial events in the formation of new bone and determination of bone quality (Nakashima et al., 2002;Yoshida et al., 2002;Komori, 2010). Bone formation begins with the differentiation of osteoblasts from pluripotent mesenchymal cells. The progenitors migrate to the sites of bone matrix deposition and differentiate into fully functional, bone matrix-producing osteoblasts (Imai et al., 1998). These events are regulated by the expression of runtrelated gene 2 (Runx2, also known as Cbfa1) and sp7 transcription factor (Sp7, also known as osterix) and by canonical Wnt signaling followed by the secretion of specific bone matrix proteins such as type I collagen (Col1a1), secreted phosphoprotein1 (Spp1, also known as osteopontin), integrin-binding sialoprotein (Ibsp), and bone -carboxyglutamate protein (Bglap, also known as osteocalcin; Harada and Rodan, 2003;Koga et al., 2005). In addition to these changes in gene expression and matrix protein secretion, the mature osteoblasts become aligned along regions of bone deposition with an epithelioid arrangement. The mature, terminally differentiated osteoblasts are highly polarized relative to the site of bone matrix deposition (Ilvesaro et al., 1999;Nakashima et al., 2002;Stains et al., 2002). These features are common to periosteal and endosteal bone and both long and flat bones. Therefore, the alignment, polarization, and interaction of osteoblasts are important events necessary for production of a functional bone matrix.Cell motility, communication, and shape are controlled via the local microenvironment where the extracellular matrix provides a substrate for cell anchorage, stores and presents growth factors or cytokines, and serves as a tissue scaffold (Rozario and DeSimone, 2010). The extracellular matrix interacts with the intracellular actin cytoskeleton via transmembrane proteins that affect cytoskeletal organization, cell motility and polarity, proliferation, and survival (Berthiaume et al., 1996;Geiger et al., 2001;Théry et al., 2005;Parsons et al., 2010;Kim et al., 2011). Thus, extracellular matrix-transmembrane protein-cytoskeleton D ifferentiated osteoblasts are polarized in regions of bone deposition, demonstrate extensive cell interaction and communication, and are responsible for bone formation and quality. Type XII collagen is a fibril-associated collagen with interrupted triple helices and has been implicated in the osteoblast response to mechanical forces. Type XII collagen is expressed by osteoblasts and localizes to areas of bone formation. A transgenic mouse null for type XII collagen exhibits skeletal abnormalities including shorter, more slender long bones with decreased mechanical strength as well as a...

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Section: Discussionmentioning

confidence: 53%

Type XII collagen regulates osteoblast polarity and communication during bone formation

Izu¹,

Sun²,

Zwolanek³

et al. 2011

J Exp Med

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“…Altered collagen remodeling is involved in disease states such as arthritis, periodontitis, atherosclerosis, and tumor metastasis (1)(2)(3)(4). Of the 29 known collagens, types I-III are the most abundant (5,6). Although these interstitial fibrillar collagens possess a similar length supersecondary triple-helical structure, differences in sequence, tissue distribution, and glycosylation patterns have been well documented (5,7).…”

mentioning

confidence: 99%

Exosite Interactions Impact Matrix Metalloproteinase Collagen Specificities

Robichaud

Steffensen

Fields

2011

Journal of Biological Chemistry

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Members of the matrix metalloproteinase (MMP) family selectively cleave collagens in vivo. However, the substrate structural determinants that facilitate interaction with specific MMPs are not well defined. We hypothesized that type I-III collagen sequences located N-or C-terminal to the physiological cleavage site mediate substrate selectivity among MMP-1, MMP-2, MMP-8, MMP-13, and MMP-14/membrane-type 1 (MT1)-MMP. The enzyme kinetics for hydrolysis of three fluorogenic triple-helical peptides (fTHPs) was evaluated herein. The first fTHP contained consensus residues 769 -783 from type I-III collagens, the second inserted ␣1(II) collagen residues 763-768 N-terminal to the consensus sequence, and the third inserted ␣1(II) collagen residues 784 -792 C-terminal to the consensus sequence. Our analyses showed that insertion of the C-terminal residues significantly increased k cat /K m and k cat for MMP-1. MMP-13 showed the opposite behavior with a decreased k cat /K m and k cat and a greatly improved K m in response to the C-terminal residues. Insertion of the N-terminal residues enhanced k cat /K m and k cat for MMP-8 and MT1-MMP. For MMP-2, the C-terminal residues enhanced K m and dramatically decreased k cat , resulting in a decrease in the overall activity. These changes in activities and kinetic parameters represented the collagen preferences of MMP-8, MMP-13, and MT1-MMP well. Thus, interactions with secondary binding sites (exosites) helped direct the specificity of these enzymes. However, MMP-1 collagen preferences were not recapitulated by the fTHP studies. The preference of MMP-1 for type III collagen appears to be primarily based on the flexibility of the hydrolysis site of type III collagen compared with types I and II. Further characterization of exosite determinants that govern interactions of MMPs with collagenous substrates should aid the development of pharmacotherapeutics that target individual MMPs.

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“…Collagens -the structural main components in joints -are extracellular matrix molecules used by cells for structural integrity and with a variety of other functions. About 28 different collagens have been identified in mammals and humans [28]. The typical mature collagen molecule consists of three single collagen polypep-tide chains, so called alpha (α) chains, which coil into a helical molecule [28].…”

Section: Type I and Type Ii Collagensmentioning

confidence: 99%

“…About 28 different collagens have been identified in mammals and humans [28]. The typical mature collagen molecule consists of three single collagen polypep-tide chains, so called alpha (α) chains, which coil into a helical molecule [28]. The different types of collagen are formed from a combination of more than 45 distinct collagen α polypeptide chains [28].…”

Section: Type I and Type Ii Collagensmentioning

confidence: 99%

Role of Cysteine Cathepsins in Joint Inflammation and Destruction in Human Rheumatoid Arthritis and Associated Animal Models

Schurigt¹

2013

Innovative Rheumatology

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Collagens

Cited by 489 publications

References 77 publications

Type XII collagen regulates osteoblast polarity and communication during bone formation

Type XII collagen regulates osteoblast polarity and communication during bone formation

Exosite Interactions Impact Matrix Metalloproteinase Collagen Specificities

Role of Cysteine Cathepsins in Joint Inflammation and Destruction in Human Rheumatoid Arthritis and Associated Animal Models

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