Secretion and matrix assembly of recombinant type VI collagen

Colombatti, Alfonso; Mucignat, Maria Teresa; Bonaldo, Paolo

doi:10.1016/0945-053x(94)90048-5

Cited by 37 publications

(48 citation statements)

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“…However, the RGD sequence does not compete with the ␣ M I domain as the GRGDSP peptide at a 1 mM concentration was unable to inhibit pro-MMP-9 binding to the I domain. 2 It will be interesting to see whether the DDGW peptide recognizes a positively and negatively charged sequence in the I domain.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Negatively Charged Peptide Motif within the Catalytic Domain of Progelatinases That Mediates Binding to Leukocyte β2 Integrins

Stefanidakis

Björklund²,

Ihanus

et al. 2003

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Identification of a Negatively Charged Peptide Motif within the Catalytic Domain of Progelatinases That Mediates Binding to Leukocyte β2 Integrins

Stefanidakis

Björklund²,

Ihanus

et al. 2003

Journal of Biological Chemistry

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“…2). In addition, CMP has type A-like domains that may be involved in cell adhesion (13). We therefore hypothesized that CMP may be an adhesion factor.…”

Section: Localization Of Cmp-conventional Immunohistochemistrymentioning

confidence: 99%

Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1

Makihira

Yan

Ohno³

et al. 1999

Journal of Biological Chemistry

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Cartilage matrix protein (CMP; also known as matrilin-1), one of the major noncollagenous proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10 -20 g/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin ␣ 1 or ␤ 1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin ␣ 2 , ␣ 3 , ␣ 5 , ␤ 2 , ␣ 5 ␤ 1 , or ␣ V ␤ 5 had little effect on cell adhesion or spreading. The antibody to integrin ␣ 1 , but not to other subunits, coprecipitated 125 I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin ␣ 1 subunit. Unlabeled CMP competed for the binding to integrin ␣ 1 with 125 I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin ␣ 1 ␤ 1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.Cartilage matrix protein (CMP 1 /matrilin-1) was originally isolated as a protein that binds to aggrecan and thereafter was shown to bind to type II collagen (1-3). CMP is synthesized in a cartilage-specific manner, except that eye tissues, notochord, and tendon express CMP at low levels (4 -7). The role of CMP is unknown, but it may have a structural role, modulating physical properties of cartilage, or may be involved in matrixcell interactions.CMP exists in vivo as a homotrimer of 148 kDa, as measured by sedimentation equilibrium centrifugation, although estimates of the molecular mass of this protein by SDS-polyacrylamide gel electrophoresis (PAGE) yield a higher value. CMP migrates at positions corresponding to 215 and 60 kDa under nonreducing and reducing conditions, respectively, during SDS-PAGE (2, 8). The subunits of CMP are connected in the C-terminal region by disulfide bonding and the presence of the coiled-coil ␣-helical assembly domain (9, 10). The monomer has two type A-like (von Willebrand factor-like or I) domains connected with an epidermal growth factor-like domain in addition to the short C-terminal domain (9,11,12). A type A-like domain is present in several proteins such as complement factors B and C2; type VI, XII, XIV, and XVI collagens; and ␣ subunits of several integrins (13). Some members of this protein family are involved in cell adhesion. However, whether CMP is an adhesion factor remains unknown.Numerous adhesion proteins are recognized by integrins, which are heterodimeric proteins with two (␣ and ␤) membrane-spanning subunits. The extracel...

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“…200 amino acids termed the I (inserted, interactive) domain [15,16]. The I domain shows sequence similarities to domains of von Willebrand factor, cartilage matrix protein, and complement factor B [9,10,17].…”

Section: Introductionmentioning

confidence: 99%

Purification and structural characterization of the CD11b/CD18 integrin α subunit I domain reveals a folded conformation in solution

Fairbanks¹,

Pollock²,

Prairie³

et al. 1995

FEBS Letters

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The a suhunits of the leukocyte CDlllCD18 integrins contain a ~200 amino acid 'inserted' or I domain. The I domain of the cell-surface Mac-1 (CD 11 b/CD18) integrin has been shown to be the major recognition site for several adhesion ligands, including iC3b, fibrinogen, factor X, and ICAM-1. The I domain from the Mac-1 a subunit has been expressed in Escherichia coli as a soluble GST-fusion protein containing a factor X" sensitive cleavage site. Analytical characterization of the purified I domain reveals that it is obtained in very high quality at high yields. CD and NMR spectra indicate that I domain adopts a predominantly folded structure in solution, independent of the remainder of the a subunit. Addition of Ca 2+ and Mg 2+ did not significantly perturb the structural conformation.

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Secretion and matrix assembly of recombinant type VI collagen

Cited by 37 publications

References 0 publications

Identification of a Negatively Charged Peptide Motif within the Catalytic Domain of Progelatinases That Mediates Binding to Leukocyte β2 Integrins

Identification of a Negatively Charged Peptide Motif within the Catalytic Domain of Progelatinases That Mediates Binding to Leukocyte β2 Integrins

Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1

Purification and structural characterization of the CD11b/CD18 integrin α subunit I domain reveals a folded conformation in solution

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