Type XIII collagen: a novel cell adhesion component present in a range of cell–matrix adhesions and in the intercalated discs between cardiac muscle cells

Hägg, Pasi; Väisänen, Timo; Tuomisto, Anne; Rehn, Marko; Tu, Hongmin; Huhtala, Pirkko; Eskelinen, Sinikka; Pihlajaniemi, Taina

doi:10.1016/s0945-053x(00)00119-0

Cited by 72 publications

(66 citation statements)

References 44 publications

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“…It occurs at cellular junctions and cell-matrix interaction sites in epithelial, mesenchymal, and neural tissues. In cultured fibroblasts, collagen XIII is a component of focal adhesions (6). It interacts with the collagen-binding integrin ␣ 1 ␤ 1 as well as with the matrix macromolecules fibronectin, nidogen-2, perlecan, and heparin, suggesting involvement in multiple cell-matrix interactions (5, 7).…”

Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke

Brückner

Bruckner‐Tuderman

2005

Journal of Biological Chemistry

151

138

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Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke

Brückner

Bruckner‐Tuderman

2005

Journal of Biological Chemistry

151

138

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“…Samples were analyzed by SDS-PAGE followed by Western blotting with anti-human type XIII collagen antibodies XIII/NC2-55 (6), XIII/NC3-1 (11), and XIII/NC4-SO (6) and anti-mouse type XIII collagen antibody XIII/NC1-Q610 (2).…”

Section: Analysis Of Recombinant Proteins Produced In Insect Cells Bymentioning

confidence: 99%

“…1-3), XIII/NC2-55 (lanes 4 -6), XIII/NC3-1 (lanes 7-9), and XIII/NC4-SO (lanes 10 -12). Lanes 1,4,7, and 10 refer to del1-38 samples; lanes 2,5,8, and 11 to del1-61 samples; and lanes 3,6,9, and 12 to del1-83 samples, all digested with pepsin. B provides a schematic presentation of the pepsin-resistant fragments of the variants del1-38, del1-61, and del1-83 and the antibodies used, and the location of the cysteine residues (C).…”

Section: Secretion Of Type XIII Collagen Molecules Expressed In Insectmentioning

confidence: 99%

“…It is located in focal adhesions of cultured fibroblasts and other cells and in adhesive structures of tissues such as the myotendinous junctions in muscle, intercalated discs in heart, and the cell basement membrane interphases (1,2). The type XIII collagen ectodomain can bind to fibronectin, heparin, the basement membrane components nidogen-2 and perlecan, and the ␣ 1 -subunit of integrin (3)(4)(5).…”

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confidence: 99%

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Type XIII Collagen and Some Other Transmembrane Collagens Contain Two Separate Coiled-coil Motifs, Which May Function as Independent Oligomerization Domains

Latvanlehto¹,

Snellman²,

et al. 2003

Journal of Biological Chemistry

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Type XIII collagen is a homotrimeric transmembrane collagen composed of a short intracellular domain, a single membrane-spanning region, and an extracellular ectodomain with three collagenous domains (COL1-3) separated by short non-collagenous domains (NC1-4). Several collagenous transmembrane proteins have been found to harbor a conserved sequence next to their membrane-spanning regions, and in the case of type XIII collagen this sequence has been demonstrated to be important for chain association. We show here that this 21-residue sequence is necessary but not sufficient for NC1 association. Furthermore, the NC1 association region was predicted to form an ␣-helical coiled-coil structure, which may already begin at the membrane-spanning region, as is also predicted for the related collagen types XXIII and XXV. Interestingly, a second coiled-coil structure is predicted to be located in the NC3 domain of type XIII collagen and in the corresponding domains of types XXIII and XXV. It is found experimentally that the absence of the NC1 coiled-coil domain leads to a lack of disulfide-bonded trimers and misfolding of the membrane-proximal collagenous domain COL1, whereas the COL2 and COL3 domains are correctly folded. We suggest that the NC1 coiled-coil domain is important for association of the N-terminal part of the type XIII collagen ␣ chains, whereas the NC3 coiled-coil domain is implicated in the association of the C-terminal part of the molecule. All in all, we propose that two widely separated coiled-coil domains of type XIII and related collagens function as independent oligomerization domains participating in the folding of distinct areas of the molecule.Type XIII collagen is a type II transmembrane protein that is expressed in many tissues throughout development and adult life (1). It is located in focal adhesions of cultured fibroblasts and other cells and in adhesive structures of tissues such as the myotendinous junctions in muscle, intercalated discs in heart, and the cell basement membrane interphases (1, 2). The type XIII collagen ectodomain can bind to fibronectin, heparin, the basement membrane components nidogen-2 and perlecan, and the ␣ 1 -subunit of integrin (3-5). Due to its location at the tissue and cell level and its binding properties, it has been postulated that type XIII collagen is involved in cellular adhesion and migration.Type XIII collagen ␣ chains produced in a recombinant insect cell culture system have been shown to form homotrimers (6). The primary structure is composed of three collagenous domains (COL1 1 to COL3), which are flanked and interrupted by non-collagenous domains (NC1 to NC4). The short cytosolic domain and the transmembrane domain encompass about half of the NC1 domain, whereas the rest of the molecule forms the ectodomain, which is a rod of about 150 nm with two flexible hinges coinciding with the NC2 and NC3 domains (5). The primary structures of COL1, NC2, COL3, and NC4 can vary, on account of complex alternative splicing (7-10). It has been shown recently that ext...

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“…9,14 Immunohistochemical studies of mature human and mouse tissues have shown that this collagen is located at many cell-matrix adhesion sites, eg, the myotendinous junctions and at cell-cell adhesion sites. 15 Type XIII collagen is expressed throughout mouse fetal development, with a clear increase toward the time of birth and strongest initial expression in the developing nervous system and heart. As development proceeds, it is found in developing bone, cartilage, intestine, skeletal muscle, lung, and skin, with clear developmental shifts in expression pattern.…”

mentioning

confidence: 99%

Lack of Cytosolic and Transmembrane Domains of Type XIII Collagen Results in Progressive Myopathy

Kvist¹,

Latvanlehto²,

Sund³

et al. 2001

The American Journal of Pathology

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Type XIII collagen is a type II transmembrane protein found at many sites of cell adhesion in tissues. Homologous recombination was used to generate a transgenic mouse line (Col13a1 N/N ) that expresses N-terminally altered type XIII collagen molecules lacking the short cytosolic and transmembrane domains but retaining the large collagenous ectodomain. The mutant molecules were correctly transported to focal adhesions in cultured fibroblasts derived from the Col13a1 N/N mice, but the cells showed decreased adhesion when plated on type IV collagen. These mice were viable and fertile, and in immunofluorescence stainings the mutant protein was located in adhesive tissue structures in the same manner as normal ␣1(XIII) chains. In immunoelectron microscopy of wild-type mice type XIII collagen was detected at the plasma membrane of skeletal muscle cells whereas in the mutant mice the protein was located in the adjacent extracellular matrix. Affected skeletal muscles showed abnormal myofibers with a fuzzy plasma membrane-basement membrane interphase along the muscle fiber and at the myotendinous junctions, disorganized myofilaments, and streaming of z-disks. The findings were progressive and the phenotype was aggravated by exercise. Thus type XIII collagen seems to participate in the linkage between muscle fiber and basement membrane, a function impaired by lack of the cytosolic and transmembrane domains. The collagen superfamily of proteins consists of more than 19 types of collagen and several other proteins with collagen-like domains.1 Type XIII collagen and the hemidesmosomal component type XVII collagen form a subfamily of transmembrane collagens. 2 The genes of human and mouse type XIII collagen are 135 to 138 kb in size, consisting of 42 exons, and they are localized to chromosome 10 in both species.3-5 The encoded type XIII collagen consists of three collagenous domains (COL1 to COL3) separated and flanked by four noncollagenous domains (NC1 to NC4). 6,7 The precursor RNAs that encode type XIII collagen undergo complex alternative splicing, which is predicted to affect the structures of the COL1, NC2, and COL3 domains of the human and mouse chains. 5,6,8 -10 Type XIII collagen produced in insect cells forms ␣1(XIII) homotrimers, and the three collagenous domains fold into a stable triple-helical conformation. 11 The type XIII collagen molecules have been shown to reside on the plasma membranes of cells in a type II orientation with a short N-terminal cytosolic portion, a transmembrane domain, and an extensive collagenous ectodomain.12 Sequences that are important for association of the three ␣1(XIII) chains reside in the Nterminal region, and hence triple helix formation is thought to proceed from the N terminus to the C terminus, in the opposite orientation to that known to occur in the fibrillar collagens.12 The extracellular ligands of type XIII collagen have not been identified, but recent studies with recombinant protein demonstrate that its ectodomain interacts strongly with the I domain of ␣1 integrin. ...

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Type XIII collagen: a novel cell adhesion component present in a range of cell–matrix adhesions and in the intercalated discs between cardiac muscle cells

Cited by 72 publications

References 44 publications

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Type XIII Collagen and Some Other Transmembrane Collagens Contain Two Separate Coiled-coil Motifs, Which May Function as Independent Oligomerization Domains

Lack of Cytosolic and Transmembrane Domains of Type XIII Collagen Results in Progressive Myopathy

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