Type XXIII Collagen, a New Transmembrane Collagen Identified in Metastatic Tumor Cells

Banyard, Jacqueline; Bao, Lidao; Zetter, Bruce R.

doi:10.1074/jbc.m210616200

Cited by 88 publications

(84 citation statements)

References 30 publications

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“…Because most members of the group contain a furin consensus sequence within the linker region, furin has been proposed as the relevant sheddase (12,(17)(18)(19)(20)(21)(22). However, processing of collagen XVII is more complex and will be discussed below in more detail.…”

Section: Structure and Functions Of Collagenousmentioning

confidence: 99%

“…Collagen XXIII-The cDNA for human collagen XXIII predicts a 540-amino acid polypeptide, which consists of an N-terminal cytoplasmic domain of 24 amino acids, a transmembrane stretch, and an extracellular domain of 481 amino acids with three collagenous domains flanked by short non-collagenous sequences (20). Thus, collagen XXIII shows structural homology with collagens XIII and XXV.…”

Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

“…2 Recombinant collagen XXIII is synthesized as a ϳ75-kDa protein, which can be released from the cell surface by furin-mediated proteolysis. The cleavage produces a 60-kDa soluble ectodomain that forms a multimeric complex, which binds heparin with low affinity (20).…”

Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

See 2 more Smart Citations

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke

Brückner

Bruckner‐Tuderman

2005

Journal of Biological Chemistry

150

138

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Section: Structure and Functions Of Collagenousmentioning

confidence: 99%

Section: Other Collagenous Transmembrane Proteins Andmentioning

confidence: 99%

See 1 more Smart Citation

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Franzke

Brückner

Bruckner‐Tuderman

2005

Journal of Biological Chemistry

150

138

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“…Similar domains occur in collagen XXIII (33), the Alzheimer amyloid plaque component precursor CLAC-P/collagen XXV (34) and the collagen-like membrane proteins MARCO and ectodysplasin-A1 (31). In all of these proteins, the transmembrane domain is found close to the N terminus and is followed immediately by a heptad repeat region at the beginning of the large ectodomain.…”

mentioning

confidence: 99%

α-Helical Coiled-coil Oligomerization Domains Are Almost Ubiquitous in the Collagen Superfamily

McAlinden

Smith

Sandell

et al. 2003

Journal of Biological Chemistry

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␣-Helical coiled coils are widely occurring protein oligomerization motifs. Here we show that most members of the collagen superfamily contain short, repeating heptad sequences typical of coiled coils. Such sequences are found at the N-terminal ends of the C-propeptide domains in all fibrillar procollagens. When fused C-terminal to a reporter molecule containing a collagen-like sequence that does not spontaneously trimerize, the Cpropeptide heptad repeats induced trimerization. C-terminal heptad repeats were also found in the oligomerization domains of the multiplexins (collagens XV and XVIII). N-terminal heptad repeats are known to drive trimerization in transmembrane collagens, whereas fibril-associated collagens with interrupted triple helices, as well as collagens VII, XIII, XXIII, and XXV, were found to contain heptad repeats between collagen domains. Finally, heptad repeats were found in the von Willebrand factor A domains known to be involved in trimerization of collagen VI, as well as in collagen VII. These observations suggest that coiled-coil oligomerization domains are widely used in the assembly of collagens and collagen-like proteins.The mechanisms controlling chain oligomerization in extracellular matrix and related proteins are currently topics of active research (1, 2). In the case of the collagen superfamily, which includes both collagens and collagen-like proteins (3-5), a number of structural features have been identified that are essential for bringing together component polypeptide chains with the correct stoichiometry, thus leading to folding of the triple helix. Early studies on the procollagen precursors of the fibrillar collagens (types I-III, V, and XI) (6) showed that the C-propeptide regions are necessary to direct correct chain association, which is followed by zipper-like folding of the triple helix in the C-to N-terminal direction (7). This concept was subsequently extended to basement membrane collagen type IV (8 -10), microfibril-forming collagen VI (11, 12), members of the C1q family (13) including collagens VIII and X (14 -17) and the emilins (18), and the FACITs 1 (19 -21).␣-Helical coiled coils have been shown to be oligomerization domains in both collagens and collagen-like proteins. The paradigm here is the collectin family (22), which includes the lung surfactant proteins (SP-A and SP-D), mannan-binding proteins (MBP-A and MBP-C), conglutinin, and collectin-43. Collectins are trimeric molecules in which each chain contains a collagenlike domain followed by an ␣-helical coiled-coil region and then a carbohydrate recognition domain (CRD). The amino acid sequence of the coiled-coil domain is characterized by up to four heptad repeats (a-b-c-d-e-f-g) in which hydrophobic amino acid residues occur at positions a and d (23). Three-dimensional structures of the coiled-coil and CRD regions in MBP and SP-D show that chains within the trimer are associated via a threestranded coiled coil, with the three CRDs arranged as distinct lobes (24 -26). Several studies have shown that the co...

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“…Collagen XXIII forms homotrimers consisting of a short intracellular domain, a single-pass transmembrane domain and three extracellular collagen domains interrupted by short noncollagenous sequences (3,4). It exists either as a full-length, membrane-anchored protein or as a soluble ectodomain.…”

mentioning

confidence: 99%

Collagen XXIII, Novel Ligand for Integrin α2β1 in the Epidermis

Veit

Zwolanek

Eckes

et al. 2011

Journal of Biological Chemistry

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Cellular receptors for collagens belong to the family of ␤ 1 integrins. In the epidermis, integrin ␣ 2 ␤ 1 is the only collagenbinding integrin present. Its expression is restricted to basal keratinocytes with uniform distribution on the cell surface of those cells. Although ␣ 2 ␤ 1 receptors localized at the basal surface interact with basement membrane proteins collagen IV and laminin 111 and 332, no interaction partners have been reported for these integrin molecules at the lateral and apical membranes of basal keratinocytes. Solid phase binding and surface plasmon resonance spectroscopy demonstrate that collagen XXIII, a member of the transmembrane collagens, directly interacts with integrin ␣ 2 ␤ 1 in an ion-and conformation-dependent manner. The two proteins co-localize on the surface of basal keratinocytes. Furthermore, collagen XXIII is sufficient to induce adhesion and spreading of keratinocytes, a process that is significantly reduced in the absence of functional integrin ␣ 2 ␤ 1 .Collagen XXIII belongs to the class of transmembrane collagens in type II orientation, which comprises the collagens XIII, XVII, XXIII, and XXV and other related proteins such as ectodysplasin A, class A macrophage scavenger receptors, and the colmedins (1, 2). Collagen XXIII forms homotrimers consisting of a short intracellular domain, a single-pass transmembrane domain and three extracellular collagen domains interrupted by short noncollagenous sequences (3, 4). It exists either as a full-length, membrane-anchored protein or as a soluble ectodomain. The proteolytic processing releasing the ectodomain is mediated by furin and is regulated by the plasma membrane microenvironment (5). Collagen XXIII is expressed in the epidermis and other epithelia such as those in the tongue, gut, and lung but also in the brain and kidney (4). In prostate, collagen XXIII expression was shown to correlate with tumor progression (6).Four integrins, ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , ␣ 10 ␤ 1 , and ␣ 11 ␤ 1 bind native collagens (7). This ␤ 1 subunit-containing subclass of integrins is characterized by the presence of an inserted domain (I domain) with homology to von Willebrand factor A domains in their ␣-subunit, which harbors the ligand-binding site (8, 9). The integrins ␣ 10 ␤ 1 and ␣ 11 ␤ 1 have a restricted expression pattern on differentiated chondrocytes and developing muscle cells (10, 11), whereas ␣ 1 ␤ 1 and ␣ 2 ␤ 1 show a broader distribution, with integrin ␣ 1 ␤ 1 being predominantly expressed by cells of mesenchymal origin and integrin ␣ 2 ␤ 1 by epithelial cells and platelets. In vitro studies suggested an implication of integrin ␣ 2 ␤ 1 in cell attachment and migration (12, 13), generation of mechanical forces and contraction of collagen matrices (14), induction of collagenase activity and matrix remodeling (15, 16), as well as angiogenesis (17) and epithelial branching morphogenesis (18). Mice lacking the integrin ␣ 2 subunit exhibit defects in mammary gland branching morphogenesis (19), delayed platelet aggregation and formation of unstable t...

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Type XXIII Collagen, a New Transmembrane Collagen Identified in Metastatic Tumor Cells

Cited by 88 publications

References 30 publications

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

Collagenous Transmembrane Proteins: Recent Insights into Biology and Pathology*

α-Helical Coiled-coil Oligomerization Domains Are Almost Ubiquitous in the Collagen Superfamily

Collagen XXIII, Novel Ligand for Integrin α2β1 in the Epidermis

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