Identification of a previously unknown human collagen chain, alpha 1(XV), characterized by extensive interruptions in the triple-helical region.

Myers, Jeanne C.; Kivirikko, Sirpa; Gordon, Marion K.; Dion, Arnold S.; Pihlajaniemi, Taina

doi:10.1073/pnas.89.21.10144

Cited by 63 publications

(62 citation statements)

References 35 publications

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“…The published al(XV) sequence (13) does not extend to the translational stop codon, making a comparison between the NC1 domains of al(XVIII) and al(XV) not possible, based on the published sequence. Screening of a human placenta cDNA library, however, resulted in clones that extended into the 3' untranslated region of al(XV) (Fig.…”

Section: Al(xvim) and Al(xv) Cobgens Belong To A Subfamily Ofmentioning

confidence: 99%

“…If these sequences are indeed utilized for attachment of glycosaminoglycans, al(XVIII) collagen would be an additional member of a growing group of known collagen-proteoglycans, including types IX and XII collagens (7,9,(20)(21)(22). Also, al(XV) collagen contains potential sites for N-and 0-linked glycosylation (13).…”

Section: Cctggtcctccaggtcccccaggagccatggctgciggtgagggaggtggccacataccamentioning

confidence: 99%

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Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.

Kamagata

Muragaki

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

161

139

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We have isolated overlapping mouse cDNAs encoding a collagenous polypeptide that we have d ated al(XVI) collagen. Nucleotide sequence analysis shows that al(XVI) collagen contains 10 triple-helical domains separated and flanked by non-triple-helical regions. Within the non-triple-helical regions, there are several Ser-Gly-containing sequences that conform to consensus sequences for glycosaminoglycan attachment sites in proteoglycan core proteins.Northern blots show that al(XVIM) transcripts are present in multiple organs, with the highest levels in liver, lung, and kidney. We have also isolated overlapping cDNAs encoding human al(XV) collagen, and their sequence extends a published partial al(XV) sequence to the 3' end. Comparison of the al(XV) and al(XVIM) sequences reveals a strking similarity in the lengths of the six most carboxyl-terminal triplehelical domains. In addition, within the carboxyl non-triplehelical domain NC1 of the two chains, a region of 177 amino acid residues shows about 60% identity at the amino acid level.We suggest, therefore, that al(XV) and al(XVIM) collagens are structurly related. Their structure is different from that of other known collagen ypes. We conclude that they belong to a subfamily of extracellular matrix proteins and we suggest the degnation multiplexins (for protein with multiple triple-helix domains and jterrptions) for members of this subfamily.The ability of collagenous proteins to form structures of high tensile strength is based on the rigid structure of collagen molecules. Collagen polypeptides contain one or more blocks of Gly-Xaa-Yaa repeats, in which Yaa frequently represents a proline or hydroxyproline residue. The presence of such sequence repeats allows groups of three polypeptides to fold into triple-helical domains which are rigid and inextensible. The use of such triple-helical domains was initially thought to be limited to molecules that make up collagen fibrils in tissues, but it is now known that such domains are present in a large number of proteins. Most of these proteins are found in the extracellular matrix and serve a structural role; thus they are considered members of the collagen superfamily of proteins. Within the superfamily of collagens, the fibrillar collagens represent a distinct family. Their triple-helical domains polymerize in a staggered fashion to form fibrils (1-3).Members of other collagen families do not by themselves form cross-striated fibrils but may be associated with fibrils (fibril-associated collagens with interrupted triple helices, FACIT) (4) or form their own distinct polymers (5, 6). The lengths as well as the number of triple-helical domains within molecules of nonfibrillar collagens are frequently quite different from those of triple-helical domains in fibrillar collagens.The non-triple-helical domains that separate triple-helical domains in some nonfibrillar collagens represent regions of flexibility. For example, in types IX, XII, and XIV collagens, non-triple-helical hinges allow triple-helical domains on eith...

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Section: Al(xvim) and Al(xv) Cobgens Belong To A Subfamily Ofmentioning

confidence: 99%

Section: Cctggtcctccaggtcccccaggagccatggctgciggtgagggaggtggccacataccamentioning

confidence: 99%

Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.

Kamagata

Muragaki

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

161

139

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“…Abbreviations: scFv, single-chain Fv; mAb, monoclonal antibody; NC1, non-collagenous domain a single α-chain that contains a central highly interrupted collagenous domain flanked at the N-and C-terminus by non-collagenous domains. [11][12][13] The highest level of sequence homology between types XV and XVIII lies in the NC1 domain. The NC1 domains of type XV and XVIII collagens are organized into a N-terminal trimerization domain, a central protease-sensitive hinge region and a compact C-terminal endostatin (collagen XVIII) or restin (collagen XV) domain.…”

Section: Introductionmentioning

confidence: 99%

Improved stability of multivalent antibodies containing the human collagen XV trimerization domain

Cuesta

Sánchez-Martín

Blanco-Toribio

et al. 2012

mAbs

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“…Collagen types XIII and XV and the a5 chain of type IV collagen were identified in our laboratory by screening of cDNA libraries under low stringency with probes encoding collagenous sequences (4,9,10). Recently we screened a mouse cDNA library to obtain clones coding for the mouse counterpart to the previously characterized human type XIII collagen (9).…”

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confidence: 99%

Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen.

Rehn

Pihlajaniemi

1994

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

154

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We for the tissues. The nonfibrillar group comprises collagen types IV, VI-X, and XII-XVII (1-3). These molecules display great heterogeneity in structure, tissue location, macromolecular organization, and function. One common feature is that they all have one or more interruptions in the collagenous sequence. Their collagenous sequences vary in length from about 330 to 1400 aa, the shortest being found in type VI collagen molecules and the longest in type VII. Their carboxyl-terminal and amino-terminal noncollagenous domains also are highly variable in both sequence and length, the latter varying in both domains from <20 aa to several hundred amino acids. One subgroup among the nonfibrillar collagens is formed by the fibril-associated collagens with interrupted triple helices (FACMI): types IX, XII, and XIV (2). These collagens share sequence homology and do not appear to form polymers alone but are associated with fibrils composed of fibrillar collagens. Another subgroup is formed by the structurally homologous types VIII and X, which are thought to form sheets in the extracellular matrix (2). The recently described types XV (4), XVI (5), and XVII (6) differ from the other nonfibrillar collagens in being characterized by numerous interruptions in their triple-helical regions. Type XVI collagen shares some structural features with the FACIT collagens, as also does another recently characterized form called Y-collagen (7,8). Type XVII (6), a hemidesmosomal protein also known as the 180-kDa bullous pemphigoid antigen, is unique among the collagens in that it is thought to be a transmembrane protein.Collagen types XIII and XV and the a5 chain of type IV collagen were identified in our laboratory by screening of cDNA libraries under low stringency with probes encoding collagenous sequences (4, 9, 10). Recently we screened a mouse cDNA library to obtain clones coding for the mouse counterpart to the previously characterized human type XIII collagen (9). One of the positive clones was found to encode a collagenous protein not described before.t We present here a partial characterization of this polypeptide, which is characterized by multiple interruptions in the triple helix, and suggest that it should be designated the al chain of type XVIII collagen. Our findings indicate that type XVIII collagen has an unusual tissue location. Furthermore, type XVIII was found to be homologous with type XV, and the two thus form a subgroup among the collagens. MATERIALS AND METHODS[solation of cDNA Clones and DNA Sequencing. A 500-bp clone, G2, encoding the al chain ofmurine type XIII collagen (unpublished results) was used as a probe to screen a mouse embryo Agtll cDNA library (ML 1027a, Clontech) under stringent conditions (11). The final wash for the filters was at 50°C in 0.5x standard saline citrate (SSC)/0.1% NaDodSO4.The recombinant phage ME-1 was isolated and the insert DNA was subcloned to the EcoRI site of pBluescript SK (Stratagene). The nucleotide sequence was determined for Abbreviation: FACIT, fibril-associ...

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Identification of a previously unknown human collagen chain, alpha 1(XV), characterized by extensive interruptions in the triple-helical region.

Cited by 63 publications

References 35 publications

Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.

Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins.

Improved stability of multivalent antibodies containing the human collagen XV trimerization domain

Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen.

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