Complete exon–intron organization and chromosomal location of the gene for mouse type XIII collagen (col13a1) and comparison with its human homologue

Kvist, Ari-Pekka; Latvanlehto, Anne; Sund, Malin; Horelli‐Kuitunen, Nina; Rehn, Marko; Palotie, Aarno; Beier, David R.; Pihlajaniemi, Taina

doi:10.1016/s0945-053x(99)00018-9

Cited by 20 publications

(15 citation statements)

References 47 publications

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“…the genes encoding collagen types VI, VII, and XIII), as well as the gene encoding the collagen tail of acetyl cholinesterase (Krejci et al, 1997). Although these genes are built of phase 0 exons, there is a predominance of 63 bp exons in the type VI gene (Saitta et al, 1991), 36 bp exons in the type VII gene (Christiano et al, 1994), and 27 bp exons in the type XIII gene (Kvist et al, 1999). The second group includes collagen genes composed of only phase 1 exons.…”

Section: Triple-helical Sequence As a Mobile Modulementioning

confidence: 99%

Evolution of collagens

et al. 2002

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The extracellular matrix is often defined as the substance that gives multicellular organisms (from plants to vertebrates) their structural integrity, and is intimately involved in their development. Although the general functions of extracellular matrices are comparable, their compositions are quite distinct. One of the specific components of metazoan extracellular matrices is collagen, which is present in organisms ranging from sponges to humans. By comparing data obtained in diploblastic, protostomic, and deuterostomic animals, we have attempted to trace the evolution of collagens and collagen-like proteins. Moreover, the collagen story is closely involved with the emergence and evolution of metazoa. The collagen triple helix is one of numerous modules that arose during the metazoan radiation which permit the formation of large multimodular proteins. One of the advantages of this module is its involvement in oligomerization, in which it acts as a structural organizer that is not only relatively resistant to proteases but also permits the creation of multivalent supramolecular networks. Anat Rec 268: 302-316, 2002.

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Section: Triple-helical Sequence As a Mobile Modulementioning

confidence: 99%

Evolution of collagens

et al. 2002

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“…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][4][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.…”

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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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“…Collagen, type XIII, ·1 (COL13A1) is a constituent of type XIII collagen. It is a transmembrane protein which belongs to a non-fibrillar collagen group (33), and is expressed in various tissues including the bone, muscle, and heart, being implicated in cellular adhesion and migration (34,35). Sema domain, immunoglobulin domain, short basic domain, secreted, 3F (SEMA3F) is a member of the class 3 semaphorins and plays an important role in endothelial cell functions in vasculature (36).…”

Section: Discussionmentioning

confidence: 99%

Genetic risk for myocardial infarction in Japanese individuals with or without chronic kidney disease

Fujimaki

Kato²,

Yokoi³

et al. 2010

Int J Mol Med

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Abstract. Although chronic kidney disease (CKD) is recognized as an important risk factor for myocardial infarction (MI), genetic factors underlying predisposition to MI in individuals with or without CKD remain largely unknown. The aim of the present study was to identify genetic variants that confer susceptibility to MI in individuals with or without CKD in order to allow prediction of genetic risk for such individuals separately. The study population comprised a total of 4344 individuals, including 1247 individuals with CKD (506 subjects with MI and 741 controls) and 3097 individuals without CKD (833 subjects with MI and 2264 controls). The 150 polymorphisms examined in this study were selected by genome-wide association studies of ischemic stroke and MI with the use of the GeneChip Human Mapping 500K Array Set (Affymetrix) and determined by a method that combines the polymerase chain reaction and sequencespecific oligonucleotide probes with suspension array technology. In individuals with CKD, no polymorphism was significantly related to MI. In individuals without CKD, an initial screen by the Chi-square test revealed that the C→T polymorphism of CLEC16A (rs9925481) and the A→G polymorphism of LAMA3 (rs12373237) were significantly (false discovery rate for allele frequencies of <0.05) associated with MI. Subsequent multivariable logistic regression analysis with adjustment for covariates revealed that the C→T polymorphism of CLEC16A (dominant model; P=0.0003; odds ratio, 0.66) and the A→G polymorphism of LAMA3 (recessive model; P=0.0087; odds ratio, 0.75) were significantly (P<0.05) associated with MI. A stepwise forward selection procedure also revealed that these polymorphisms were significant and independent determinants of MI. CLEC16A and LAMA3 may be susceptibility loci for MI in Japanese individuals without CKD. Determination of genotypes for CLEC16A and LAMA3 may prove informative for assessment of the genetic risk for MI in such individuals.

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Complete exon–intron organization and chromosomal location of the gene for mouse type XIII collagen (col13a1) and comparison with its human homologue

Cited by 20 publications

References 47 publications

Evolution of collagens

Evolution of collagens

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

Genetic risk for myocardial infarction in Japanese individuals with or without chronic kidney disease

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