HGNC Approved Gene Symbol: COL6A3
SNOMEDCT: 1220573009;
Cytogenetic location: 2q37.3 Genomic coordinates (GRCh38) : 2:237,324,018-237,414,164 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 2q37.3 | Bethlem myopathy 1C | 620726 | Autosomal dominant; Autosomal recessive | 3 |
| Dystonia 27 | 616411 | Autosomal recessive | 3 | |
| Ullrich congenital muscular dystrophy 1C | 620728 | Autosomal dominant; Autosomal recessive | 3 |
The COL6A3 gene encodes the alpha-3 chain of type VI collagen. See also COL6A1 (120220).
Chu et al. (1990) isolated and sequenced human cDNA clones corresponding to the COL6A3 gene.
Klewer et al. (1998) studied COL6A3 gene expression in the developing mammalian heart. The pattern of expression was identical to that of COL6A1.
By microarray analysis, Jun et al. (2001) demonstrated expression of the COL6A3 gene in human donor corneas.
Zech et al. (2015) found expression of the Col6a3 gene in neurons of the mouse brain, including in the cerebellum and striatum, with highest expression in the brainstem and midbrain. Astroglia did not express Col6a3.
Stokes et al. (1991) reported information on the exons for part of the COL6A3 gene.
Weil et al. (1987, 1988) localized the COL6A3 gene to chromosome 2q37 by Southern blot analysis of somatic cell hybrids and by in situ hybridization. At least 3 other extracellular matrix genes are also located on 2q: 2 collagen genes, COL3A1 (120180) and COL5A2 (120190), and the fibronectin gene (135600).
Using fluorescence in situ hybridization, Speer et al. (1996) localized the COL6A3 gene to chromosome 2q37 within a 17-cM region spanned by D2S336 and D2S395. By linkage analysis, they mapped a candidate gene for Bethlem myopathy (620726) to the same chromosomal region.
Bethlem Myopathy 1C and Ullrich Congenital Muscular Dystrophy 1C
Pan et al. (1998) identified a heterozygous mutation in the COL6A3 gene (120250.0001) in affected members of a large American pedigree of French Canadian descent (family 1949) with Bethlem myopathy-1C (BTHLM1C; 620726), a rare proximal myopathy characterized by early childhood onset and joint contractures. The mutation segregated with the disorder in the family, which was originally reported by Mohire et al. (1988).
In 2 unrelated patients with Bethlem myopathy, Baker et al. (2007) identified different heterozygous mutations in the COL6A3 gene (120250.0005; 120250.0006).
Ullrich congenital muscular dystrophy-1C (UCMD1C; 620728) is characterized by generalized muscular weakness, contractures of multiple joints, and distal hyperextensibility. Demir et al. (2002) demonstrated linkage of UCMD to 2q37 in 3 families, each of which demonstrated homozygous mutation in the COL6A3 gene (see, e.g., 120250.0002 and 120250.0003). One family (family I) had a phenotype of intermediate severity, a second (family II) had an unusually mild phenotype, and a third (family III) had a severe phenotype as previously described in patients with UCMD. This was the first description of mutations in COL6A3 in UCMD; mutations had previously been described in COL6A2 (120240).
Lampe et al. (2005) developed a method for rapid direct sequence analysis of all 107 coding exons of the COL6 genes (COL6A1, COL6A2, COL6A3) using single condition amplification/internal primer (SCAIP) sequencing. They sequenced all 3 COL6 genes from genomic DNA in 79 patients with UCMD or Bethlem myopathy, and found putative mutations in one of the COL6 genes in 62% of patients. Some patients showed changes in more than one of the COL6 genes, and some UCMD patients appeared to have dominant rather than recessive disease. Lampe et al. (2005) concluded that these findings may explain some or all of the cases of UCMD that are unlinked to the COL6 genes under a recessive model.
Nadeau et al. (2009) identified a recurrent de novo heterozygous splice site mutation in the COL6A3 gene (120250.0004) in 2 unrelated individuals with UCMD1C.
In 2 brothers (P9A and P9B) with variable manifestations of autosomal recessive Bethlem myopathy-1C (BTHLM1C; 620726), Panades-de Oliveira et al. (2019) identified a homozygous missense variant in the COL6A3 gene (K2483E; 120250.0012). Another patient (P8A) with the disorder was compound heterozygous for K2483E and a frameshift mutation (c.8540delA; 120250.0013). The mutations were found by next-generation sequencing and confirmed by Sanger sequencing. Functional studies of the variants and studies of patient cells were not performed. P9A, a 42-year-old man, had onset of proximal muscle weakness in childhood, whereas his brother (P9B) was almost asymptomatic at 48 years of age, except for hyperCKemia and distal contractures.
Villar-Quiles et al. (2021) reported 16 patients with autosomal recessive BTHLM1C associated with the K2483E substitution in the COL6A3 gene (120250.0012). Four unrelated patients were homozygous for the mutation, and 12 patients from 10 families carried it in the compound heterozygous state with another putative loss-of-function COL6A3 mutation (see, e.g., R1597X, 120250.0014). Segregation studies, performed in 8 families, confirmed that the unaffected parents were heterozygous carriers. Fibroblasts derived from 5 of the compound heterozygous patients showed reduced collagen VI secretion, which was most likely due to the second loss-of-function COL6A3 variant. In contrast, fibroblasts from 3 patients who were homozygous for the K2483E variant showed essentially normal collagen VI secretion in 2 and mildly reduced secretion in 1, suggesting that the missense variant does not significantly impact COL6 assembly and secretion. Villar-Quiles et al. (2021) suggested that this missense variant may act as a modulator of the clinical phenotype.
Dystonia 27
In affected members of 3 unrelated German families with autosomal recessive dystonia-27 (DYT27; 616411), Zech et al. (2015) identified compound heterozygous mutations in the COL6A3 gene (120250.0007-120250.0011) that segregated with the disorder in each family. The mutations in the first family were found by exome sequencing; mutations in the subsequent 2 families were found by sequencing exons 41 and 42 of the COL6A3 gene in 367 German cases with isolated dystonia. All patients carried mutations affecting the C terminus, with at least 1 mutation specifically affecting exon 41. The patients presented before age 25 years with isolated dystonia mainly affecting the craniocervical region and the upper limbs. None of the patients had signs of muscular involvement, and patient fibroblasts showed normal distribution and organization of collagen VI. Functional studies of the variants were not performed, but selective knockdown of the zebrafish ortholog resulted in axonal targeting defects. Zech et al. (2015) hypothesized that perturbation of the brain extracellular matrix may underlie this form of dystonia.
Zech et al. (2015) found that morpholino knockdown of exon 42 of the zebrafish col6a3 gene, which corresponds to exon 41 of the human COL6A3 gene, caused dose-dependent motor neuron pathfinding, branching, and extension errors without overt collagen defects.
In affected members of a large American kindred of French Canadian descent (family 1489) with Bethlem myopathy (BTHLM1C; 620726), originally reported by Mohire et al. (1988) and linked to chromosome 2 by Speer et al. (1996), Pan et al. (1998) identified a heterozygous G-to-A transition in the COL6A3 gene, resulting in a gly1679-to-glu (G1679E) substitution in the N-terminal globular domain of the protein, rather than in the triple-helical domain where mutations had been found in the COL6A1 (120220) and COL6A2 (120240) genes. The mutation occurred in the N2 subdomain, one of the von Willebrand factor type A domains of the COL6A3 gene. The mutation segregated with the disorder in the family.
In 3 sibs, a brother and 2 sisters, with consanguineous parents originating from Morocco (family I), Demir et al. (2002) identified homozygosity for a splice donor site mutation in intron 29 (c.6930+5A-G) as the cause of autosomal recessive Ullrich congenital muscular dystrophy (UCMD1C; 620728). The phenotype was of intermediate severity. The mutation caused skipping of exon 29 and partial reduction of collagen VI in muscle biopsy. Neonatal hypotonia, severe in most cases, was found in all 5 cases in the 3 families reported by Demir et al. (2002). In this family the 2 eldest sibs were never able to walk without support (calipers or walking frame). Generalized muscle weakness, associated with predominantly distal amyotrophy, became evident in the first years of life. Axial muscles (mainly neck flexors), pelvic girdle muscles, and intrinsic muscles in hands and feet were the most severely affected ones. Lower limbs tended to be more severely affected than upper limbs; in most cases, hip extensors and abductors were weaker than hip flexors, leading to hip contractures that interfered with standing position. No significant facial weakness was observed. CK levels were normal or moderately raised (up to 4 times the normal values).
In a girl of Italian extraction (family II) with unusually mild Ullrich congenital muscular dystrophy (UCMD1C; 620728), Demir et al. (2002) found a homozygous nonsense mutation in exon 5 of the COL6A3 gene: arg465 to ter (R465X). Analysis of the patient's COL6A3 transcript showed the presence of various mRNA species, one of which lacked several exons, including the exon containing the nonsense mutation. The patient in this case was still ambulant at age 18 and showed an unusual combination of hyperlaxity and finger contractures (see Figure 2). When the wrist was extended, the retraction of finger flexor muscles impeded complete finger extension, causing flexion contractures of fingers, which is regarded as a characteristic 'Bethlem' sign. When the wrist was not extended, the finger laxity became evident. The patient was able to overlap, cross, or extend fingers beyond the normal range of motion ('Ullrich sign').
In a patient (UCMD5) with Ullrich congenital muscular dystrophy (UCMD1C; 620728), Baker et al. (2005) identified heterozygosity for a de novo splice site mutation (IVS16DS+1G-A) in intron 16 of the COL6A3 gene. The mutation was predicted to result in loss of exon 16, which encodes amino acids 13 to 33 of the triple helical region of COL6A3.
Nadeau et al. (2009) identified a recurrent de novo heterozygous IVS16DS+1G-A mutation in 2 unrelated patients with UCMD1C. The first patient was a 30-year-old individual who had onset at birth with hypotonia, congenital hip dislocation, delayed motor development, and feeding difficulties. Independent walking was not achieved, and the patient became wheelchair-bound at age 12 years. There was spinal rigidity, scoliosis, and kyphosis, as well as follicular hyperkeratosis, keloid formation, and need for nocturnal ventilation. The second patient had onset at age 1.5 years but never achieved independent walking and was wheelchair-bound by age 3.5 years. This patient died at age 10 years during a respiratory illness.
In a 40-year-old Australian man with Bethlem myopathy (BTHLM1C; 620726), Baker et al. (2007) identified a heterozygous 2-bp change (GT-to-TC) in intron 15 of the COL6A3 gene, resulting in the skipping of exon 16, which encodes the cysteine-rich linker region and the most N-terminal 15 amino acids of the triple helix. Further studies showed that the mutation also resulted in a premature stop codon and nonsense-mediated decay. There was decreased collagen VI in the extracellular matrix, indicating impaired microfibril formation. The patient had delayed motor development, diffuse muscle weakness, decreased motor capacity, kyphosis, and dystrophic features on muscle biopsy.
In a 20-year-old man with Bethlem myopathy (BTHLM1C; 620726), Baker et al. (2007) identified a heterozygous 5177T-G transversion in a highly conserved residue in exon 11 of the COL6A3 gene, resulting in a leu1726-to-arg (L1726R) substitution in the globular N2 A domain. The patient had reduced motor capacity, proximal muscle weakness, joint contractures, and dystrophic findings on muscle biopsy. Further studies showed normal levels of collagen VI in the extracellular matrix, indicating that the mutant protein was able to fold and incorporate into collagen VI.
In 2 sibs, born of unrelated German parents, with dystonia-27 (DYT27; 616411), Zech et al. (2015) identified compound heterozygous missense mutations in the COL6A3 gene: a c.9128G-A transition (rs552651651) in exon 41, resulting in an arg3043-to-his (R3043H) substitution, and a c.9245C-G transversion in exon 42, resulting in a pro3082-to-arg (P3082R; 120250.0008) substitution. Both mutations occurred at highly conserved residues in the C-terminal fibronectin type III motif (C4 domain). The mutations, which were found by exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. The c.9128G-A variant was not found in the Exome Sequencing Project (ESP) database, whereas the c.9245C-G variant was found in 8 of 8,600 ESP alleles (frequency of 0.0009). Analysis of the Exome Aggregation Consortium database identified the 2 variants at very low frequencies (0.0003 for c.9128G-A and 0.001 for c.9245C-G). Notably, homozygosity for both variants was reported in 2 South Asian control exomes, suggesting either reduced penetrance or the possibility that these individuals may develop dystonia. Functional studies of the variants were not performed.
For discussion of the c.9245C-G transversion (rs182976977) in the COL6A3 gene, resulting in a pro3082-to-arg (P3082R) substitution, that was found in compound heterozygous state in a patient with dystonia-27 (DYT27; 616411) by Zech et al. (2015), see 120250.0007.
In 2 patients with dystonia-27 (DYT27; 616411), Zech et al. (2015) identified compound heterozygous mutations in the COL6A3 gene: both patients carried a G-to-C transversion in intron 40 (c.8966-1G-C, NM_004369.3), resulting in the skipping of exon 41 and an in-frame deletion of 98 residues from the C4 domain (Val2989_Lys3077delinsGlu). One patient carried a c.7502G-A transition resulting in an arg2501-to-his (R2501H; 120250.0010) substitution on the other allele, whereas the other patient carried a c.7660G-A transition, resulting in an ala2554-to-thr (A2554T; 120250.0011) substitution on the other allele. The c.7502G-A and c.7660G-A transitions occurred in exon 36 and affected highly conserved residues. None of the 3 variants were found in the Exome Sequencing Project database or in 752 control alleles. The c.8966-1G-C and c.7502G-A variants were found at very low frequencies in the Exome Aggregation Consortium (0.00003 and 0.00001, respectively); c.7660G-A was not found in this database. Functional studies of the variants were not performed.
For discussion of the c.7502G-A transition (rs541928674) in the COL6A3 gene, resulting in an arg2501-to-his (R2501H) substitution, that was found in compound heterozygous state in a patient with dystonia-27 (DYT27; 616411) by Zech et al. (2015), see 120250.0009.
For discussion of the c.7660G-A transition (c.7660G-A, NM_004369.3) in the COL6A3 gene, resulting in an ala2554-to-thr (A2554T) substitution, that was found in compound heterozygous state in a patient with dystonia-27 (DYT27; 616411) by Zech et al. (2015), see 120250.0009.
In 2 brothers (P9A and P9B) with variable manifestations of autosomal recessive Bethlem myopathy-1C (BTHLM1C; 620726), Panades-de Oliveira et al. (2019) identified a homozygous c.7447A-G transition (c.7447A-G, NM_004369.3) in exon 36 of the COL6A3 gene, resulting in a lys2483-to-glu (K2483E) substitution. (In the article by Panades-de Oliveira et al. (2019), this variant is incorrectly cited as lys2486-to-glu (K2486E) in the abstract and at various places in the text, but correctly as K2483E in Table 2 and at other places in the text.) Another patient (P8A) with the disorder was compound heterozygous for K2483E and a 1-bp deletion (c.8540delA; 120250.0013) in exon 39, predicted to result in a frameshift and premature termination. The mutations were found by next-generation sequencing and confirmed by Sanger sequencing. Functional studies of the variants and studies of patient cells were not performed. P9A, a 42-year-old man, had onset of proximal muscle weakness in childhood, whereas his brother (P9B) was almost asymptomatic at 48 years of age, except for hyperCKemia and distal contractures.
In 16 patients from 14 families with autosomal recessive Bethlem myopathy-1C (BTHLM1C; 620726), Villar-Quiles et al. (2021) identified a c.7447A-G transition in the COL6A3 gene, resulting in a lys2483-to-glu (K2483E) substitution in a nonhelical domain. Twelve patients carried the variant in compound heterozygosity with another putative loss-of-function variant in the COL6A3 gene (see, e.g., R1597X, 120250.0014), whereas 4 patients (P11, P12, P13, and P14) were homozygous for the K2483E variant. Segregation studies performed in 8 families confirmed that the tested parents were unaffected heterozygous carriers. Fibroblasts derived from 5 of the compound heterozygous patients showed reduced collagen VI secretion, which was most likely due to the second loss-of-function COL6A3 variant. In contrast, fibroblasts from 3 patients who were homozygous for the K2483E variant showed essentially normal collagen VI secretion in 2 and mildly reduced secretion in 1, suggesting that the missense variant does not significantly impact COL6 assembly and secretion. Villar-Quiles et al. (2021) suggested that this missense variant may act as a modulator of the clinical phenotype. The 12 patients who were compound heterozygous for K2483E and another COL6A3 variant tended to present in childhood with proximal muscle weakness, joint contractures, and variable presence of rigid spine, skin abnormalities, and mild respiratory involvement. In contrast, the patients who were homozygous for the K2483E variant had fewer joint contractures, and none had distal hyperlaxity, skin abnormalities, or respiratory involvement. Hamosh (2024) noted that the K2483E variant was present in heterozygous state in 1,158 of 1,614,090 alleles in gnomAD (v4.1.0) and in 1 homozygote (frequency of 7.0 x 10(-4)).
For discussion of the 1-bp deletion (c.8540delA) in exon 39 of the COL6A3 gene, predicted to result in a frameshift and premature termination, that was found in compound heterozygous state in a patient (P8A) with autosomal recessive Bethlem myopathy-1C (BTHLM1C; 620726) by Panades-de Oliveira et al. (2019), see 120250.0012.
For discussion of the c.4789C-T transition in the COL6A3 gene, resulting in an arg1597-to-ter (R1597X) substitution, that was found in compound heterozygous state in 2 sibs (family 1) with autosomal recessive Bethlem myopathy-1C (BTHLM1C; 620726) by Villar-Quiles et al. (2021), see 120250.0012.
Baker, N. L., Morgelin, M., Pace, R. A., Peat, R. A., Adams, N. E., Gardner, R. J. M., Rowland, L. P., Miller, G., De Jonghe, P., Ceulemans, B., Hannibal, M. C., Edwards, M., Thompson, E. M., Jacobson, R., Quinlivan, R. C. M., Aftimos, S., Kornberg, A. J., North, K. N., Bateman, J. F., Lamande, S. R. Molecular consequences of dominant Bethlem myopathy collagen VI mutations. Ann. Neurol. 62: 390-405, 2007. [PubMed: 17886299] [Full Text: https://doi.org/10.1002/ana.21213]
Baker, N. L., Morgelin, M., Peat, R., Goemans, N., North, K. N., Bateman, J. F., Lamande, S. R. Dominant collagen VI mutations are a common cause of Ullrich congenital muscular dystrophy. Hum. Molec. Genet. 14: 279-293, 2005. [PubMed: 15563506] [Full Text: https://doi.org/10.1093/hmg/ddi025]
Chu, M.-L., Zhang, R.-Z., Pan, T.-C., Stokes, D., Conway, D., Kuo, H.-J., Glanville, R., Mayer, U., Mann, K., Deutzmann, R., Timpl, R. Mosaic structure of globular domains in the human type VI collagen alpha-3 chain: similarity to von Willebrand factor, fibronectin, actin, salivary proteins and apotinin type protease inhibitors. EMBO J. 9: 385-393, 1990. [PubMed: 1689238] [Full Text: https://doi.org/10.1002/j.1460-2075.1990.tb08122.x]
Demir, E., Sabatelli, P., Allamand, V., Ferreiro, A., Moghadaszadeh, B., Makrelouf, M., Topaloglu, H., Echenne, B., Merlini, E., Guicheney, P. Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital muscular dystrophy. Am. J. Hum. Genet. 70: 1446-1458, 2002. [PubMed: 11992252] [Full Text: https://doi.org/10.1086/340608]
Hamosh, A. Personal Communication. Baltimore, Md. 7/10/2024.
Jun, A. S., Liu, S. H., Koo, E. H., Do, D. V., Stark, W. J., Gottsch, J. D. Microarray analysis of gene expression in human donor corneas. Arch. Ophthal. 119: 1629-1634, 2001. [PubMed: 11709013] [Full Text: https://doi.org/10.1001/archopht.119.11.1629]
Klewer, S. E., Krob, S. L., Kolker, S. J., Kitten, G. T. Expression of type VI collagen in the developing mouse heart. Dev. Dyn. 211: 248-255, 1998. [PubMed: 9520112] [Full Text: https://doi.org/10.1002/(SICI)1097-0177(199803)211:3<248::AID-AJA6>3.0.CO;2-H]
Lampe, A. K., Dunn, D. M., von Niederhausern, A. C., Hamil, C., Aoyagi, A., Laval, S. H., Marie, S. K., Chu, M.-L., Swoboda, K., Muntoni, F., Bonnemann, C. G., Flanigan, K. M., Bushby, K. M. D., Weiss, R. B. Automated genomic sequence analysis of the three collagen VI genes: applications to Ullrich congenital muscular dystrophy and Bethlem myopathy. J. Med. Genet. 42: 108-120, 2005. [PubMed: 15689448] [Full Text: https://doi.org/10.1136/jmg.2004.023754]
Mohire, M. D., Tandan, R., Fries, T. J., Little, B. W., Pendlebury, W. W., Bradley, W. G. Early-onset benign autosomal dominant limb-girdle myopathy with contractures (Bethlem myopathy). Neurology 38: 573-580, 1988. [PubMed: 3352914] [Full Text: https://doi.org/10.1212/wnl.38.4.573]
Nadeau, A., Kinali, M., Main, M., Jimenez-Mallebrera, C., Aloysius, A., Clement, E., North, B., Manzur, A. Y., Robb, S. A., Mercuri, E., Muntoni, F. Natural history of Ullrich congenital muscular dystrophy. Neurology 73: 25-31, 2009. [PubMed: 19564581] [Full Text: https://doi.org/10.1212/WNL.0b013e3181aae851]
Pan, T.-C., Zhang, R.-Z., Pericak-Vance, M. A., Tandan, R., Fries, T., Stajich, J. M., Viles, K., Vance, J. M., Chu, M.-L., Speer, M. C. Missense mutation in a von Willebrand factor type A domain of the alpha-3(VI) collagen gene (COL6A3) in a family with Bethlem myopathy. Hum. Molec. Genet. 7: 807-812, 1998. [PubMed: 9536084] [Full Text: https://doi.org/10.1093/hmg/7.5.807]
Panades-de Oliveira, L., Rodriguez-Lopez, C., Cantero Montenegro, D., Marcos Toledano, M. D. M., Fernandez-Marmiesse, A., Esteban Perez, J., Hernandez Lain, A., Dominguez-Gonzalez, C. Bethlem myopathy: a series of 16 patients and description of seven new associated mutations. J. Neurol. 266: 934-941, 2019. [PubMed: 30706156] [Full Text: https://doi.org/10.1007/s00415-019-09217-z]
Speer, M. C., Tandan, R., Rao, P. N., Fries, T., Stajich, J. M., Bolhuis, P. A., Jobsis, G. J., Vance, J. M., Viles, K. D., Sheffield, K., James, C., Kahler, S. G., Pettenati, M., Gilbert, J. R., Denton, P. H., Yamaoka, L. H., Pericak-Vance, M. A. Evidence for locus heterogeneity in the Bethlem myopathy and linkage to 2q37. Hum. Molec. Genet. 5: 1043-1046, 1996. [PubMed: 8817344] [Full Text: https://doi.org/10.1093/hmg/5.7.1043]
Stokes, D. G., Saitta, B., Timpl, R., Chu, M.-L. Human alpha-3(VI) collagen gene: characterization of exons coding for the amino-terminal globular domain and alternative splicing in normal and tumor cells. J. Biol. Chem. 266: 8626-8633, 1991. [PubMed: 2022673]
Villar-Quiles, R. N., Donkervoort, S., de Becdelievre, A., Gartioux, C., Jobic, V., Foley, A. R., McCarty, R. M., Hu, Y., Menassa, R., Michel, L., Gousse, G., Lacour, A., and 20 others. Clinical and molecular spectrum associated with COL6A3 c.7447A-G p.(Lys2483Glu) variant: elucidating its role in collagen VI-related myopathies. J. Neuromusc. Dis. 8: 633-645, 2021. [PubMed: 33749658] [Full Text: https://doi.org/10.3233/JND-200577]
Weil, D., Mattei, M.-G., Passage, E., Van Cong, N., Pribula-Conway, D., Mann, K., Deutzmann, R., Timpl, R., Chu, M.-L. Assignment of the three genes coding for the different chains of type VI collagen (COL6A1, COL6A2, COL6A3). (Abstract) Cytogenet. Cell Genet. 46: 713 only, 1987.
Weil, D., Mattei, M.-G., Passage, E., Van Cong, N., Pribula-Conway, D., Mann, K., Deutzmann, R., Timpl, R., Chu, M.-L. Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen. Am. J. Hum. Genet. 42: 435-445, 1988. [PubMed: 3348212]
Zech, M., Lam, D. D., Francescatto, L., Schormair, B., Salminen, A. V., Jochim, A., Wieland, T., Lichtner, P., Peters, A., Gieger, C., Lochmuller, H., Strom, T. M., Haslinger, B., Katsanis, N., Winkelmann, J. Recessive mutations in the alpha-3 (VI) collagen gene COL6A3 cause early-onset isolated dystonia. Am. J. Hum. Genet. 96: 883-893, 2015. [PubMed: 26004199] [Full Text: https://doi.org/10.1016/j.ajhg.2015.04.010]