HGNC Approved Gene Symbol: COL11A1
SNOMEDCT: 1010664005, 17144009, 33410002;
Cytogenetic location: 1p21.1 Genomic coordinates (GRCh38): 1:102,876,473-103,108,522 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 1p21.1 | {Lumbar disc herniation, susceptibility to} | 603932 | 3 | |
| Deafness, autosomal dominant 37 | 618533 | Autosomal dominant | 3 | |
| Fibrochondrogenesis 1 | 228520 | Autosomal recessive | 3 | |
| Marshall syndrome | 154780 | Autosomal dominant | 3 | |
| Stickler syndrome, type II | 604841 | Autosomal dominant | 3 |
Yoshioka et al. (1995) reported 93% sequence identity between the predicted amino acid sequence of mouse and human type XI collagen. Cloning experiments also revealed alternative splicing of the sequence coding for 85 residues located within the acidic region of the amino-globular domain of alpha-1 (XI). Analysis of RNA samples from different embryonic tissues suggested that alternative splicing may be confined to tissue destined to become bone.
Bernard et al. (1988) showed that the cDNA-derived amino acid sequence of type XI collagen shows a variety of structural features characteristic of fibril-forming collagens. In addition, nucleotide sequence analysis of a selected portion of the human gene showed the characteristic 54-bp exon motif. They concluded, therefore, that type XI collagen belongs to the group of fibrillar collagens. They also suggested that expression of this gene is not restricted to cartilage, as previously thought, since the cDNA libraries from which the clones were isolated originated from both cartilaginous and noncartilaginous tissues.
Booth et al. (2019) noted that the COL11A1 gene is expressed in the tectorial membrane of the inner ear.
Jacenko et al. (1994) pointed out the usefulness of studies of the more than 40 well-characterized murine skeletal dysplasias as contributions to the understanding of human osteochondrodysplasias. As one example, they pointed to the work of Li et al. (1993), which demonstrated that the mutation in the mouse autosomal recessive disease chondrodysplasia (cho) maps to mouse chromosome 3 in the same region as the COL11A1 gene. Li et al. (1995) demonstrated deletion of a cytidine residue about 570 nucleotides downstream of the translation initiation codon in COL11A1 mRNA from cho homozygotes. The deletion caused a reading frame shift and introduced a premature stop codon. Limb bones of newborn cho/cho mice are wider at the metaphyses than normal bones and only about half the normal length. The findings demonstrate that collagen XI is essential for normal formation of cartilage collagen fibrils and the cohesive properties of cartilage. The results also suggest that the normal differentiation and spatial organization of growth plate chondrocytes are critically dependent on the presence of type XI collagen in cartilage extracellular matrix.
By microarray analysis, Jun et al. (2001) demonstrated expression of the COL11A1 gene in human donor corneas.
Fichard et al. (1995) reviewed collagens V (120215) and XI and commented on their fundamental role in the control of fibrillogenesis, probably by forming a core within the fibrils. Another characteristic of these collagens is the partial retention of their N-propeptide extensions in tissue forms, which is unusual for known fibrillar collagens. The tissue locations of collagen V and XI are different, but their structural and biologic properties seem to be closely related. Their primary structures are highly conserved at both the gene and the protein level, and this conservation is the basis of their similar biologic properties. In particular, they are both resistant to mammalian collagenases, and surprisingly sensitive to trypsin. Although they have both cell adhesion and heparin binding sites that could be crucial in physiologic processes such as development and wound healing, the 2 collagens are usually buried within the major collagen fibrils. It had become evident that several collagen-type molecules are, in fact, heterotypic associations of chains from both collagens V and XI, demonstrating that these 2 collagens are not distinct types but a single type that can be called collagen V/XI.
Annunen et al. (1999) characterized the genomic structure of the COL11A1 gene. The gene spans over 150 kb and consists of 68 exons. The exons were numbered 1 to 67, with numbers 6A and 6B used for the sixth and seventh exons (previously called IIA and IIB) because they are alternatively spliced and do not exist in the same mRNA (Zhidkova et al., 1995). Exons numbered 9-15 by Bernard et al. (1988) corresponded to exon 16-22 in the numbering of Annunen et al. (1999). No cysteinyl residue was found in the triple-helical region. The amino acid at position 690 was methionine instead of tryptophan, an amino acid rarely found in collagen triple helices.
The gene for at least one subunit of type XI collagen was assigned to chromosome 1 by probing of DNA isolated from flow-sorted chromosomes (Henry et al., 1988); by in situ hybridization, the gene was regionalized to 1p21.
Sirko-Osadsa et al. (1996) presented evidence that a form of Stickler syndrome (STL2; 604841) is caused by a mutation in the COL11A1 gene. They identified and used intragenic and highly linked markers of COL11A1 to show that this locus was linked to Stickler syndrome in families in which linkage to COL11A2 and COL2A1 had been excluded.
Stickler Syndrome Type II and Marshall Syndrome
Richards et al. (1996) studied a 4-generation family in which 7 individuals were affected with Stickler syndrome type II (STL2; 604841) with vitreous and retinal abnormalities and 9 individuals were normal. The authors demonstrated linkage to the COL11A1 gene region. Mutation analysis of COL11A1 was performed on RT-PCR products using RNA extracted from cultured dermal fibroblasts. Sequence analysis revealed that affected individuals were heterozygous for a gly97-to-val substitution (120280.0001) that disrupts the Gly-X-Y collagen sequence. SSCP analysis of 100 chromosomes from 50 unrelated controls revealed only the pattern of bands seen in normal family members. Richards et al. (1996) concluded that collagen XI is an important structural component of human vitreous.
Martin et al. (1999) pointed out that Stickler syndrome patients with mutations in COL11A1 show a 'beaded' or type 2 vitreous phenotype. In 5 families with the type 2 vitreous phenotype, Martin et al. (1999) identified 2 families that were linked to COL11A1; sequencing identified mutations resulting in shortened collagen chains, one through exon skipping and the other through a multiexon deletion.
Annunen et al. (1999) identified 15 novel mutations in the COL11A1 gene and 8 in the COL2A1 gene in patients with Marshall syndrome (MRSHS; 154780), Stickler syndrome, or Stickler-like syndrome. Most of the mutations in the COL11A1 gene altered the splicing consensus sequences, but all of them affected the splicing-consensus sequences of 54-bp exons, as reported by Griffith et al. (1998). In addition, one patient had a genomic deletion resulting in the loss of a 54-bp exon (120280.0002). Nine out of 10 of these mutations affected the splicing of 54-bp exons in the region spanning exons 38 to 54 of the gene. Although more than one-third of the exons in this region are 90 or 108 bp in size, no splicing mutations were found in them.
Majava et al. (2007) analyzed 44 patients with a phenotype suggestive of Stickler syndrome or Marshall syndrome who were negative for mutations in the COL2A1 gene, and they identified mutations in COL11A1 in 10 patients (see, e.g., 120280.0002 and 120280.0006). Four of the 10 mutation-positive patients were diagnosed with Marshall syndrome, but the remaining 6 showed an overlapping Marshall/Stickler phenotype. Majava et al. (2007) concluded that heterozygous COL11A1 mutations can result in either Marshall syndrome or Stickler syndrome, and also in phenotypes that are difficult to classify with respect to the 2 disorders. A type I vitreous anomaly was diagnosed in a patient with a mutation in COL11A1 (120280.0006), suggesting that the vitreous phenotype does not always allow prediction of the defective gene in Stickler and Marshall syndromes.
In a mother and son with Marshall syndrome, Ala-Kokko and Shanske (2009) identified heterozygosity for a splice site mutation in the COL11A1 gene (120280.0012). The mother, who was more mildly affected, was mosaic for the mutation; the authors stated that this was the first report of mosaicism in Marshall syndrome.
Lumbar Disc Herniation, Susceptibility to
Lumbar disc herniation (see 603932), degeneration and herniation of the nucleus pulposus of the intervertebral disc of the lumbar spine, is one of the most common musculoskeletal disorders. Type XI collagen is important for cartilage collagen formation and for organization of the extracellular matrix. Mio et al. (2007) identified an association between polymorphism of the COL11A1 gene and lumbar disc herniation in Japanese populations. A single-nucleotide polymorphism (4603C-T; 120280.0007) had the most significant association with lumbar disc herniation, P = 3.3 x 10(-6). Normally, the COL11A1 gene is highly expressed in the intervertebral disc; its expression was decreased in the intervertebral disc in patients with lumbar disc herniation. The expression level was inversely correlated with the severity of disc degeneration. The transcript containing the disease-associated allele was decreased because of its decreased stability. These observations indicated that type XI collagen is critical for intervertebral disc metabolism and that its decrease is related to lumbar disc herniation.
Fibrochondrogenesis 1
Tompson et al. (2010) sequenced the COL11A1 gene in 2 unrelated patients with fibrochondrogenesis (FBCG1; 228520) and demonstrated that each was a compound heterozygote for a loss-of-function mutation on one allele and a mutation predicting substitution for a conserved triple-helical glycine residue on the other (120280.0008-120280.0011). The parents who were carriers of a missense mutation had myopia. Early-onset hearing loss was noted in both parents who carried a loss-of-function allele. Tompson et al. (2010) suggested that COL11A1 is a locus for mild, dominantly inherited hearing loss and that there might be phenotypic manifestations among carriers.
Autosomal Dominant Deafness 37
In affected members of a large 4-generation family of European descent with autosomal dominant deafness-37 (DFNA37; 618533), Booth et al. (2019) identified a heterozygous splice site mutation in the COL11A gene (120280.0013). The mutation, which was found by a combination of linkage analysis and exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. Using a minigene construct to express the mutation in cell lines, the authors showed that the mutation resulted in the skipping of exon 5, causing an in-frame deletion and a peptide lacking residues 218 to 260 in the N-terminal propeptide. The mutation was predicted to affect all 5 transcripts of the gene, but possibly had a 'leaky' effect.
In affected individuals from 2 unrelated German families segregating autosomal dominant nonsyndromic prelingual sensorineural hearing loss, Rad et al. (2021) identified heterozygous splicing mutations in the COL11A1 gene (120280.0014 and 120280.0015, respectively).
In affected individuals from a 4-generation Italian family with prelingual or postlingual sensorineural nonsyndromic hearing loss (NSHL) who were negative for mutation in the GJB2 (121011) and GJB6 (604418) genes as well as 96 other NSHL-associated genes, Ciorba et al. (2021) identified heterozygosity for a missense mutation in the COL11A1 gene (H165L; 120280.0016) that segregated fully with disease and was not found in public variant databases.
Implication of type XI collagen in human osteochondrodysplasias was supported by the fact that mice with chondrodysplasia (cho), an autosomal recessive disorder in which there is neonatal lethality, small mandible, cleft palate, small thorax, disproportionate limbs, and fragile cartilage (Seegmiller et al., 1971), were shown to have abnormality in the alpha-1 chain of type XI collagen.
Morris and Bachinger (1987) concluded that type XI collagen is a trimer consisting of 3 different polypeptides--alpha-1, alpha-2, and alpha-3. All 3 chains retain non-triple-helical domains. Wu and Eyre (1995), however, provided evidence that what was formerly termed the alpha-3 chain of type XI collagen is actually transcribed from the COL2A1 gene (120140).
In a 4-generation family with Stickler syndrome type II (STL2; 604841), Richards et al. (1996) found that affected individuals were heterozygous for a single-basepair change that led to a substitution of glycine-97 for valine (G97V) and disruption of the Gly-X-Y collagen sequence.
In a large 3-generation kindred with Marshall syndrome (MRSHS; 154780), Griffith et al. (1998) demonstrated a splice site mutation in the COL11A1 gene in affected individuals. A G-to-A transition at the 5-prime end of an intron caused in-frame skipping of the preceding 54-bp exon and deletion of amino acids 726 to 743 from the major triple helical domain of the alpha-1(XI) collagen polypeptide.
Shanske et al. (1998) suggested that the family reported by Griffith et al. (1998) suffered from Stickler syndrome (STL2; 604841), not Marshall syndrome. Shanske et al. (1997) reported a family in which 6 members in 4 generations were affected with Marshall syndrome. From a review of the literature, they attempted to distinguish the Stickler and Marshall syndromes. In both disorders, ophthalmologic abnormalities including high myopia, as well as midfacial hypoplasia, micrognathia with or without palatal clefting, and nonspecific skeletal abnormalities have been reported. In spite of these overlaps, each of the disorders has distinctive features. Striking ocular hypertelorism and abnormalities of ectodermal derivatives had been reported only in Marshall syndrome. The phenotype described by Griffith et al. (1998) included only 'mild' orbital hypertelorism and no evidence of ectodermal derivative abnormalities.
Warman et al. (1998) vigorously defended the diagnosis of Marshall syndrome in the family they reported (Griffith et al., 1998). They argued that a comparison of the principal findings reported by Marshall (1958) with the findings in their family revealed high concordance, whereas comparison with the patients reported by Shanske et al. (1997) showed low concordance. Marshall's patients and their patients all had congenital or juvenile cataracts and fluid vitreous; none of the patients described by Shanske et al. (1997) had these conditions. Marshall's patients and their patients all had significant hearing loss; none of the patients described by Shanske et al. (1997) had hearing loss. Marshall's patients had 'ample and normal hair,' as did their patients; the patients described by Shanske et al. (1997) all had 'sparse' hair or a 'paucity of hair.' Two of Marshall's patients were studied radiographically; each had nasal bones that were 'small, short, and far back of their normal position.' These patients also had 'prominence of the frontal bossae,' which served to 'accentuate the flatness or depression of the bridge of the nose,' and 'thickening of the outer table of the skull and absent frontal sinuses.' In their report (Griffith et al., 1998), a patient photograph and cranial CT scan were included that showed nearly identical features. In contrast, the patients described by Shanske et al. (1997) had 'significant frontal recession' and normal skeletal surveys.
Warman et al. (1998) pointed out that although the presence of ectodermal abnormalities in the patients of Marshall (1958) had been emphasized, e.g., sparse hair, eyebrows, and eyelashes, the patients, in fact, did not have these; instead, Marshall (1958) thought that his patients had an altered ability to sweat. When comparing his patients with a 32-year-old female control, Marshall (1958) observed that sweat production was 'diminished, perhaps 25% below normal.'
In 3 unrelated patients with Marshall syndrome, Majava et al. (2007) identified heterozygosity for the 54-bp deletion of exon 50. All 3 patients had severe midface hypoplasia with a short nose, anteverted nares, and bulging eyes; sensorineural hearing loss was confirmed in the 2 patients who were old enough to test. No signs of ectodermal dysplasia were observed.
In their case 15, representing 'family B' reported by Zlotogora et al. (1992), Annunen et al. (1999) found a gly988-to-val (G988V) missense mutation in the COL11A1 gene. Affected family members had hearing loss, vitreoretinal degeneration, cataract, high myopia, short nose, anteverted nares, micro/retrognathia, midfacial hypoplasia, flat nasal bridge, long philtrum, and palatal defect, but had no retinal detachment, and were of average stature. This family was one of a group that presented with phenotypes overlapping those of both Marshall (154780) and Stickler (604841) syndromes.
In their case 8, representing several affected family members, Annunen et al. (1999) found a 4-bp deletion involving the last 3 bp of exon 50 and the first bp of intron 50. Affected family members showed typical features of Marshall syndrome (MRSHS; 154780), including hearing loss, retinal detachment, and midfacial hypoplasia, but no palatal defect. Other features included abnormal frontal sinuses, intracranial ossifications, and thick calvarium, which are frequent features of Marshall syndrome but not of Stickler syndrome (STL2; 604841).
In 2 families with Stickler syndrome and the type 2 (beaded) vitreous phenotype (STL2; 604841), Martin et al. (1999) found the causative mutation to be the substitution of a glycine residue in the collagen helix, likely to have a dominant-negative effect. The quantitatively minor type V and XI collagens form heterotypic fibrils with a more abundant type II fibrillar collagen and help to regulate fibril assembly and diameter. Type XI collagen is more abundant in tissues expressing type II collagen so it is to be expected that mutations in either COL2A1 or COL11A1 can cause Stickler syndrome. However, COL11A2 is not expressed in the vitreous, which explains why mutations in this gene give rise to some manifestations of Stickler syndrome but without eye anomalies (e.g., 120290.0001). In 1 family, analysis of cDNA between bases 930-1892 detected a deletion. Cloning and sequencing showed a loss of 54 bp from the RT-PCR product. Amplification and sequencing of this region of the gene showed that the 54 bp corresponded to a complete exon (gly16-gln33), which was present in both alleles of an affected individual. The 5-prime donor splice sequence of the following intron was found to be normal in both alleles. However, one allele had a single base deletion which altered the 3-prime acceptor splice site of the preceding intron, from consensus ag to tg. This led to skipping of the 54-bp exon from the mRNA.
In a 28-year-old female clinically diagnosed with Marshall syndrome (MRSHS; 154780), Annunen et al. (1999) identified heterozygosity for a 1-bp insertion at the splice donor site of intron 50 of the COL11A1 gene (IVS50DS+3insT). Neither parent had the insertion.
In a 36-year-old female diagnosed with MRSHS, Majava et al. (2007) identified heterozygosity for the 1-bp insertion in IVS50 of the COL11A1 gene. The patient had severe midface hypoplasia with a short nose, anteverted nares, and bulging eyes; she also had sensorineural hearing loss, but no signs of ectodermal dysplasia. Type I vitreous anomaly was diagnosed in this patient by an experienced ophthalmologist, suggesting that vitreous phenotype does not always allow prediction of the defective gene in Stickler and Marshall syndrome cases.
In Japanese populations, Mio et al. (2007) found an association between a functional single-nucleotide polymorphism in the COL11A1 gene, 4603C-T (rs1676486), and susceptibility to lumbar disc herniation (603932) (p = 3.3 x 10(-6)). The authors showed that levels of the transcript containing the disease-associated allele were lower because of its decreased stability.
In a patient of European descent with fibrochondrogenesis (FBCG1; 228520), Tompson et al. (2010) identified compound heterozygosity for 2 mutations in the COL11A1 gene: a 1-bp duplication (1786dupG) in exon 18 that produced a frameshift and subsequent premature termination codon (Ala596GlyfsTer8), and a 3124G-A transition in exon 42 predicting a triple-helical gly1042-to-arg (G1042R) substitution (120280.0009). By allele-specific expression based on the missense mutation, Tompson et al. (2010) showed that the frameshift mutation causes nonsense-mediated decay. The mother had had myopia from about 10 years of age, was of average stature, had normal hearing, and was heterozygous for the missense mutation. The father reported that he had hearing loss at age 7 and wore glasses from 6 years of age, but his DNA was not available for testing.
For discussion of the gly1042-to-arg (G1042R) mutation in the COL11A1 gene that was found in compound heterozygous state in a patient with fibrochondrogenesis (FBCG1; 228520) by Tompson et al. (2010), see 120280.0008.
In a patient with a milder form of fibrochondrogenesis (FBCG1; 228520), born to a father of European descent and an African American mother, Tompson et al. (2010) identified compound heterozygosity for 2 mutations in the COL11A1 gene: a 2386G-C transversion in exon 30 that predicts a gly796-to-arg (G796R) substitution, and a 3943G-T transversion in exon 53 that predicts a gly1315-to-ter (G1315X) substitution (120280.0011). The mother had mild myopia and was a carrier for the missense mutation. The father had mild hearing loss and was heterozygous for the null mutation.
For discussion of the gly1315-to-ter (G1315X) mutation in the COL11A1 gene that was found in compound heterozygous state in a patient with fibrochondrogenesis (FBCG1; 228520) by Tompson et al. (2010), see 120280.0010.
In a 3-year-old boy with Marshall syndrome (MRSHS; 154780), Ala-Kokko and Shanske (2009) identified heterozygosity for a G-A transition in intron 50 of the COL11A1 gene (IVS50+1G-A). The same mutation was present in his mildly affected mother; however, the amount of mutant allele was only about 20% of the wildtype allele in the mother's sample. Similar results were obtained with both lymphocytes and skin fibroblasts from the mother, strongly suggesting that the mutation was mosaic in the mother and that mosaicism was the reason for her less severe manifestations.
In affected members of a large 4-generation family of European descent with autosomal dominant deafness-37 (DFNA37; 618533), Booth et al. (2019) identified a heterozygous A-to-C transversion in intron 4 (c.652-2A-C, NM_080629.1) of the COL11A gene, resulting in a splice site alteration. The mutation, which was found by a combination of linkage analysis and exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. It was not found in the 1000 Genomes Project, Exome Variant Server, ExAC, or gnomAD databases. Using a minigene construct to express the mutation in cell lines, the authors showed that the mutation resulted in the skipping of exon 5, causing an in-frame deletion and a peptide lacking residues 218 to 260 in the N-terminal propeptide. The mutation was predicted to affect all 5 transcripts of the gene, but possibly had a 'leaky' effect.
In a German father and daughter (family 1) with nonsyndromic prelingual sensorineural hearing loss (DFNA37; 618533), Rad et al. (2021) identified heterozygosity for a splicing mutation (c.652-1G-C, NM_080629.2) in intron 4 of the COL11A1 gene. An in vitro splicing assay revealed that the c.652-1C variant impacts splicing through the loss of an acceptor site and activation of 2 cryptic splice acceptor sites in exon 5 that cause in-frame deletions. TA cloning analysis showed that 67% of amplicons used the first cryptic splice site (r.652_663del; Gly218_Gln221del) and 33% of amplicons used the second cryptic acceptor site (r.652_666del; Gly218_Gln222del).
In a German mother and son (family 2) with nonsyndromic prelingual sensorineural hearing loss (DFNA37; 618533), Rad et al. (2021) identified heterozygosity for a splicing mutation (c.4338+2T-C, NM_080629.2) in intron 57 of the COL11A1 gene. Neither of the mother's parents carried the mutation, suggesting that it arose de novo in the mother; paternity testing was not possible for confirmation. An in vitro splicing assay revealed that the c.4338+2C variant results in 3 abnormally spliced amplicons that include the activation of 2 cryptic splice donor sites in intron 57 and skipping of exon 57. In TA cloning analysis, 87% of amplicons showed evidence of skipping of exon 57, 6.5% used the first cryptic donor site (r.4338_4339ins4338+1_4338+4), and 6.5% used the second cryptic donor site (r.4338_4339ins4338+1_4338+30).
In 5 affected members of a 4-generation Italian family with nonsyndromic pre- and postlingual sensorineural hearing loss (DFNA37; 618533), Ciorba et al. (2021) identified heterozygosity for a c.494A-T transversion (c.494A-T, NM_001854.3) in the COL11A1 gene, resulting in a his165-to-leu (H165L) substitution within the laminin G domain. The mutation segregated fully with disease in the family and was not found in the dbSNP, 1000 Genomes Project, ExAC, or gnomAD databases.
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