* 120190

COLLAGEN, TYPE V, ALPHA-2; COL5A2


Alternative titles; symbols

AB COLLAGEN


HGNC Approved Gene Symbol: COL5A2

Cytogenetic location: 2q32.2     Genomic coordinates (GRCh38): 2:189,031,898-189,441,111 (from NCBI)


Gene-Phenotype Relationships
Location Phenotype Phenotype
MIM number
Inheritance Phenotype
mapping key
2q32.2 Ehlers-Danlos syndrome, classic type, 2 130010 AD 3

TEXT

Description

Type V collagen has 3 varieties of alpha chains: alpha-1 (COL5A1, 120215); alpha-2 (COL5A2), and alpha-3 (COL5A3; 120216). It has a specific pericellular distribution and is not considered an interstitial collagen. It is thought also to provide an inner core for large collagen fibers. Thus, collagen V may aid in the orientation of large diameter fibers. (summary by Emanuel et al., 1985).


Cloning and Expression

Burgeson et al. (1976) identified in human fetal membranes (placenta) 2 novel genetically distinct collagen polypeptide chains, which are subunits of a hitherto unknown molecular species of collagen. They were tentatively labeled alpha-A and alpha-B. The existence of a 'new' species of collagen containing one A and two B alpha chains was suggested. This is called collagen V and presumably is determined by 2 loci. Placental collagen is sometimes referred to as AB collagen. Some have considered it to consist of 2 separate molecules, one composed of 3 alpha-A chains and one composed of 3 alpha-B chains. Others view it as a trimer of 1 alpha-A and 2 alpha-B chains. Brown and Weiss (1979) concluded that these are 2 separate molecules (and perhaps a third consisting of 3 alpha-C chains), the first option, and that all 3 chains are derived from one basic chain through posttranslational modification. Type V collagen is usually found between the basement membrane and interstitial space.


Mapping

Emanuel et al. (1985) concluded that both the alpha-1(III) and the alpha-2(V) procollagen genes map to 2q24.3-q31. To the time of this report, this was the only example of synteny of procollagen genes.

By in situ hybridization and analysis of DNA from somatic cell hybrids, Huerre-Jeanpierre et al. (1986) obtained results consistent with the assignment of COL5A2 to 2q24.3-q31 by Emanuel et al. (1985). Tsipouras et al. (1988) demonstrated that the COL3A1 locus (120180) and the COL5A2 locus are very close together; they found a maximum lod score of 9.33 at a recombination fraction of 0.00.

Hartz (2013) mapped the COL5A2 gene to chromosome 2q32.2 based on an alignment of the COL5A2 sequence (GenBank Y14690) with the genomic sequence (GRCh37).


Gene Function

By microarray analysis, Jun et al. (2001) demonstrated expression of the COL5A2 gene in human donor corneas.


Molecular Genetics

Michalickova et al. (1998) identified mutations in the COL5A2 gene in 2 unrelated patients with Ehlers-Danlos classic type 2 (EDSCL2; 130010) (formerly the severe type I form of EDS). The first proband was heterozygous for a 7-bp deletion that resulted in skipping of exon 27 (120190.0001), whereas the second proband was heterozygous for a single-nucleotide substitution that resulted in skipping of exon 28 (120190.0002). Cultured dermal fibroblasts from both probands produced about equal amounts of the normal and mutant alpha-2(V) mRNAs and protein chains. The dermis from the first proband contained a sparse collagen fibrillar network with great variability in collagen fibril sizes and shapes. The dermal collagens were also abnormally soluble. Bone cells from the first proband also produced about equal amounts of the normal and mutant mRNAs. However, the collagen fibrillar architecture and collagen solubility of the bone matrix were normal. The findings indicated that heterozygous mutations in the COL5A2 gene can produce the classic severe phenotype. Michalickova et al. (1998) suggested that type V collagen plays a more important role in collagen fibrillogenesis of dermis rather than of bone.

Symoens et al. (2012) analyzed COL5A1 (120215) and COL5A2 in 126 patients with a diagnosis or suspicion of classic EDS. In 93 patients, a type V collagen defect was found, of which 73 were COL5A1 mutations (see EDSCL1, 130000), 13 were COL5A2 mutations, and 7 were COL5A1 null-alleles (see 130000 and 130010) with mutation unknown. The majority of the 73 COL5A1 mutations generated a COL5A1 null-allele, whereas one-third were structural mutations, scattered throughout COL5A1. All COL5A2 mutations were structural mutations. Reduced availability of type V collagen appeared to be the major disease-causing mechanism, besides other intra- and extracellular contributing factors. All type V collagen defects were identified within a group of 102 patients fulfilling all major clinical Villefranche criteria, that is, skin hyperextensibility, dystrophic scarring and joint hypermobility. No COL5A1/COL5A2 mutation was detected in 24 patients who displayed skin and joint hyperextensibility but lacked dystrophic scarring. Overall, over 90% of patients fulfilling all major Villefranche criteria for classic EDS were shown to harbor a type V collagen defect, indicating that this is the major, if not the only, cause of classic EDS.


Animal Model

The tissue-specific organization of collagen molecules into tridimensional macroaggregates determines the physiomechanical properties of most connective tissues. It had been postulated that quantitatively minor types V and XI collagen regulate the growth of type I and type II collagen fibrils, respectively. To test this hypothesis, Andrikopoulos et al. (1995) created mice homozygous for deletion of the Col5a2 gene. These mice survived poorly, possibly because of complications from spinal deformities, and exhibited skin and eye abnormalities caused by disorganized type I collagen fibrils.


ALLELIC VARIANTS ( 7 Selected Examples):

.0001 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, 7-BP DEL
  
RCV000018736

Michalickova et al. (1998) screened 28 unrelated individuals and families with typical classic Ehlers-Danlos syndrome for mutations in type V collagen. Of 26 patients in whom no mutations were identified in the COL5A1 gene, they identified abnormalities of COL5A2 cDNA in 2 patients (EDSCL2; 130010). In 1 proband (patient EDS3), the mutation was a 54-bp deletion in heterozygous state (nucleotides 1924-1977 of COL5A2 cDNA). The deletion removed 18 amino acids, gly430 to pro447, from the triple helical domain of the alpha-2(V) chain. The region corresponded to a 54-bp exon, tentatively considered exon 27. This was thought to be due to deletion of the splice acceptor site as a result of a 7-bp deletion that included the consensus ag dinucleotide of the 3-prime splice site of intron 26 and the most 5-prime nucleotides of exon 27.


.0002 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, IVS28DS, G-T, +1
  
RCV000018737

See 120190.0001. In a patient (patient EDS38) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Michalickova et al. (1998) found a heterozygous deletion of 54 bp, removing 18 amino acids from the triple helical domain of the alpha-2(V) chain. In this case, however, nucleotides 1978 to 2031 were removed. It was thought that the mutation had resulted in deletion of exon 28. The patient was found to be heterozygous for a single nucleotide substitution that changed the consensus gt dinucleotide of the 5-prime splice donor of intron 28 to tt. They concluded from the nature of the mutation that the missing splice donor site caused exon 28 to be skipped during splicing of the mutant allele of COL5A2. Studies in the parents indicated that this was a new mutation.


.0003 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, GLY934ARG
  
RCV000018738...

In 3 family members with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Richards et al. (1998) found a G-C base change in the COL5A2 gene, resulting in the substitution of arginine for glycine within the triple helical domain at position 934.


.0004 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, c.2544+2delT
  
RCV000609676

In a patient (patient EDS2) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a splice site mutation (c.2544+2delT, NM_000393.2) in the COL5A2 gene, predicted to result in the skipping of exon 36.


.0005 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, 1-BP DEL, 4289T
  
RCV000615676

In a patient (patient EDS2) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a 1-bp deletion (c.4289delT) in the COL5A2 gene, predicted to result in a frameshift and a premature termination codon (c.4289delT, NM_000393.2).


.0006 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, c.3139-2A-G
  
RCV000604241

In a patient (patient EDS6) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a splice site mutation (c.3139-2A-G, NM_000393.2) in the COL5A2 gene, predicted to result in deletion of exon 43.


.0007 EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, c.1608+4T-C
  
RCV000610100

In a patient (patient EDS22) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a splice site mutation (c.1608+4T-C, NM_000393.2) in the COL5A2 gene, predicted to result in deletion of exon 22.


REFERENCES

  1. Andrikopoulos, K., Liu, X., Keene, D. R., Jaenisch, R., Ramirez, F. Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly. Nature Genet. 9: 31-36, 1995. [PubMed: 7704020, related citations] [Full Text]

  2. Brown, R. A., Weiss, J. B. Type V collagen: possible shared identity of alpha-A, alpha-B and alpha-C chains. FEBS Lett. 106: 71-75, 1979. [PubMed: 499505, related citations] [Full Text]

  3. Burgeson, R. E., El Adli, F. A., Kaitila, I. J., Hollister, D. W. Fetal membrane collagens: identification of two new collagen alpha chains. Proc. Nat. Acad. Sci. 73: 2579-2583, 1976. [PubMed: 1066666, related citations] [Full Text]

  4. Emanuel, B. S., Cannizzaro, L. A., Seyer, J. M., Myers, J. C. Human alpha-1(III) and alpha-2(V) procollagen genes are located on the long arm of chromosome 2. Proc. Nat. Acad. Sci. 82: 3385-3389, 1985. [PubMed: 3858826, related citations] [Full Text]

  5. Hartz, P. A. Personal Communication. Baltimore, Md. 10/28/2013.

  6. Huerre-Jeanpierre, C., Henry, I., Bernard, M., Gallano, P., Weil, D., Grzeschik, K.-H., Ramirez, F., Junien, C. The pro-alpha-2(V) collagen gene (COL5A2) maps to 2q14-2q32, syntenic to the pro-alpha-1(III) collagen locus (COL3A1). Hum. Genet. 73: 64-67, 1986. [PubMed: 3011647, related citations] [Full Text]

  7. 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, related citations] [Full Text]

  8. Malfait, F., Coucke, P., Symoens, S., Loeys, B., Nuytinck, L., De Paepe, A. The molecular basis of classic Ehlers-Danlos syndrome: a comprehensive study of biochemical and molecular findings in 48 unrelated patients. Hum. Mutat. 25: 28-37, 2005. [PubMed: 15580559, related citations] [Full Text]

  9. Michalickova, K., Susic, M., Willing, M. C., Wenstrup, R. J., Cole, W. G. Mutations of the alpha-2(V) chain of type V collagen impair matrix assembly and produce Ehlers-Danlos syndrome type I. Hum. Molec. Genet. 7: 249-255, 1998. [PubMed: 9425231, related citations] [Full Text]

  10. Richards, A. J., Martin, S., Nicholls, A. C., Harrison, J. B., Pope, F. M., Burrows, N. P. A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II. J. Med. Genet. 35: 846-848, 1998. [PubMed: 9783710, related citations] [Full Text]

  11. Sage, H., Bornstein, P. Characterization of a novel collagen chain in human placenta and its relation to AB collagen. Biochemistry 18: 3815-3822, 1979. [PubMed: 224919, related citations] [Full Text]

  12. Symoens, S., Syx, D., Malfait, F., Callewaert, B., De Backer, J., Vanakker, O., Coucke, P., De Paepe, A. Comprehensive molecular analysis demonstrates type V collagen mutations in over 90% of patients with classic EDS and allows to refine diagnostic criteria. Hum. Mutat. 33: 1485-1493, 2012. [PubMed: 22696272, related citations] [Full Text]

  13. Tsipouras, P., Schwartz, R. C., Liddell, A. C., Salkeld, C. S., Weil, D., Ramirez, F. Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, located on the long arm of human chromosome 2. Genomics 3: 275-277, 1988. [PubMed: 3224983, related citations] [Full Text]

  14. van der Rest, M., Niyibizi, C., Fietzek, P. P. Human placental alpha-1(V)alpha-2(V)alpha-3(V) and [alpha-1(V)]-2-alpha-2(V) collagen heterotrimers. Ann. N.Y. Acad. Sci. 460: 517-519, 1985.


Patricia A. Hartz - updated : 10/28/2013
Nara Sobreira - updated : 2/25/2013
Jane Kelly - updated : 12/6/2002
Victor A. McKusick - updated : 8/9/2002
Michael J. Wright - updated : 11/9/1998
Victor A. McKusick - updated : 4/15/1998
Creation Date:
Victor A. McKusick : 6/4/1986
carol : 11/14/2018
carol : 04/05/2018
carol : 12/21/2017
carol : 12/21/2017
carol : 04/13/2015
mgross : 10/28/2013
carol : 2/25/2013
alopez : 8/20/2012
carol : 12/6/2002
tkritzer : 8/15/2002
tkritzer : 8/13/2002
tkritzer : 8/13/2002
terry : 8/9/2002
carol : 7/5/2001
alopez : 12/11/1998
terry : 11/9/1998
carol : 4/17/1998
terry : 4/15/1998
joanna : 11/12/1996
mark : 1/5/1996
terry : 1/3/1996
terry : 12/26/1995
supermim : 3/16/1992
carol : 10/1/1991
carol : 8/24/1990
supermim : 3/20/1990
ddp : 10/26/1989
root : 11/11/1988

* 120190

COLLAGEN, TYPE V, ALPHA-2; COL5A2


Alternative titles; symbols

AB COLLAGEN


HGNC Approved Gene Symbol: COL5A2

SNOMEDCT: 20766005;  


Cytogenetic location: 2q32.2     Genomic coordinates (GRCh38): 2:189,031,898-189,441,111 (from NCBI)


Gene-Phenotype Relationships

Location Phenotype Phenotype
MIM number
Inheritance Phenotype
mapping key
2q32.2 Ehlers-Danlos syndrome, classic type, 2 130010 Autosomal dominant 3

TEXT

Description

Type V collagen has 3 varieties of alpha chains: alpha-1 (COL5A1, 120215); alpha-2 (COL5A2), and alpha-3 (COL5A3; 120216). It has a specific pericellular distribution and is not considered an interstitial collagen. It is thought also to provide an inner core for large collagen fibers. Thus, collagen V may aid in the orientation of large diameter fibers. (summary by Emanuel et al., 1985).


Cloning and Expression

Burgeson et al. (1976) identified in human fetal membranes (placenta) 2 novel genetically distinct collagen polypeptide chains, which are subunits of a hitherto unknown molecular species of collagen. They were tentatively labeled alpha-A and alpha-B. The existence of a 'new' species of collagen containing one A and two B alpha chains was suggested. This is called collagen V and presumably is determined by 2 loci. Placental collagen is sometimes referred to as AB collagen. Some have considered it to consist of 2 separate molecules, one composed of 3 alpha-A chains and one composed of 3 alpha-B chains. Others view it as a trimer of 1 alpha-A and 2 alpha-B chains. Brown and Weiss (1979) concluded that these are 2 separate molecules (and perhaps a third consisting of 3 alpha-C chains), the first option, and that all 3 chains are derived from one basic chain through posttranslational modification. Type V collagen is usually found between the basement membrane and interstitial space.


Mapping

Emanuel et al. (1985) concluded that both the alpha-1(III) and the alpha-2(V) procollagen genes map to 2q24.3-q31. To the time of this report, this was the only example of synteny of procollagen genes.

By in situ hybridization and analysis of DNA from somatic cell hybrids, Huerre-Jeanpierre et al. (1986) obtained results consistent with the assignment of COL5A2 to 2q24.3-q31 by Emanuel et al. (1985). Tsipouras et al. (1988) demonstrated that the COL3A1 locus (120180) and the COL5A2 locus are very close together; they found a maximum lod score of 9.33 at a recombination fraction of 0.00.

Hartz (2013) mapped the COL5A2 gene to chromosome 2q32.2 based on an alignment of the COL5A2 sequence (GenBank Y14690) with the genomic sequence (GRCh37).


Gene Function

By microarray analysis, Jun et al. (2001) demonstrated expression of the COL5A2 gene in human donor corneas.


Molecular Genetics

Michalickova et al. (1998) identified mutations in the COL5A2 gene in 2 unrelated patients with Ehlers-Danlos classic type 2 (EDSCL2; 130010) (formerly the severe type I form of EDS). The first proband was heterozygous for a 7-bp deletion that resulted in skipping of exon 27 (120190.0001), whereas the second proband was heterozygous for a single-nucleotide substitution that resulted in skipping of exon 28 (120190.0002). Cultured dermal fibroblasts from both probands produced about equal amounts of the normal and mutant alpha-2(V) mRNAs and protein chains. The dermis from the first proband contained a sparse collagen fibrillar network with great variability in collagen fibril sizes and shapes. The dermal collagens were also abnormally soluble. Bone cells from the first proband also produced about equal amounts of the normal and mutant mRNAs. However, the collagen fibrillar architecture and collagen solubility of the bone matrix were normal. The findings indicated that heterozygous mutations in the COL5A2 gene can produce the classic severe phenotype. Michalickova et al. (1998) suggested that type V collagen plays a more important role in collagen fibrillogenesis of dermis rather than of bone.

Symoens et al. (2012) analyzed COL5A1 (120215) and COL5A2 in 126 patients with a diagnosis or suspicion of classic EDS. In 93 patients, a type V collagen defect was found, of which 73 were COL5A1 mutations (see EDSCL1, 130000), 13 were COL5A2 mutations, and 7 were COL5A1 null-alleles (see 130000 and 130010) with mutation unknown. The majority of the 73 COL5A1 mutations generated a COL5A1 null-allele, whereas one-third were structural mutations, scattered throughout COL5A1. All COL5A2 mutations were structural mutations. Reduced availability of type V collagen appeared to be the major disease-causing mechanism, besides other intra- and extracellular contributing factors. All type V collagen defects were identified within a group of 102 patients fulfilling all major clinical Villefranche criteria, that is, skin hyperextensibility, dystrophic scarring and joint hypermobility. No COL5A1/COL5A2 mutation was detected in 24 patients who displayed skin and joint hyperextensibility but lacked dystrophic scarring. Overall, over 90% of patients fulfilling all major Villefranche criteria for classic EDS were shown to harbor a type V collagen defect, indicating that this is the major, if not the only, cause of classic EDS.


Animal Model

The tissue-specific organization of collagen molecules into tridimensional macroaggregates determines the physiomechanical properties of most connective tissues. It had been postulated that quantitatively minor types V and XI collagen regulate the growth of type I and type II collagen fibrils, respectively. To test this hypothesis, Andrikopoulos et al. (1995) created mice homozygous for deletion of the Col5a2 gene. These mice survived poorly, possibly because of complications from spinal deformities, and exhibited skin and eye abnormalities caused by disorganized type I collagen fibrils.


ALLELIC VARIANTS 7 Selected Examples):

.0001   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, 7-BP DEL
SNP: rs786205103, ClinVar: RCV000018736

Michalickova et al. (1998) screened 28 unrelated individuals and families with typical classic Ehlers-Danlos syndrome for mutations in type V collagen. Of 26 patients in whom no mutations were identified in the COL5A1 gene, they identified abnormalities of COL5A2 cDNA in 2 patients (EDSCL2; 130010). In 1 proband (patient EDS3), the mutation was a 54-bp deletion in heterozygous state (nucleotides 1924-1977 of COL5A2 cDNA). The deletion removed 18 amino acids, gly430 to pro447, from the triple helical domain of the alpha-2(V) chain. The region corresponded to a 54-bp exon, tentatively considered exon 27. This was thought to be due to deletion of the splice acceptor site as a result of a 7-bp deletion that included the consensus ag dinucleotide of the 3-prime splice site of intron 26 and the most 5-prime nucleotides of exon 27.


.0002   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, IVS28DS, G-T, +1
SNP: rs786205104, ClinVar: RCV000018737

See 120190.0001. In a patient (patient EDS38) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Michalickova et al. (1998) found a heterozygous deletion of 54 bp, removing 18 amino acids from the triple helical domain of the alpha-2(V) chain. In this case, however, nucleotides 1978 to 2031 were removed. It was thought that the mutation had resulted in deletion of exon 28. The patient was found to be heterozygous for a single nucleotide substitution that changed the consensus gt dinucleotide of the 5-prime splice donor of intron 28 to tt. They concluded from the nature of the mutation that the missing splice donor site caused exon 28 to be skipped during splicing of the mutant allele of COL5A2. Studies in the parents indicated that this was a new mutation.


.0003   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, GLY934ARG
SNP: rs121912930, gnomAD: rs121912930, ClinVar: RCV000018738, RCV002513108

In 3 family members with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Richards et al. (1998) found a G-C base change in the COL5A2 gene, resulting in the substitution of arginine for glycine within the triple helical domain at position 934.


.0004   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, c.2544+2delT
SNP: rs1553514506, ClinVar: RCV000609676

In a patient (patient EDS2) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a splice site mutation (c.2544+2delT, NM_000393.2) in the COL5A2 gene, predicted to result in the skipping of exon 36.


.0005   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, 1-BP DEL, 4289T
SNP: rs1553512393, ClinVar: RCV000615676

In a patient (patient EDS2) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a 1-bp deletion (c.4289delT) in the COL5A2 gene, predicted to result in a frameshift and a premature termination codon (c.4289delT, NM_000393.2).


.0006   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, c.3139-2A-G
SNP: rs1553513971, ClinVar: RCV000604241

In a patient (patient EDS6) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a splice site mutation (c.3139-2A-G, NM_000393.2) in the COL5A2 gene, predicted to result in deletion of exon 43.


.0007   EHLERS-DANLOS SYNDROME, CLASSIC TYPE, 2

COL5A2, c.1608+4T-C
SNP: rs1553515517, ClinVar: RCV000610100

In a patient (patient EDS22) with classic Ehlers-Danlos syndrome (EDSCL2; 130010), Malfait et al. (2005) identified a splice site mutation (c.1608+4T-C, NM_000393.2) in the COL5A2 gene, predicted to result in deletion of exon 22.


See Also:

Sage and Bornstein (1979); van der Rest et al. (1985)

REFERENCES

  1. Andrikopoulos, K., Liu, X., Keene, D. R., Jaenisch, R., Ramirez, F. Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly. Nature Genet. 9: 31-36, 1995. [PubMed: 7704020] [Full Text: https://doi.org/10.1038/ng0195-31]

  2. Brown, R. A., Weiss, J. B. Type V collagen: possible shared identity of alpha-A, alpha-B and alpha-C chains. FEBS Lett. 106: 71-75, 1979. [PubMed: 499505] [Full Text: https://doi.org/10.1016/0014-5793(79)80697-3]

  3. Burgeson, R. E., El Adli, F. A., Kaitila, I. J., Hollister, D. W. Fetal membrane collagens: identification of two new collagen alpha chains. Proc. Nat. Acad. Sci. 73: 2579-2583, 1976. [PubMed: 1066666] [Full Text: https://doi.org/10.1073/pnas.73.8.2579]

  4. Emanuel, B. S., Cannizzaro, L. A., Seyer, J. M., Myers, J. C. Human alpha-1(III) and alpha-2(V) procollagen genes are located on the long arm of chromosome 2. Proc. Nat. Acad. Sci. 82: 3385-3389, 1985. [PubMed: 3858826] [Full Text: https://doi.org/10.1073/pnas.82.10.3385]

  5. Hartz, P. A. Personal Communication. Baltimore, Md. 10/28/2013.

  6. Huerre-Jeanpierre, C., Henry, I., Bernard, M., Gallano, P., Weil, D., Grzeschik, K.-H., Ramirez, F., Junien, C. The pro-alpha-2(V) collagen gene (COL5A2) maps to 2q14-2q32, syntenic to the pro-alpha-1(III) collagen locus (COL3A1). Hum. Genet. 73: 64-67, 1986. [PubMed: 3011647] [Full Text: https://doi.org/10.1007/BF00292666]

  7. 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]

  8. Malfait, F., Coucke, P., Symoens, S., Loeys, B., Nuytinck, L., De Paepe, A. The molecular basis of classic Ehlers-Danlos syndrome: a comprehensive study of biochemical and molecular findings in 48 unrelated patients. Hum. Mutat. 25: 28-37, 2005. [PubMed: 15580559] [Full Text: https://doi.org/10.1002/humu.20107]

  9. Michalickova, K., Susic, M., Willing, M. C., Wenstrup, R. J., Cole, W. G. Mutations of the alpha-2(V) chain of type V collagen impair matrix assembly and produce Ehlers-Danlos syndrome type I. Hum. Molec. Genet. 7: 249-255, 1998. [PubMed: 9425231] [Full Text: https://doi.org/10.1093/hmg/7.2.249]

  10. Richards, A. J., Martin, S., Nicholls, A. C., Harrison, J. B., Pope, F. M., Burrows, N. P. A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II. J. Med. Genet. 35: 846-848, 1998. [PubMed: 9783710] [Full Text: https://doi.org/10.1136/jmg.35.10.846]

  11. Sage, H., Bornstein, P. Characterization of a novel collagen chain in human placenta and its relation to AB collagen. Biochemistry 18: 3815-3822, 1979. [PubMed: 224919] [Full Text: https://doi.org/10.1021/bi00584a027]

  12. Symoens, S., Syx, D., Malfait, F., Callewaert, B., De Backer, J., Vanakker, O., Coucke, P., De Paepe, A. Comprehensive molecular analysis demonstrates type V collagen mutations in over 90% of patients with classic EDS and allows to refine diagnostic criteria. Hum. Mutat. 33: 1485-1493, 2012. [PubMed: 22696272] [Full Text: https://doi.org/10.1002/humu.22137]

  13. Tsipouras, P., Schwartz, R. C., Liddell, A. C., Salkeld, C. S., Weil, D., Ramirez, F. Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, located on the long arm of human chromosome 2. Genomics 3: 275-277, 1988. [PubMed: 3224983] [Full Text: https://doi.org/10.1016/0888-7543(88)90089-4]

  14. van der Rest, M., Niyibizi, C., Fietzek, P. P. Human placental alpha-1(V)alpha-2(V)alpha-3(V) and [alpha-1(V)]-2-alpha-2(V) collagen heterotrimers. Ann. N.Y. Acad. Sci. 460: 517-519, 1985.


Contributors:
Patricia A. Hartz - updated : 10/28/2013
Nara Sobreira - updated : 2/25/2013
Jane Kelly - updated : 12/6/2002
Victor A. McKusick - updated : 8/9/2002
Michael J. Wright - updated : 11/9/1998
Victor A. McKusick - updated : 4/15/1998

Creation Date:
Victor A. McKusick : 6/4/1986

Edit History:
carol : 11/14/2018
carol : 04/05/2018
carol : 12/21/2017
carol : 12/21/2017
carol : 04/13/2015
mgross : 10/28/2013
carol : 2/25/2013
alopez : 8/20/2012
carol : 12/6/2002
tkritzer : 8/15/2002
tkritzer : 8/13/2002
tkritzer : 8/13/2002
terry : 8/9/2002
carol : 7/5/2001
alopez : 12/11/1998
terry : 11/9/1998
carol : 4/17/1998
terry : 4/15/1998
joanna : 11/12/1996
mark : 1/5/1996
terry : 1/3/1996
terry : 12/26/1995
supermim : 3/16/1992
carol : 10/1/1991
carol : 8/24/1990
supermim : 3/20/1990
ddp : 10/26/1989
root : 11/11/1988