Evolution of collagens

Exposito, Jean‐Yves; Cluzel, Caroline; Garrone, R.; Lethias, Claire

doi:10.1002/ar.10162

Cited by 168 publications

(132 citation statements)

References 122 publications

Supporting

Mentioning

124

Contrasting

Unclassified

Order By: Relevance

“…In our study, collagen types I11 and I were co-localized, and looked morphologically so similar that each of them could be identified only through using immunogold staining. Collagen types IV and VI belong to the non-fibrillar collagen subfamily, with collagen type IV found in basement membrane and collagen type VI in most body tissues, usually in the form of beaded filaments, as noted on TEM [7].…”

Section: Discussionmentioning

confidence: 90%

“…Collagen types I, Under scanning electron microscopy, the SSCT looks like multiple parallel sheets linked to each other by collagen bundles [6,12]. Biochemically, human SSCT has been I11 and V belong to the fibrillar collagen family [7]. These collagens participate in the formation of cross-striated fibrils, and share the characteristic repeating collagenous domain triplet Gly-X-Y in each chain [7].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Immunolocalization of collagen types in the subsynovial connective tissue within the carpal tunnel in humans

Jinrok¹,

Zhao²,

Amadio³

et al. 2005

Journal Orthopaedic Research

View full text Add to dashboard Cite

The tenosynovium within the carpal tunnel consists of a single layer of synovial cells, which lines the bursae within the carpal tunnel, and the subsynovial connective tissue (SSCT), which contains the tendon vasculature and other structural elements. In this study, we used immunogold labeling to localize collagen types within the SSCT in three cadaver specimens and three patients with carpal tunnel syndrome. Positive labeling for collagen types I, 111 and VI was found with immunoelectron microscopy. Collagen types I and 111 were codistributed within the SSCT. Type VI was primarily located in microfibrillar structures between collagen bundles, between elastin and collagen bundles and between collagen bundles and cells. There was no difference in the distribution of collagen types when comparing cadaver specimens and carpal tunnel patients.

show abstract

Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Immunolocalization of collagen types in the subsynovial connective tissue within the carpal tunnel in humans

Jinrok¹,

Zhao²,

Amadio³

et al. 2005

Journal Orthopaedic Research

View full text Add to dashboard Cite

show abstract

“…The A and B clades are linked to the HOX and Notch paralogons, respectively (2,24,25). From their exon/intron organizations, the presence of a TSPN module in their Npropeptide and phylogenetic analyses, the C clade is more closely related to the B clade than the A clade (11,12).…”

Section: Phylogenetic Studiesmentioning

confidence: 99%

“…Fibrillar collagens are present from sponges to humans and are the primary component of striated fibrils (1,2). A fibrillar procollagen molecule is made of three identical or different pro-␣ chains.…”

mentioning

confidence: 99%

Invertebrate Data Predict an Early Emergence of Vertebrate Fibrillar Collagen Clades and an Anti-incest Model

Aouacheria

Cluzel

Lethias

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Chem. 278, 31067-31077). In this model, a rare genomic event leads to the formation of the founder vertebrate fibrillar collagen gene prior to the early vertebrate genome duplications and the radiation of the vertebrate fibrillar collagen clades (A, B, and C). Here, we present the modular structure of the fibrillar collagen chains present in different invertebrates from the protostome Anopheles gambiae to the chordate Ciona intestinalis. From their modular structure and the use of a triple helix instead of C-propeptide sequences in phylogenetic analyses, we were able to show that the divergence of A and B clades arose early during evolution because ␣ chains related to these clades are present in protostomes. Moreover, the event leading to the divergence of B and C clades from a founder gene arose before the appearance of vertebrates; altogether these data contradict the Boot-Handford model. Moreover, they indicate that all the key steps required for the formation of fibrils of variable structure and functionality arose step by step during invertebrate evolution.Fibrillar collagens are present from sponges to humans and are the primary component of striated fibrils (1, 2). A fibrillar procollagen molecule is made of three identical or different pro-␣ chains. Each pro-␣ chain contains a central triple helix made of ϳ338 Gly-Xaa-Yaa triplets flanked by non-collagenous telopeptide regions, which in turn are flanked by the N-and C-propeptides. The C-propeptide is known to contain the most conserved regions of the fibrillar ␣ chains. This domain is involved in ␣ chain recognition and in the registration of the major triple helical domain, an important step preceding elongation of the triple helix from the carboxyl to the amino terminus. In vertebrates, a short region of the C-propeptide appears to be involved in chain recognition (3). Recently, Boot-Handford and Tuckwell (4) indicated that most of this recognition sequence is absent in all invertebrate fibrillar chains characterized to date. During the extracellular maturation of procollagen molecules, the propeptides are generally removed by specific proteinases. The resultant collagen molecules participate in fibril formation.In humans, fibrillar collagens are subdivided quantitatively into major (types I-III) and minor (types V/XI) collagens. According to the collagen types incorporated into the fibrils and their ratio, the partial processing of the N-propeptide, and interactions with other extracellular matrix components, the shape and functional properties of the fibrils can vary. The importance of quantitatively minor collagens in the regulation of fibril diameter has been pointed out in several studies (5-7). From the model of Linsenmayer et al. (6), the retention of the type V N-propeptide at the surface of types I/V heterotypic fibrils is one of the key elements regulating the diameter of these fibrils.From phylogenetic studies and the exon/intron organization, it has been shown that vertebrate fibrillar collagens can be divided into two clades (8 -10): the A...

show abstract

“…1C) (47,48). Both the length and distance of the heptad repeats from the end of the collagen triple-helical region were similar to those in the vertebrate fibrillar collagens (Fig.…”

Section: C-terminal Coiled Coils In Other Members Of the Collagenmentioning

confidence: 99%

α-Helical Coiled-coil Oligomerization Domains Are Almost Ubiquitous in the Collagen Superfamily

McAlinden

Smith

Sandell

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

␣-Helical coiled coils are widely occurring protein oligomerization motifs. Here we show that most members of the collagen superfamily contain short, repeating heptad sequences typical of coiled coils. Such sequences are found at the N-terminal ends of the C-propeptide domains in all fibrillar procollagens. When fused C-terminal to a reporter molecule containing a collagen-like sequence that does not spontaneously trimerize, the Cpropeptide heptad repeats induced trimerization. C-terminal heptad repeats were also found in the oligomerization domains of the multiplexins (collagens XV and XVIII). N-terminal heptad repeats are known to drive trimerization in transmembrane collagens, whereas fibril-associated collagens with interrupted triple helices, as well as collagens VII, XIII, XXIII, and XXV, were found to contain heptad repeats between collagen domains. Finally, heptad repeats were found in the von Willebrand factor A domains known to be involved in trimerization of collagen VI, as well as in collagen VII. These observations suggest that coiled-coil oligomerization domains are widely used in the assembly of collagens and collagen-like proteins.The mechanisms controlling chain oligomerization in extracellular matrix and related proteins are currently topics of active research (1, 2). In the case of the collagen superfamily, which includes both collagens and collagen-like proteins (3-5), a number of structural features have been identified that are essential for bringing together component polypeptide chains with the correct stoichiometry, thus leading to folding of the triple helix. Early studies on the procollagen precursors of the fibrillar collagens (types I-III, V, and XI) (6) showed that the C-propeptide regions are necessary to direct correct chain association, which is followed by zipper-like folding of the triple helix in the C-to N-terminal direction (7). This concept was subsequently extended to basement membrane collagen type IV (8 -10), microfibril-forming collagen VI (11, 12), members of the C1q family (13) including collagens VIII and X (14 -17) and the emilins (18), and the FACITs 1 (19 -21).␣-Helical coiled coils have been shown to be oligomerization domains in both collagens and collagen-like proteins. The paradigm here is the collectin family (22), which includes the lung surfactant proteins (SP-A and SP-D), mannan-binding proteins (MBP-A and MBP-C), conglutinin, and collectin-43. Collectins are trimeric molecules in which each chain contains a collagenlike domain followed by an ␣-helical coiled-coil region and then a carbohydrate recognition domain (CRD). The amino acid sequence of the coiled-coil domain is characterized by up to four heptad repeats (a-b-c-d-e-f-g) in which hydrophobic amino acid residues occur at positions a and d (23). Three-dimensional structures of the coiled-coil and CRD regions in MBP and SP-D show that chains within the trimer are associated via a threestranded coiled coil, with the three CRDs arranged as distinct lobes (24 -26). Several studies have shown that the co...

show abstract

Evolution of collagens

Cited by 168 publications

References 122 publications

Immunolocalization of collagen types in the subsynovial connective tissue within the carpal tunnel in humans

Immunolocalization of collagen types in the subsynovial connective tissue within the carpal tunnel in humans

Invertebrate Data Predict an Early Emergence of Vertebrate Fibrillar Collagen Clades and an Anti-incest Model

α-Helical Coiled-coil Oligomerization Domains Are Almost Ubiquitous in the Collagen Superfamily

Contact Info

Product

Resources

About