Tissue‐specific expression of type XII collagen during mouse embryonic development

Oh, S. Paul; Griffith, C.M.; Hay, Elizabeth D.; Olsen, Bjørn R.

doi:10.1002/aja.1001960105

Cited by 76 publications

(54 citation statements)

References 14 publications

(21 reference statements)

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“…5, A-C). Similar to the findings in chick (34), there is a strong expression of collagen XII in tendon, perichondrium, and periosteum (35). Tenascin-X is expressed throughout the dermis of mouse embryos, and the staining decreases toward the epidermis.…”

Section: The Nc3 Domain Of Collagen XII Contains the Binding Site Forsupporting

confidence: 70%

Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain

Veit

Hansen

Keene

et al. 2006

Journal of Biological Chemistry

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Large oligomeric proteins often contain several binding sites for different molecules and can therefore induce formation of larger protein complexes. Collagen XII, a multidomain protein with a small collagenous region, interacts with fibrillar collagens through its C-terminal region. However, no interactions to other extracellular proteins have been identified involving the non-collagenous N-terminal NC3 domain. To further elucidate the components of protein complexes present close to collagen fibrils, different extracellular matrix proteins were tested for interaction in a solid phase assay. Binding to the NC3 domain of collagen XII was found for the avian homologue of tenascin-X that in humans is linked to Ehlers-Danlos disease. The binding was further characterized by surface plasmon resonance spectroscopy and supported by immunohistochemical co-localization in chick and mouse tissue. On the ultrastructural level, detection of collagen XII and tenascin-X by immunogold labeling confirmed this finding.The integrity of extracellular matrix is maintained by supramolecular networks assembled by a large variety of matrix macromolecules. Among those is the group of 28 different collagen types so far described in the literature. Collagens are further subdivided into several families reflecting their assemblyforming properties (1). As a common feature, fibril-associated collagens with interrupted triple helices (FACITs) 2 comprise at least two collagenous domains interrupted by non-collagenous domains. Collagen XII is a member of the FACIT subfamily, and its three chains are encoded by a single gene. The two collagenous domains (Col1 and Col2) are interrupted and flanked by three non-collagenous domains (NC1-NC3), of which the large trimeric NC3 domain contains up to 90% of the molecular mass of collagen XII. The N-terminal NC3 part of each polypeptide chain consists of two to four von Willebrand factor type A domains, several fibronectin type III repeats, and a thrombospondin N-terminal domain (2, 3). The size of the protein is variable due to two alternative splice sites located at the 5Ј-and 3Ј-ends of the collagen XII mRNA. Especially remarkable is the splicing mechanism that produces mRNA encoding for NC3 domains that differ ϳ100 kDa in mass, denoted as XIIA for the large form and as XIIB for the small form (4, 5). The other alternative splicing generates two NC1 domains of similar size, termed -1 or -2, which results in the nomenclature of the four different collagen XII isoforms: XIIA-1, XIIA-2, XIIB-1 and XIIB-2 (for overview of the domain structure please refer to Fig. 2A) (6). The isoforms differ in their histological and developmental distribution: the large forms XIIA-1 and XIIA-2 are preferably expressed during embryonic stages, whereas the expression of the small forms persists in adult tissues (7). Furthermore, the small isoform XIIB-1 predominantly occurs in ligaments and tendons, whereas the XIIB-2 shows a more widespread expression (6). The isoforms also differ in their biochemical properties. The ...

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Section: The Nc3 Domain Of Collagen XII Contains the Binding Site Forsupporting

confidence: 70%

Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain

Veit

Hansen

Keene

et al. 2006

Journal of Biological Chemistry

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“…The cDNA sequence covering the 3' region of mouse type XI1 collagen has previously been described (Oh et al, 1993). Using the 5' RACE protocol and by screening of a mouse cDNA library we extended the sequence by about 6.5 kb to the translational start codon.…”

Section: Sequence and Domain Structurementioning

confidence: 99%

Primary structure of the long and short splice variants of mouse collagen XII and their tissue‐specific expression during embryonic development

Böhme

et al. 1995

Developmental Dynamics

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Type XI1 collagen, a member of the FACIT group of extracellular matrix proteins, consists of molecules that are trimers of orl(XI1) chains. The three chains in each molecule form a cross-shaped structure with a central globule from which a triple-helical tail and three finger-like regions (containing von Willebrand factor A-like domains and fibronectin type I11 repeats) extend. cDNA cloninglsequencing of chicken al(XI1) collagen and protein studies with mouse, bovine, and human material suggest that the cyl(XI1) collagen gene gives rise to two molecular variants, differing in the length of the finger-like regions, by alternative splicing of the primary transcript. To provide a basis for studies of the function of the two variants in an organism that can be genetically manipulated, we have isolated and sequenced mouse cDNAs encoding both splice variants. The sequence provides the first complete nucleotide and amino acid sequence of mammalian type XI1 collagen. From these cDNAs we have generated digoxigenin-labeled RNA probes for in situ hybridization of developing mouse embryos to find out whether the splicing mechanism responsible for generation of the two forms is developmentally regulated. The results, combined with Northern blot and RT-PCR analysis of RNA from embryos at various developmental stages, demonstrate that the long form of collagen XII, XIIA, is the predominant form at early stages (ED7 and 11); at later stages of development (ED15 and 17) the short form, XIIB, becomes the major form. As the short form becomes the major product, the long splice variant continues to be expressed in several tissues, even after birth. An exception is dermis, which is positive for the long form up to embryonic day 15, but negative at day 18, when only the short form RNA can be detected. o 1995 Wiley-Liss, Inc.

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“…23 Subsequently, PL fibroblasts express ␣-SMA 24 as well as collagen XII, 25 and in wounded periodontal tissues expression of these proteins is an indicator of soft-tissue regeneration. Notably, during early stages of wound healing, OPN 26 is expressed by mineralized and nonmineralized tissue-forming PL cells (reviewed by Denhardt and Guo 27 ).…”

Section: Discussionmentioning

confidence: 99%

Healing of Periodontal Tissues Following Transplantation of Cells in a Rat Orthodontic Tooth Movement Model

Nayak

Wiltshire

Ganss

et al. 2008

The Angle Orthodontist

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Objective: To determine the fate and differentiation of transplanted periodontal ligament (PL) precursor cells and mouse embryonic stem (ES) cells and their relative capacity to regenerate wounded periodontium. Materials and Methods: Orthodontic tooth movement was introduced 24 hours before transplantation of PL or ES cells, and rats were euthanized either 24 hours or 72 hours after cell transplantation. The control rats received either no tooth movement and no cell transplantation or tooth movement and no cell transplantation. Differentiation of transplanted cells was assessed from mandibular periodontal histological tissue sections by immunohistochemical methods using monoclonal antibodies against PL cell differentiation markers. Data were analyzed using Student's t-test at a significance level of P ϭ .05. Results: Transplantation of PL and ES cells resulted in a higher number of osteopontin, bone sialoprotein, and ␣-smooth muscle actin labeled transplanted cells, predominantly around the blood vessels of the periodontium in study rats compared with control rats (cell transplantation but no orthodontic tooth movement, P ϭ .05). Combined treatments of tooth movement and cell transplantation resulted in enhanced regeneration of the periodontium as a result of tooth movement. Transplantation of PL cells induced a higher number of differentiating cells in the PL and alveolar bone than did transplantation of ES cells. Conclusions: Orthodontic tooth movement promotes the differentiation of transplanted cells, and the differentiation occurs predominantly in the paravascular areas of the periodontium. In terms of regeneration of wounded periodontium, transplantation of PL cells produced a higher level of regeneration than ES cells, possibly because of PL cell plasticity and the capacity to undergo effective differentiation in the periodontal cellular microenvironment.

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Tissue‐specific expression of type XII collagen during mouse embryonic development

Cited by 76 publications

References 14 publications

Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain

Collagen XII Interacts with Avian Tenascin-X through Its NC3 Domain

Primary structure of the long and short splice variants of mouse collagen XII and their tissue‐specific expression during embryonic development

Healing of Periodontal Tissues Following Transplantation of Cells in a Rat Orthodontic Tooth Movement Model

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