Bovine type XII collagen: Amino acid sequence of a 10 kDa pepsin fragment from periodontal ligament reveals a high degree of homology with the chicken α<sub>1</sub>(XII) sequence

Dublet, Bernard; Dixon, Eric P.; Miguel, Elisa de; Rest, Michel van der

doi:10.1016/0014-5793(88)81379-6

Cited by 24 publications

(8 citation statements)

References 11 publications

(12 reference statements)

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“…The periodontal ligament (PDL) contains fibril-forming collagen types I and III (Butler et al, 1975;Limeback et al, 1978;Limeback and Sodek, 1979) as well as type XII, a member of Fibril Associated Collagens with Interrupted Triple Helices (FACITs) (Yamauchi et al, 1986;Dublet et al, 1988;Karimbux et al, 1992). Type XII collagen is a homotrimer composed of otl(XII) chains.…”

Section: Introductionmentioning

confidence: 98%

Temporal and Spatial Expressions of Type XII Collagen in the Remodeling Periodontal Ligament during Experimental Tooth Movement

Karimbux

Nishimura

1995

J Dent Res

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This study tested the hypothesis that the remodeling processes of adult periodontal ligament (PDL) reiterate the cellular and molecular events that occur sequentially during development. Type XII collagen has been implicated in the three-dimensional organization of the PDL extracellular matrix, and its expression has been restricted to the terminally differentiated stages. This study focused on the examination of the temporal and spatial expression of type XII collagen during experimental PDL remodeling in the rat. The temporal expressions of types I and XII collagen mRNAs were examined by RNA transfer blot and RNase protection assays, respectively, and were found to be relatively stable in the control group throughout the experimental period. In the tooth movement group, the expression of type I collagen increased at 72 hours and sustained the high level of expression at one week, while an increase in the expression of type XII collagen was first noted at the one-week period. The temporal activation of types I and XII collagen expression in the remodeling occurred in a pattern similar to that found during the development of the PDL. The spatial expression of type XII collagen mRNA was examined by in situ hybridization in the one-week-tooth-movement specimens. Labeled cells, which were more evident in the tension side, typically exhibited a spindle shape and were surrounded by the mature PDL matrix. Our data suggest that the type XII collagen expression may be closely associated with the functional regeneration of the PDL.

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Section: Introductionmentioning

confidence: 98%

Temporal and Spatial Expressions of Type XII Collagen in the Remodeling Periodontal Ligament during Experimental Tooth Movement

Karimbux

Nishimura

1995

J Dent Res

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“…One isolated from periodontal ligament has nearly identical sequences to chick type XII, and has a very similar rotary-shadowed image (Dublet et al, 1988). Another was isolated from bovine skin and tendon that demonstrated less sequence homology, but again a similar rotary shadowed image .…”

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confidence: 98%

Identification and partial characterization of two type XII-like collagen molecules.

Lunstrum

Morris

McDonough

et al. 1991

The Journal of Cell Biology

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Abstract. We have identified two distinct collagenous macromolecules in extracts of fetal bovine skin. Each of the molecules appears to contain three identical u-chains with short triple-helical domains of ,',, 25 kD, and nontriple-helical domains of--190 kD. Consistent with these observations, extracted molecules contain a relatively short triple-helical domain (75 nm) and a large globular domain comprised of three similar arms. Despite these similarities, the purified collagenase-resistant domains are distinguished by a number of criteria. The globular domains can be chromatographically separated on the basis of charge distribution. Peptide profiles generated by V8 protease digestion are dissimilar. These molecules are immunologically unique and have distinct distributions in tissue. Finally, rotary shadow analysis of purified domains identifies size and conformation differences. Structurally, the molecules are very similar to type XII collagen, but differ in tissue distribution, since both these molecules are present in cartilage, while type XII is reported to be absent from that tissue.

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“…The PDL contains many different types of collagen including types I, III, V, VI, XII, and XIV [Bornstein and Sage, 1980; Dublet et al, 1988; Zhang et al, 1993]. PLF can induce collagen molecules to respond to mechanical stimuli in the PDL [Wang et al, 2003], and this is an essential event in the process of alveolar bone remodeling induced by mechanical force [Bumann et al, 1997].…”

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confidence: 99%

Mechanical force induces type I collagen expression in human periodontal ligament fibroblasts through activation of ERK/JNK and AP‐1

Kook

Hwang

Park

et al. 2009

J of Cellular Biochemistry

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Type I collagen (COL I) is the predominant collagen in the extracellular matrix of periodontal ligament (PDL), and its expression in PDL fibroblasts (PLF) is sensitive to mechanical force. However, the mechanism by which PLF induces COL I to respond to mechanical force is unclear. This study examined the nature of human PLF in mediating COL I expression in response to centrifugal force. Signal transduction pathways in the early stages of mechanotransduction involved in the force-driven regulation of COL I expression were also investigated. Centrifugal force up-regulated COL I without cytotoxicity and activated extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38 kinase. ERK and JNK inhibitor blocked the expression of COL I but p38 kinase inhibitor had no effect. Centrifugal force activated activator protein-1 (AP-1) through dimerization between c-Fos and c-Jun transcription factors. ERK and JNK inhibitors also inhibited AP-1-DNA binding, c-Fos nuclear translocation, and c-Jun phosphorylation that were increased in the force-exposed PLF. Further, transfecting the cells with c-Jun antisense oligonucleotides almost completely abolished the force-induced increase of c-Jun phosphorylation and COL I induction. Our findings suggest that mechanical signals are transmitted into the nucleus by ERK/JNK signaling pathways and then stimulate COL I expression through AP-1 activation in force-exposed human PLF.

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Bovine type XII collagen: Amino acid sequence of a 10 kDa pepsin fragment from periodontal ligament reveals a high degree of homology with the chicken α₁(XII) sequence

Cited by 24 publications

References 11 publications

Temporal and Spatial Expressions of Type XII Collagen in the Remodeling Periodontal Ligament during Experimental Tooth Movement

Temporal and Spatial Expressions of Type XII Collagen in the Remodeling Periodontal Ligament during Experimental Tooth Movement

Identification and partial characterization of two type XII-like collagen molecules.

Mechanical force induces type I collagen expression in human periodontal ligament fibroblasts through activation of ERK/JNK and AP‐1

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Bovine type XII collagen: Amino acid sequence of a 10 kDa pepsin fragment from periodontal ligament reveals a high degree of homology with the chicken α1(XII) sequence

Cited by 24 publications

References 11 publications

Temporal and Spatial Expressions of Type XII Collagen in the Remodeling Periodontal Ligament during Experimental Tooth Movement

Temporal and Spatial Expressions of Type XII Collagen in the Remodeling Periodontal Ligament during Experimental Tooth Movement

Identification and partial characterization of two type XII-like collagen molecules.

Mechanical force induces type I collagen expression in human periodontal ligament fibroblasts through activation of ERK/JNK and AP‐1

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Bovine type XII collagen: Amino acid sequence of a 10 kDa pepsin fragment from periodontal ligament reveals a high degree of homology with the chicken α₁(XII) sequence