Localization of pro‐α2(V) collagen transcripts in the tissues of the developing mouse embryo

Ανδρικόπουλος, Κωνσταντίνος; Suzuki, Hiroaki; Solursh, Michael; Ramirez, Francesco

doi:10.1002/aja.1001950205

Cited by 41 publications

(26 citation statements)

References 23 publications

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“…Additional levels of regulation may include the amounts and identities of the HOX partners and, consequently, the ability of the resulting PBX-HOX dimers to compete more or less effectively with PBX-PREP1 complexes for FPB binding. The combinatorial alternatives of the FPB complex are compatible with the available data on HOX, TALE, and COL5A2 gene expression during mouse embryogenesis (47)(48)(49)(50). COL5A2 transcripts are first detectable, widely and diffusely distributed in the intestinal and craniofacial mesenchyme of the 12.5-day embryo (50).…”

Section: Discussionsupporting

confidence: 55%

Cooperative Interactions between PBX, PREP, and HOX Proteins Modulate the Activity of the α2(V) Collagen (COL5A2) Promoter

Penkov¹,

Tanaka²,

Rocco³

et al. 2000

Journal of Biological Chemistry

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Cell type-specific expression of the human ␣2(V) collagen (COL5A2) gene depends on a cis-acting element that consists of two contiguous protein binding sites (FPA and FPB) located between nucleotides ؊149 and ؊95, relative to the transcription start site. The present study focused on the characterization of the FPB-bound complex. DNA binding assays and cell transfection experiments revealed that the bipartite core sequence of FPB (5-ATCAATCA-3) binds the PBX1/2, PREP1, and HOXB1 proteins, and this in turn leads to promoter transactivation. In the presence of all three nuclear factors, cooperative interactions between recombinant PBX1 and PREP1 or PBX1 and HOXB1 result in binding of the heterodimers to FPB in vitro. Similarly, overexpression of different combinations of PBX1, PREP1, and HOXB1 transactivates FPB-driven transcription. In contrast to the composition of the FPB complex purified from COL5A2-positive cells, the FPB complex from COL5A2-negative cells contains PBX2 and PREP1 but lacks PBX1. However, PBX1 exogenously introduced into COL5A2-negative cells cannot stimulate FPBdriven transcription unless co-expressed with PREP1. Within the intrinsic limitations of the experimental model, our results indicate that combinatorial interactions among PBX and PREP or HOX proteins are involved in regulating tissue-specific production of collagen V.Proper assembly of collagenous networks in the developing connective tissue is critically important for the formation and function of virtually every organ system (1). Collagens I and II are the major fibrillar structures that confer strength and resilience to noncartilaginous and cartilaginous tissues, respectively (1). Aside from spatiotemporal regulation of the respective genes, formation of collagens I and II fibers is under the control of a variety of cellular and structural elements (2). Among the latter are the so-called minor fibrillar collagens (types V and XI), which regulate fibrillogenesis by co-polymerizing with the major fibrillar collagens (types I and II) (3, 4).Understanding the mechanisms that underlie the production of minor fibrillar collagens is therefore relevant to elucidating the genetic determinants responsible for stage-and tissue-specific diversification of the extracellular matrix.Our previous work has shown that transcription of the human ␣2(V) collagen (COL5A2) gene is controlled by an evolutionarily conserved sequence located between nucleotides Ϫ149 and Ϫ95 (5). DNase I footprinting and the electrophoretic mobility shift assay (EMSA) 1 have divided this upstream promoter sequence into two contiguous cis-acting elements, termed FPB (Ϫ149 to Ϫ115) and FPA (Ϫ114 to Ϫ95). Deletion of the Ϫ149 to Ϫ95 region as well as nucleotide substitutions in FPB and FPA were shown to adversely affect COL5A2 promoter activity in cell transfection experiments. Moreover, the core sequence of FPB was subsequently noted to exhibit some homology with FP7, a cis-acting element of the ␣1(XI) collagen (COL11A1) promoter (6). Indeed, the EMSA documented the ability of...

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Section: Discussionsupporting

confidence: 55%

Cooperative Interactions between PBX, PREP, and HOX Proteins Modulate the Activity of the α2(V) Collagen (COL5A2) Promoter

Penkov¹,

Tanaka²,

Rocco³

et al. 2000

Journal of Biological Chemistry

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“…The study revealed that some of the al(X1)-positive tissues of the chick coincide with the sites known to produce al(I1) collagen in the mouse (Cheah et al, 1991). Moreover, al(X1) transcripts were found to accumulate in organs of the chick, which in the mouse have been shown to contain a2(V) collagen-producing sites (Andrikopoulos et al, 1992). The informative value of these correlations is unfortunately limited by two major differences in the experimental designs of the (rl(X1) compared to the ul(I1) and a2(V) studies.…”

Section: Introductionmentioning

confidence: 99%

“…The hybridization procedures used in this study were essentially the same as those described elsewhere (Hayashi et al, 1986;Iyama et al, 1991). In situ probes included mouse ul(X1) , al(I1) (Andrikopoulos et al, 1992), and al (1) collagen (Yoshioka, unpublished data); their sizes are 1,810, 618, and 250 bp, respectively. The cDNAs were labeled with 35S-thymidine 5'-[a-thiol triphosphates (TTP) (Dupont, Boston, MA) by nick-translation to a specific activity of 1.8-4.5 x 10' cpmlbg DNA.…”

Section: In Situ Hybridizationsmentioning

confidence: 99%

“…Poly (A)' RNA was purified by oligotex 30 (Japan Synthetic Rubber Co., Tokyo, Japan) and subjected to Northern analysis as previously described (Yoshioka and Ramirez, 1990;. The Northern analysis employed cDNAs coding for mouse a l ( X I ) , al(V), and a2(V) collagen [clones mHYl , mHY8 (Yoshioka, unpublished data), and KA311 (Andrikopoulos et al, 1992)l and for human a2(XI) collagen [clone HY9 (Yoshioka, unpublished data)]. RT-PCR amplifications were performed for 35 cycles with 2.5 U of Taq DNA polymerase at 94°C for 1 min, 60°C for 2 min, 72°C for 3 min, followed by finalextension at 72°C for 7 rnin (Wang et al, 1989).…”

Section: Experimental Procedures Rna Analysismentioning

confidence: 99%

“…The informative value of these correlations is unfortunately limited by two major differences in the experimental designs of the (rl(X1) compared to the ul(I1) and a2(V) studies. First, embryonic expression of c1 l(X1) collagen was examined in the chick and not in the mouse, the organism where the patterns of the ul(I1) and a2(V) collagen genes have been described in the greatest details (Nah et al, 1992;Cheah et al, 1991;Andrikopoulos et al, 1992). Second, the al(X1) analysis could not determine the precise sites of gene expression within each of the positive organs because it relied mostly on Northern rather than in situ hybridization data (Nah et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

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Developmental pattern of expression of the mouse α1(XI) collagen gene (Col11a1)

Yoshioka

Iyama

Inoguchi

et al. 1995

Developmental Dynamics

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Fibrillar networks are intimately involved in several morphogenetic processes which underlie the harmonious development of the vertebrate embryo. Recent genetic evidence has demonstrated that the minor types V and XI collagen are key regulators of types I and XI fibrillogenesis in non-cartilaginous and cartilaginous matrices, respectively. A comprehensive understanding of the expression and regulation of the genes coding for the chains of the minor collagen types is therefore relevant to animal morphogenesis and development. The present study was undertaken to elucidate the embryonic pattern of expression of the gene coding for the mouse a1 chain of type XI colagen ( C o l l l a l ) using the technique of in situ hybridization. Transcripts of the C o l l l a l gene were detected as early as 11 days of gestation. The oll(X1) transcripts were found to accumulate mostly in cartilaginous tissues, such as the chondrocranium and the developing limbs. Like the major cartilage-specific collagen (type XI), Colllal expression was also noted in the neuro-epithelium of the brain. However, al(X1) transcripts accumulated in several other non-cartilaginous sites. They include odontoblasts, trabecular bones, atrioventricular valve of the heart, the tongue, the intestine, and the otic vesicle. Altogether, the data confirm that C o l l l a l has a broader spectrum of expression than previously thought. This finding raises the possibility that the (ul(X1) chain may participate in the formation of stage-and tissue-specific trimers with distinct functional properties.

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Distribution of minor collagens during skin development

Garrone

Lethias

Guellec

1997

Microsc. Res. Tech.

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The skin is a tissue containing a large number of collagen types. Several collagens are restricted at the dermo‐epidermal junction, contrarily to others present throughout the dermis. However, the distribution of the dermal collagen varies during embryonic development. In this contribution, we have been interested in the collagen types associated with the major collagenous components of the dermis, which are the collagen types I and III. Type V collagen, which is mixed with collagen types I and III to form heterotypic fibrils, has been studied during mouse embryo development. Transcripts of the α1(V) gene have been localized by in situ hybridization, on flattened cells of the stratum germinativum first, and then only on dermal cells. The expression of the gene decreases at birth, while the expression of the α1(I) gene remains constant, with, however, a ring of high intensity around hair follicles. Other collagen types (VI, and the fibril‐associated collagens XII and XIV) have been studied during calf embryonic development by immunofluorescence and ultrastructural immunogold detection. Type VI collagen appears homogeneously distributed throughout the dermis. Type XII collagen is first widely distributed and becomes restricted in the upper, papillary dermis after 6 months of gestation. Type XIV collagen, on the contrary, is first located as a delicate framework around hair follicles (at 19 weeks of gestation), and progressively invades the whole dermis where it appears abundant just before birth. The different functions of all these collagens are discussed in terms of dermis architecture, mechanical properties and physiology. Microsc. Res. Tech. 38:407–412, 1997. © 1997 Wiley‐Liss, Inc.

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Localization of pro‐α2(V) collagen transcripts in the tissues of the developing mouse embryo

Cited by 41 publications

References 23 publications

Cooperative Interactions between PBX, PREP, and HOX Proteins Modulate the Activity of the α2(V) Collagen (COL5A2) Promoter

Cooperative Interactions between PBX, PREP, and HOX Proteins Modulate the Activity of the α2(V) Collagen (COL5A2) Promoter

Developmental pattern of expression of the mouse α1(XI) collagen gene (Col11a1)

Distribution of minor collagens during skin development

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