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M van der Rest

Publications and source records attributed to M van der Rest.

At least 55 records · Page 3Linked to original sources
PubMed1992

Tissue-specific expression of type XIV collagen--a member of the FACIT class of collagens.

The collagens represent a highly diverse superfamily of extracellular matrix proteins that can be divided into several distinct families. One of the families, called FACIT (fibril-associated collagens with interrupted triple-helices) family, contains molecules that appear to be associated with cross-striated fibrils composed of members of the fibrillar collagen family. We have determined a portion of the primary structure of a recently discovered member of the FACIT family, chicken alpha 1(XIV) collagen, based on cloning and sequencing cDNAs. A synthetic oligopeptide from within the carboxy-terminal non-triple-helical domain of the alpha 1(XIV) chain has been used for generating specific polyclonal antibodies. The antiserum, PS1, recognizes a 220 kDa polypeptide in immunoblots of extracts of chicken skin, tendons, and cartilage. Sequencing of a tryptic peptide generated from purified, immunoreactive material, gives a sequence identical to that derived from cDNA sequencing, providing strong support for the type XIV-specificity of PS1. We have examined the expression of type XIV collagen in developing chick embryos by immunostaining of sections from 12-day-old embryos with PS1 and by Northern blot analysis of RNA from several tissues from both 12- and 17-day-old embryos. The results show that type XIV collagen is prevalent within relatively dense connective tissues such as dermis, tendons, perichondrium, perimysium, the stroma of lungs and liver, and blood vessels.

Amino Acid Sequence↗
PubMed1991

Type XIV collagen, a new homotrimeric molecule extracted from fetal bovine skin and tendon, with a triple helical disulfide-bonded domain homologous to type IX and type XII collagens.

Previously undescribed disulfide-bonded collagenous pepsin-derived fragments have been isolated from fetal calf tendon and skin. One fragment, 10.5 kDa after reduction, was shown to be similar but distinct to the COL1 domain of the recently characterized type XII collagen (64% primary structure identity). The similarity includes important features such as size, location of the cysteine residues, and nature and position of an imperfection of the triple helix. From fetal calf skin, two approximately 34-kDa disulfide-bonded trimeric fragments were isolated in the unreduced form. Amino acid sequencing showed that one fragment contained solely the COL1 domain of type XII collagen while the other one only contained the COL1 domain of the new chain. Like type XII collagen, the new chain is therefore part of a homotrimeric molecule and should thus be considered as a distinct collagen type. We propose to call the molecule from which this fragment is derived, type XIV collagen, with a chain composition (alpha 1 (XIV]3. The presence of a domain similar to the COL1 domain of collagens types IX and XII suggests that type XIV collagen belongs to the group of fibril-associated collagens with interrupted triple helices (FACIT). Two other fragments, 13.5 and 17 kDa after reduction, were also purified. They were shown to contain the same triple helical domain with different pepsin cleavage sites at the amino terminus. Several tryptic peptides were sequenced, and the derived sequences could be aligned with the COL2 domain of type XII collagen or with flanking sequences in the NC2 and NC3 domains (61% sequence identity). These fragments are very likely to be also derived from type XIV collagen.

Amino Acid Sequence↗
PubMed1991

Proteoglycan and collagen synthesis are correlated with actin organization in dedifferentiating chondrocytes.

The dedifferentiation of chondrocytes in culture is classically associated with a transition from a rounded to a spread morphology. However, the loss of chondroitin sulfate proteoglycan (CSPG) and type II collagen gene expression (markers of the differentiated chondrocyte) does not occur for all polygonal or fibroblast-like cells at the same stage of culture. Furthermore, it has been demonstrated that retinoic acid-dedifferentiated chondrocytes can reexpress type II collagen if treated by the microfilament disruptive drug dihydrocytochalasin B, without a return to the spherical shape. In the present study, we have investigated by fluorescent double-staining whether the synthesis of both CSPG and type II collagen by dedifferentiating chick chondrocytes in low density cultures is dependent on a type of actin organization. We report that the synthesis of CSPG and type II collagen synthesis is coincident with the presence of a faint microfibrillar actin architecture but is absent in chondrocytes showing well defined actin cables. This correlation was observed independently of the shapes exhibited by the cells. Moreover, type I collagen (marker of the dedifferentiated chondrocyte) is synthesized mainly in cells showing large actin cables. This study, performed in the absence of drugs, suggests that actin organization, rather than changes in cell shape, is involved in modulating the chondrogenic phenotype in vitro.

Actins↗
PubMed1991

Collagen family of proteins.

Collagen molecules are structural macro-molecules of the extracellular matrix that include in their structure one or several domains that have a characteristic triple helical conformation. They have been classified by types that define distinct sets of polypeptide chains that can form homo- and heterotrimeric assemblies. All the collagen molecules participate in supramolecular aggregates that are stabilized in part by interactions between triple helical domains. Fourteen collagen types have been defined so far. They form a wide range of structures. Most notable are 1) fibrils that are found in most connective tissues and are made by alloys of fibrillar collagens (types I, II, III, V, and XI) and 2) sheets constituting basement membranes (type IV collagen), Descemet's membrane (type VIII collagen), worm cuticle, and organic exoskeleton of sponges. Other collagens, present in smaller quantities in tissues, play the role of connecting elements between these major structures and other tissue components. The fibril-associated collagens with interrupted triple helices (FACITs) (types IX, XII, and XIV) appear to connect fibrils to other matrix elements. Type VII collagen assemble into anchoring fibrils that bind epithelial basement membranes and entrap collagen fibrils from the underlying stroma to glue the two structures together. Type VI collagen forms thin-beaded filaments that may interact with fibrils and cells.

Amino Acid Sequence↗
PubMed1990

Fibril-associated collagens.

Many collagen fibrils have been shown to be heterotypic, i.e. composed of more than one collagen type. Fibrils containing type I collagen as the major constituent do also contain, at least in some tissues, type III and type V collagens. Fibrils containing type II collagen have been shown to also contain type XI collagen. The type I, II, III, V and XI collagen molecules are very similar and are clearly derived from a single ancestral gene. However their processings are not identical. While collagen types I and II have a N-propeptide which is cleaved for their insertion in the fibrils, collagen types V and XI keep a N-terminal extension which must include, based on the cDNA derived structures, a short triple helix and a globular domain. They are thought to contribute to the control of fibril lateral growth and diameter. Other collagens are associated with fibrils without having the long triple uninterrupted triple helix characteristic of collagen types I, II, III, V and XI. Type IX collagen has been shown to be covalently cross-linked to type II collagen and to lay at or near the surface of fibrils, with a triple helical arm projecting in the extrafibrillar space a globular N-terminal domain. Type XII collagen is found in type I collagen containing matrices and contains a triple helical domain homologous to the type IX COL1 domain. This suggests a similar function.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1989

Type XII collagen. A large multidomain molecule with partial homology to type IX collagen.

Three overlapping cDNAs encoding alpha 1 (XII) collagen have been isolated and sequenced. The DNAs define five sequence domains within the chain. Three domains are nontriple-helical; two are relatively short triple-helical regions. The amino acid sequences of tryptic peptides derived from 16- and 10-kDa pepsin-resistant fragments isolated from tendon extracts are in full agreement with the deduced sequences of the triple-helical regions. Two of the five sequence domains in alpha 1 (XII), one triple-helical and one nontriple-helical, show a high degree of similarity to regions in type IX collagen chains. In addition, examination of seven exons in the alpha 1 (XII) gene shows that the gene is, in part, similar to the structure of type IX collagen genes. Therefore, collagen types IX and XII are partially homologous. The alpha 1 (XII) sequence data predict an asymmetric structure for type XII collagen molecules, fully consistent with the rotary shadowing images. These images show a triple-helical 75-nm tail attached through a central globule to three finger-like structures, each 60 nm long (Dublet, B., Oh, S., Sugrue, S. P., Gordon, M. K., Gerecke, D. R., Olsen, B. R., and van der Rest, M. (1989) J. Biol. Chem. 264, 13150-13156).

Amino Acid Sequence↗
PubMed1989

The cloning and sequencing of alpha 1(VIII) collagen cDNAs demonstrate that type VIII collagen is a short chain collagen and contains triple-helical and carboxyl-terminal non-triple-helical domains similar to those of type X collagen.

We have isolated two overlapping cDNA clones covering 2425 base pairs encoding a short type VIII collagen chain synthesized by rabbit corneal endothelial cells. The cDNAs encode an open reading frame of 744 amino acid residues containing a triple-helical domain of 454 residues flanked by 117- and 173-residue amino and carboxyl non-triple-helical domains (called NC2 and NC1, respectively). Based on the identity between the DNA-derived amino acid sequence and the amino acid sequence of a type VIII collagen CNBr peptide obtained from rabbit corneal Descemet's membrane, we conclude that the cDNAs code for a type VIII collagen chain. We give this chain the designation alpha 1(VIII). The alpha 1(VIII) triple-helical domain contains eight imperfections in the Gly-X-Y repeated structure with Gly-X instead of a full triplet. The length of the triple-helical domain and number and relative locations of these imperfections are remarkably similar to those of chicken alpha 1(X) collagen. The amino acid sequence of the carboxyl three-quarters of the NC1 domain has high sequence similarity to that of alpha 1(X) collagen. These data suggest that the triple-helix coding portions and carboxyl three-quarters of the NC1 domains of the alpha 1(VIII) and alpha 1(X) genes have a common evolutionary origin.

Amino Acid Sequence↗
PubMed1989

The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization.

We have isolated three overlapping cDNA clones encoding the pro alpha 2(XI) collagen chain from a human chondrocyte cDNA library. Together, the cDNAs code for 257 uninterrupted Gly-X-Y triplets (almost 80% of the triple helical domain) and about 200 amino acid residues of the carboxyl telopeptide and carboxyl propeptide. The identification of the clones as pro alpha 2(XI) cDNAs was based on the complete identity between the amino acid sequences of three tryptic peptides derived from human alpha 2(XI) collagen and the cDNA-derived sequence. We have also sequenced six exons within a human genomic alpha 2(XI) cosmid clone. This sequence shows that although type XI collagen belongs to the fibril-forming class of collagens, there are substantial differences in exon sizes at the 3' end of the gene when comparing the alpha 2(XI) gene with those of human types I, II, and III collagens. Finally, pro alpha 2(XI) cDNA has been used as a probe to determine the location of the gene by in situ hybridization of chromosome spreads. The results demonstrate that the gene is located close to the region p212 on chromosome 6. Northern blot analysis shows that the gene is expressed in cartilage but not in adult liver, skin, and tendon.

Amino Acid Sequence↗
PubMed1989

The structure of avian type XII collagen. Alpha 1 (XII) chains contain 190-kDa non-triple helical amino-terminal domains and form homotrimeric molecules.

The monoclonal antibody 75d7, specific for type XII collagen (Sugrue, S.P., Gordon, M.K., Seyer, J., Dublet, B., van der Rest, M., and Olsen, B. R. (1989) J. Cell Biol., in press), was used to characterize the intact form of type XII collagen from chick embryo leg tendons. On an immunoblot of a 6% polyacrylamide gel of tendon extracts, one sharp band is recognized by the antibody at Mr = 220,000, while two fuzzy and poorly resolved bands are seen at Mr = 270,000 and Mr = 290,000. By immunoprecipitation of radiolabeled tendon culture media and electrophoresis of the precipitated material, bands with the same mobilities are observed, indicating that type XII collagen is not proteolytically processed in the extracellular space. Type XII collagen was extracted from tendons with 1 M NaCl in a Tris-HCl buffer and partially purified by concanavalin A-Sepharose and gel permeation chromatographies, using dot immunoblots to monitor the purification. Fractions highly enriched in bacterial collagenase-sensitive proteins with the same electrophoretic properties as type XII collagen were obtained. These fractions did not stain with Alcian blue and neither they nor the immunostained type XII collagen were affected by chondroitinase ABC digestion, indicating that type XII collagen is not a proteoglycan. A disulfide-bonded trimeric CNBr peptide was isolated by affinity chromatography on an antibody column and further purified by gel electrophoresis. Its NH2-terminal amino acid sequence was shown to be unique, demonstrating that type XII collagen is a homotrimer [alpha 1 (XII)]3. After bacterial collagenase digestion, both the immunopurified radiolabeled preparation and the purified tendon extract fraction showed by gel electrophoresis the presence of a large disulfide-bonded, 3 x 190-kDa, collagenase-resistant domain. Rotary shadowing and electron microscopy of the purified type XII fraction demonstrated that the molecule has the structure of a cross consisting of a 75 nm collagenase-sensitive tail, a central globule, and three 60 nm arms each ending in a small globule. After heat denaturation and renaturation, only a very large globule can be seen, attached to the triple helical tail. These results show that type XII collagen has a unique structure and is different from the other matrix constituents described so far.

Amino Acid Sequence↗
PubMed1989

Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides.

Procollagen N-proteinase (EC 3.4.24.14), the enzyme that cleaves the NH2-terminal propeptides from type I procollagen, was purified over 20,000-fold with a yield of 12% from extracts of 17-day-old chick embryo tendons. The procedure involved precipitation with ammonium sulfate, adsorption on concanavalin A-Sepharose, and five additional column chromatographic steps. The purified enzyme was a neutral, Ca2+-dependent proteinase (5-10 mM) that was inhibited by metal chelators. It had a molecular mass of 500 kDa as determined by gel filtration. The enzyme contained unreduced polypeptides of 61, 120, 135, and 161 kDa that were separated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The 135- and 161-kDa polypeptides were catalytically active after elution from the polyacrylamide gel. Other properties of 500-kDa enzyme are: 1) the Km for type I procollagen is 54 nM at pH 7.5 and 35 degrees C, and the kappa cat is 350 h-1; 2) the activation energy for reaction with type I procollagen is 7,100 cal mol-1; 3) the isoelectric point is 3.6; and 4) the enzyme specifically cleaves the NH2-terminal propeptides of type I and II procollagen, but not of type III procollagen. A minor form of N-proteinase with a 300-kDa mass was also purified and was found to contain a 90-kDa polypeptide as the major active polypeptide. The enzyme appeared to be a degraded form of the 500-kDa N-proteinase. The properties of the 300-kDa enzyme were similar to those observed for the 500-kDa enzyme.

Ammonium Sulfate↗
PubMed1989

Immunoidentification of type XII collagen in embryonic tissues.

We have generated a monoclonal antibody against a synthetic peptide whose sequence was derived from the nucleotide sequence of a cDNA encoding alpha 1(XII) collagen. The antibody, 75d7, has been used to identify the alpha 1(XII) chain on immunoblots of SDS-PAGE tendon extracts as a 220-kD polypeptide, under reducing conditions. Amino-terminal amino acid sequence analysis of an immunopurified cyanogen bromide fragment of type XII collagen from embryonic chick tendons gave a single sequence identical to that predicted from the cDNA, thus confirming that the antibody recognizes the type XII protein. Immunofluorescence studies with the antibody demonstrate that type XII collagen is localized in type I-containing dense connective tissue structures such as tendons, ligaments, perichondrium, and periosteum. With these data, taken together with previous results showing that a portion of the sequence domains of type XII collagen is similar to domains of type IX, a nonfibrillar collagen associated with cross-striated fibrils in cartilage, we suggest that types IX and XII collagens are members of a distinct class of extracellular matrix proteins found in association with quarter-staggered collagen fibrils.

Animals↗
PubMed1989

Absence of collagen deficiency in familial cerebral aneurysms.

It has been suggested that a deficiency in the expression of type III collagen may play a role in the pathogenesis of cerebral aneurysms. To test this hypothesis in cases of familial cerebral aneurysms, fibroblast cell cultures were established and the expression of collagen types I and III was studied in a patient with three cerebral aneurysms whose mother and sister also had cerebral aneurysms. Cultured skin fibroblasts were labeled with tritiated proline. The collagens and procollagens were precipitated and run on sodium dodecyl sulfate-polyacrylamide gel electrophoresis after reduction to analyze procollagen chains. Control cell lines were analyzed simultaneously. Quantitation of the ratios of type III to type I procollagen synthesis was achieved by integration of the intensities of the pro-alpha 1(III), pro-alpha 1(I), and pro-alpha 2(I) bands on fluorograms of electrophoretic gels of medium proteins. There was no difference in type I and III procollagen levels observed between the cells from the aneurysm patient and those from the control cell lines. These data do not support the hypothesis that familial cerebral aneurysms are caused by a deficiency of type III collagen.

Collagen↗
PubMed1988

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 alpha 1(XII) sequence.

A 10 kDa collagenous peptide, derived from a 30 kDa disulfide bonded fragment, was purified from bovine periodontal ligament. Amino acid sequence analysis of tryptic peptides demonstrated a 92.8% homology with the chicken alpha 1(XII) cDNA derived sequence, demonstrating for the first time the presence of type XII collagen in a mammalian species and in an adult tissue.

Amino Acid Sequence↗