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Results for “Collagen Type V”

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At least 19 recordsLinked to original sources

PubMed1993

Inhibition of cell adhesion by proteolytic fragments of type V collagen.

Type V collagen inhibits the cell-substratum adhesion of many types of cells. In this study, inhibitory effects of type V collagen on the adhesion of mouse melanoma B16-F10 cells to fibronectin, laminin and vitronectin were investigated. When the culture dishes were coated with a mixture of fibronectin and type V collagen, adhesion of the cells was inhibited by 50% at a fibronectin/collagen molar ratio of 10/1. At a similar molar ratio, adhesion of the cells to laminin was inhibited moderately, but that to vitronectin was not significantly affected. Type V collagen added into culture medium was less effective in inhibiting cell adhesion. The antiadhesive activity of type V collagen was partially retained in the alpha 1 (V) chain of heat-denatured collagen. The alpha 1 (V) chain was split into two large fragments, 90 kDa and 60 kDa, by limited digestion with Staphylococcus aureus V8 proteinase. The 90-kDa fragment, which was derived from the C-terminal half of the alpha 1 (V) chain, inhibited the cell adhesion more profoundly than alpha 1 (V). However, little fibronectin bound to the 90-kDa fragment, while fibronectin bound to the 60-kDa fragment, which was less antiadhesive than the 90-kDa fragment, with the same extent as alpha 1 (V). We therefore concluded that the antiadhesive effect of type V collagen was not due to its specific binding to the fibronectin molecule.

Amino Acid Sequence↗

PubMed1986

In vitro formation of hybrid fibrils of type V collagen and type I collagen. Limited growth of type I collagen into thick fibrils by type V collagen.

Type V collagen and type I collagen were obtained from human placentas by pepsin treatment, followed by salt fractionation. The precipitates formed at 37 degrees C from a mixed solution of type V collagen and type I collagen, reacted with antibodies to either type V collagen or type I collagen. The precipitates seen by electron microscopy were fine flexible fibrils, with a D-periodic banding pattern. The average diameter of hybrid fibrils was smaller than 50 nm, when the proportion of type V collagen exceeded that of type I collagen. Type V collagen directly interacts with type I collagen in forming hybrid fibrils, resulting in limitation of the growth of type I collagen fibrils into thicker fibrils. We propose that the fibrils with a predominant type V collagen content may occur in the pericellular environment of various tissues, as a basic structure in connecting basal laminae with interstitial collagen fibrils.

Chemical Precipitation↗

PubMed1985

Glycoproteins on the surface of smooth muscle cells involved in their interaction with type V collagen.

Type V collagen is a major component of the pericellular coat of smooth cells (SMC). The purpose of the present study was to assess biochemically the nature of an in vitro interaction between bovine aortic SMC and type V collagen from the same source. This interaction was originally shown to be mediated by a cell-surface glycoconjugate. Data obtained in the present study suggests that the binding system consists of integral membrane glycoproteins which act alone or in combination with a surface glycolipid in type V attachment. The nature of this system was indicated by the finding of 80 000 and 50 000 components in the plasma membrane fractions which were specifically retained by type V collagen--Sepharose columns and incorporated both methionine and mannose label. Moreover, inhibition of protein synthesis lowered SMC attachment by 25%. The mannose label associated with these components was probably in the form of a simple oligosaccharide at the attachment site since it bound to concanavalin A (ConA) and was sensitive to endoglycosidase H. Iodinated ConA labelling indicated elevated levels of these components were associated with SMC--type V collagen interaction. The attachment region on the type V molecule was localized within the cyanogen bromide peptide 6 of the alpha 2 (V) chain.

Animals↗

PubMed1985

In vitro formation of fine fibrils with a D-periodic banding pattern from type V collagen.

Type V collagen was isolated from human placenta by limited pepsin treatment and purified by salt fractionation. A solution of type V collagen was dialyzed at 4 degrees C against phosphate-buffered saline or against 0.02 M Na2HPO4. Aggregates formed under these in vitro conditions from a pure type V collagen solution were examined by electron microscopy. The aggregates were fine flexible fibrils. The fibrils formed during incubation at 25 degrees C were of relatively uniform diameter, 34.8 +/- 9.1 nm and did not show an axial banding pattern. When the specimen was incubated at 37 degrees C, the fibrils were of slightly larger diameter, 38.2 +/- 9.1 nm and almost all the fibrils had the axial repeat pattern of 67 nm. The ability of type V collagen to form banding fibrils is discussed in relation in the localization of the collagen in tissues.

Basement Membrane↗

PubMed1990

Adhesion, growth and cytoskeletal characteristics of 8701-BC breast carcinoma cells cultured in the presence of type V collagen.

Type V collagen is one of the minor components of the extracellular matrix (ECM) whose content is increased in cases of ductal infiltrating carcinomas of the breast. In order to clarify its biological role, we have investigated the effect of this molecule, both as substrate and as soluble factor, on the behaviour of a breast carcinoma cell line (8701-BC) grown in vitro. Cell-collagen adhesion was monitored for 24 h from plating in the absence or presence of serum. The influence of type V collagen on cell growth was followed during 9 days of culture, and the actin-vinculin arrangement was studied by simultaneous fluorescent immuno-staining. The results indicate that type V collagen is not a permissive substrate for neoplastic cell proliferation and dissemination in vitro.

Breast Neoplasms↗

PubMed1987

Comparison of axial banding patterns in fibrils of type V collagen and type I collagen.

Type V collagen and type I collagen were obtained from human placenta, essentially by salt fractionation. Precipitates were formed from mixed solutions of type V collagen and type I collagen in various ratios. They were incubated at 37 degrees C for 1 hour and negatively stained with 0.5% uranyl acetate (pH 4.4) at 37 degrees C. The specimens, seen by electron microscopy, were fibrils with a D-periodic banding pattern. Axial electron density profiles of collagen fibrils were obtained from selected electron micrographs by densitometric tracing. The slit width corresponded to 1.5 nm. The relative electron densities of overlap region vs. hole region were lower than 20% in fine fibrils containing a significant amount of type V collagen. It is suggested that the overlap region of such collagen fibrils may be loosely packed, being accessible to uranyl acetate, or the hole region may be filled by larger non-collagenous portions of type V collagen, resulting in loss of the light and dark alternation. Six to 8 white transverse lines were discerned per period and labeled consecutively with Arabic numerals. White lines 2 and 5 tended to merge with lines 1 and 4, respectively, in collagen fibrils formed from a solution containing a significant amount of type I collagen or pure type I collagen. The eight white lines corresponded to c2, c1, b2, b1, a4, a1, e1 and d with reference to their locations in the D-period. The locations of white lines in collagen fibrils which contain significant amount of type V collagen were identical with those in type I collagen fibrils. This is consistent with the primary structure that the axial distribution of charged amino acids in type V collagen is quite similar to that in type I collagen.

Collagen↗

PubMed2000

Schwann cells synthesize type V collagen that contains a novel alpha 4 chain. Molecular cloning, biochemical characterization, and high affinity heparin binding of alpha 4(V) collagen.

Previously, we reported the isolation of a heparan sulfate-binding collagenous protein, p200, that is expressed by Schwann cells in developing peripheral nerves ((1996) J. Biol. Chem. 271, 13844-13853; (1999) J. Neurosci. Res. 56, 284-294). Here, we report the cloning of p200 cDNA from a Schwann cell cDNA library. The deduced amino acid sequence identifies p200 as a novel member of the collagen type V gene family. This polypeptide, which we have named alpha4 type V (alpha4(V)) collagen, contains an uninterrupted Gly-X-X collagen domain of 1011 amino acids that shows 82% sequence identity to human alpha3(V) collagen and 71% identity to rat alpha1(V) collagen. alpha4(V) is secreted by Schwann cells as a collagen heterotrimer that also contains alpha1(V) chains. alpha4(V)-containing collagen molecules synthesized by Schwann cells retain their amino-terminal non-collagenous domains. alpha4(V) mRNA was detected by reverse transcriptase-linked polymerase chain reaction amplification in neonatal and adult brain and neonatal peripheral nerve. alpha4(V) mRNA and protein were not detected in most other tissues, including the placenta and heart, which are known to contain alpha3(V). This pattern of alpha4(V) expression contrasted with that of alpha1(V) mRNA and protein, which were ubiquitously expressed. The isolated alpha4(V) chain demonstrated an unusually high affinity for heparin. The restricted expression and unusual properties of alpha4(V)-containing collagen type V molecules suggest a unique and important role for these molecules in peripheral nerve development.

Amino Acid Sequence↗

PubMed2001

Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assembly.

Type V collagen is a quantitatively minor fibrillar collagen with a broad tissue distribution. The most common type V collagen isoform is alpha1(V)(2) alpha2(V) found in cornea. However, other isoforms exist, including an [alpha1(V)alpha2(V)alpha3(V)] form, an alpha1(V)(3) homotrimer and hybrid type V/XI forms. The functional role and fibrillar organization of these isoforms is not understood. In the cornea, type V collagen has a key role in the regulation of initial fibril assembly. Type I and type V collagen co-assemble into heterotypic fibrils. The entire triple-helical domain of the type V collagen molecules is buried within the fibril and type I collagen molecules are present along the fibril surface. The retained NH(2)-terminal domains of the type V collagen are exposed at the surface, extending outward through the gap zones. The molecular model of the NH(2)-terminal domain indicates that the short alpha helical region is a flexible hinge-like region allowing the peptide to project away from the major axis of the molecule; the short triple-helical regions serve as an extension through the hole zone, placing the tyrosine-rich domain at the surface. The assembly of early, immature fibril intermediates (segments) is regulated by the NH(2)-terminal domain of type V collagen. These NH(2)-terminal domains alter accretion of collagen molecules onto fibrils and therefore lateral growth. A critical density would favor the initiation of new fibrils rather than the continued growth of existing fibrils. Other type V collagen isoforms are likely to have an important role in non-cornea tissues. This role may be mediated by supramolecular aggregates different from those in the corneal stroma or by an alteration of the interactions mediated by tissue-specific type V collagen domains generated by different isoforms or aggregate structures. Presumably, the aggregate structure or specific domains are involved in the regionalization of fibril-associated macromolecules necessary for the tissue-specific regulation of later fibril growth and matrix assembly stages.

Collagen↗

PubMed1984

Localization of type V collagen and type IV collagen in human cornea, lung, and skin. Immunohistochemical evidence by anti-collagen antibodies characterized by immunoelectroblotting.

Tissue distribution of Type V collagen in comparison with Type IV collagen was investigated by indirect immunofluorescence microscopy. Affinity-purified rat antibodies to Type IV and Type V collagens obtained from human placenta reacted specifically only with the corresponding type of collagen in both native and denatured conformations. In indirect immunofluorescent stainings of human skin, lung, and cornea tissues, Type IV and Type V collagens showed distinct distributions. Type IV collagen was distributed exclusively in basement membrane. However, Type V collagen had two characteristic features; a diffuse distribution in interstitium and the locations on or adjacent to basement membrane. On the basis of these findings and of biochemical characterization of the collagens, it is postulated that Type V collagen is an intermediate collagen, possibly having a function of binding or connecting of interstitial collagen fibrils with membranous collagen networks.

Adult↗

PubMed1994

A 92 kDa gelatinase (MMP-9) cleavage site in native type V collagen.

Native type V collagen molecules resist mammalian collagenase but are cleaved by certain gelatinases. We report a prominent site of cleavage within the collagen type V molecules by 92 kDa gelatinase (MMP-9). The enzyme was purified from conditioned medium of a rabbit synovial cell line (HIG-82). It cleaved native type V collagen from bovine bone in solution at two molecular sites, one near the amino-terminus, the other producing a 3/5 C-terminal fragment. Amino-terminal sequence analysis of the individual alpha chains from this latter fragment showed that MMP-9 had cleaved between residues Gly439-Val in both alpha 1(V) and alpha (XI) and between residues Gly445-Leu in the alpha 2(V) chain. These sites are close to the previously reported trypsin-cleavage site. The findings imply that gelatinases may be necessary for initiating or completing degradation of type I/type V copolymeric fibrils for growth and remodeling of extracellular collagen.

Amino Acid Sequence↗

PubMed2001

Type V collagen distribution in liver is reconstructed in coculture system of hepatocytes and stellate cells; the possible functions of type V collagen in liver under normal and pathological conditions.

The contents of type I, type III and type V collagen and the collagen type specific distributions in liver under normal and cirrhotic conditions were examined. In CCl4 injected rat, the increasing amount of type V collagen was a specific event during the progression of cirrhosis. In normal liver, immunohistochemical observation showed that type V collagen was localized on the fine fibrils, while type I was localized on the thick fibril. Type V collagen was partially colocalized with type IV collagen. In the cirrhotic liver, type V collagen was localized on the margin of the thick fibrous septa along with type IV collagen. Type I collagen existed in the core region of fibrous septa where the stellate cells were prominent. To elucidate the mechanism of the type specific deposition of collagen in the liver, we constructed a coculture system using both stellate cells and hepatocytes. In this system, type V collagen was mainly deposited on hepatocyte colonies not on stellate cells, while type I collagen fibrils were localized on stellate cells. The spatial positioning of type I and type V collagens in vitro was similar to that in the liver. In the cell adhesion assay, the adhesion of stellate cells to type V collagen was poorer than that of the hepatocytes. The collagen type-specific affinity of the stellate cells and hepatocytes may explain the specific localization of type V collagen in the liver and coculture system. These results suggested that the functions of type V collagen are not only to connect type IV collagen with type I collagen fibril, but also to protect the parenchyma from excess type I collagen deposition produced by stellate cells under pathological conditions.

Animals↗

PubMed2004

Type V collagen controls the initiation of collagen fibril assembly.

Vertebrate collagen fibrils are heterotypically composed of a quantitatively major and minor fibril collagen. In non-cartilaginous tissues, type I collagen accounts for the majority of the collagen mass, and collagen type V, the functions of which are poorly understood, is a minor component. Type V collagen has been implicated in the regulation of fibril diameter, and we reported recently preliminary evidence that type V collagen is required for collagen fibril nucleation (Wenstrup, R. J., Florer, J. B., Cole, W. G., Willing, M. C., and Birk, D. E. (2004) J. Cell. Biochem. 92, 113-124). The purpose of this study was to define the roles of type V collagen in the regulation of collagen fibrillogenesis and matrix assembly. Mouse embryos completely deficient in pro-alpha1(V) chains were created by homologous recombination. The col5a1-/- animals die in early embryogenesis, at approximately embryonic day 10. The type V collagen-deficient mice demonstrate a virtual lack of collagen fibril formation. In contrast, the col5a1+/- animals are viable. The reduced type V collagen content is associated with a 50% reduction in fibril number and dermal collagen content. In addition, relatively normal, cylindrical fibrils are assembled with a second population of large, structurally abnormal collagen fibrils. The structural properties of the abnormal matrix are decreased relative to the wild type control animals. These data indicate a central role for the evolutionary, ancient type V collagen in the regulation of fibrillogenesis. The complete dependence of fibril formation on type V collagen is indicative of the critical role of the latter in early fibril initiation. In addition, this fibril collagen is important in the determination of fibril structure and matrix organization.

Animals↗

PubMed2001

The fibril structure of type V collagen triple-helical domain.

Although the triple-helical structure of fibrillar collagen is regarded in general as being quite similar, each type of collagen molecule has inherent characteristics in the triple-helical domain. Few studies have ever been performed in terms of the aggregate structure of the triple-helical domain of fibrillar collagen. Reconstituted aggregates from the purified triple-helical domain of each type of fibrillar collagen might amplify the subtle differences in the structural characteristics of each type of collagen molecule. In this study, the reconstituted aggregate structure of pepsin-treated type V collagen (type Vp collagen), that is, virtually its triple-helical domain was characterized by transmission electron microscopy. Pepsin-treated type I (type Ip) and type II (type IIp) collagen were compared with type Vp collagen. Unique features of the aggregate structure of the triple-helical domain of the type V collagen can be summarized as follows:These results suggested that the lateral packing of the triple-helical domain of type V collagen is determined by its molecular structure. The characteristics of type Vp collagen fibrils might be explained by their characteristic amino acid composition. A significant feature of the triple-helical domain of type V collagen is the high content of glycosylated hydroxylysine residues. Molecular model building of the collagenous structure suggests that a change in surface roughness is conspicuous by incorporating the glycosylated hydroxylysine residues. More than a ten-fold content of bulky glycosylated hydroxylysine residues in type V collagen compared to that of type I might have a significant influence on both the intermolecular and interfibrillar interactions of the triple-helical domain of type V collagen molecule.

Amino Acid Sequence↗

PubMed1992

The human rhabdomyosarcoma cell line A204 lays down a highly insoluble matrix composed mainly of alpha 1 type-XI and alpha 2 type-V collagen chains.

The biosynthesis of collagen by the A204 cell line was examined using polyclonal antibodies raised against collagen type V and type XI. The study of the pepsin-digested collagen showed that it is composed mainly of alpha 1(XI) and alpha 2(V) collagen chains in an apparent 2:1 ratio, suggesting the formation of heterotypic molecules [alpha 1(XI)]2 alpha 2(V). The existence of this chain stoichiometry was further demonstrated by immunoprecipitation of the molecule with an antibody recognizing alpha 2(V) but not alpha 1(XI) collagen chains. Electron microscopy analyses of 24-h cultures showed that this matrix is composed of thin fibrils, that can be decorated with immunogold-labelled anti-(type-V collagen) IgG, but not with anti-(type-XI collagen) IgG. The collagen matrix laid down by A204 cells is highly insoluble. In the presence of beta-aminopropionitrile, an inhibitor of lysyl oxidase, only a small proportion of intact collagen could be extracted without proteolytic treatment. Immunoblotting of intact medium collagen from cultures performed in the presence of beta-aminopropionitrile showed four distinct bands with each antibody. The migration of the bands, stained with anti-(type-V collagen) IgG, had apparent molecular masses of 127, 149, 161 and 198 kDa (compared to globular standards) while the bands stained with anti-(type-XI collagen) IgG had apparent masses of 145, 182, 207 and 225 kDa. These data indicate that type-V and type-XI collagen chains can assemble in heterotypic isoforms. In this system, the synthesized isoforms are able to aggregate into a highly cohesive matrix and they undergo a proteolytic processing closely similar to that of other fibrillar collagens.

Blotting, Western↗

PubMed1999

Cloning of cDNA for rat pro alpha1(V) collagen mRNA. Expression patterns of type I, type III and type V collagen genes in experimental granulation tissue.

A cDNA clone for rat pro alpha1(V) collagen mRNA was constructed using PCR amplification, with primers based on human and hamster COL5A1 gene sequences. The clone pRCVA1 is 560 nucleotides long and it encodes for the carboxy propeptide of type V procollagen. Homology shared with type I collagen sequence was 64%, with type II collagen 65% and with type III collagen 61%. To evaluate the spatial and temporal expression of type V collagen mRNA in wound healing model, subcutaneously implanted viscose cellulose sponges in rats were used to induce granulation tissue formation. Analyses on granulation tissue were carried out on days 5, 8, 14, 21, 30, 59 and 84. Specific cDNA probes to pro alpha1(I), pro alpha1(III) and pro alpha1(V) collagen mRNA were used in slot blot, Northern and in situ hybridization. Type I collagen gene expression was upregulated at the initial stage of wound healing, type III collagen gene expression was constant and from the day 14 onwards type I and III collagen gene expressions were at the same level. Type V collagen gene expression was seen at every time point studied but at a considerably lower level than type I and III collagens. In situ hybridization showed that type V collagen was expressed in two different cell types. In conclusion, type V collagen was expressed in the wound healing model from at least day 5 onwards and it was synthesized by fibroblast-like and rounded cells.

Actins↗

PubMedDate not supplied

Diminished platelet adherence to type V collagen.

Different types of collagen vary in their influence on platelet reactivity. Collagen Types III, IV, and V were obtained from human placental tissue, and Type I collagen was prepared from rat skin. Each collagen type was coated onto a plastic surface. Each collagen-coated surface or appropriate plastic surface control was studied using citrated human 51Cr-labeled platelet-rich plasma in both the presence and absence of 10 microM adenosine 5'-diphosphate (ADP). Both unstimulated and ADP-induced platelet adherence were: 1) reduced by Type V collagen coating in comparison to uncoated wells; and 2) increased by Types III and IV collagen coating in comparison to Type V coated or plastic surfaces. Addition of the fast-acting thrombin inhibitor dansylarginine (DAPA) had no significant effect on unstimulated and ADP-induced platelet adherence to Type III, IV or V collagen-coated surfaces. Type I collagen-coated surfaces, studied only in the presence of DAPA, caused greater platelet adherence than those coated with Types III, IV, or V collagen. We conclude that Type V collagen may be less thrombogenic than Types, I, III, or IV.

Adenosine Diphosphate↗

PubMed2002

Collagenofibrotic glomerulopathy with a widespread expression of type-V collagen.

Collagenofibrotic glomerulopathy is considered as a form of glomerulopathy in which organized collagen type III progressively deposits. We report a case of this disease with widespread expression of collagen type V. A 65-year-old woman was admitted to our hospital for further evaluation of nephrotic-range proteinuria. The patient had had anemia and hypertension for 9 years, and proteinuria for 3 years. A renal biopsy specimen showed a remarkable mesangial expansion with Congo red-negative and periodic acid-Schiff-positive deposits. At the ultrastructural level, two forms of bundling fibers were found in the mesangium and subendothelial side of the glomerular basement membranes (GBM). The GBM itself appeared normal. Immunohistochemical investigation showed that the glomerular lesions were strongly reactive with both anti-collagen type-III and -V antibodies. Immunoelectron microscopy demonstrated collagen type V in both forms of bundling fibers. Despite therapy, her renal function declined. The clinical course and renal pathology of this case were in accordance with collagenofibrotic glomerulopathy except for the widespread expression of collagen type V. Collagen type V is a fibrillar collagen capable of forming banding fibrils. This report poses the question whether collagen type V accumulates only in this particular case or whether it is a normal component in collagenofibrotic glomerulopathy.

Aged↗

PubMed1986

Localization of type V collagen with monoclonal antibodies in developing dental and peridental tissues of the rat and hamster.

The distribution of collagen type V in developing dental and peridental tissues was investigated with the indirect immunofluorescence technique using unfixed, frozen sections of jaws from 1-2 day old neonatal rats and hamsters. Immunostaining for type V collagens was found both intracellularly and extracellularly in dental tissues of mesenchymal origin. In non-dental tissues, weak immunostaining was observed in the mesenchymally derived stroma surrounding the developing molar tooth germs but was more pronounced in larger cells, probably young osteoblasts in close vicinity to alveolar bone, and in some cells within developing salivary glands. Decalcification revealed a strong immunostaining in the extracellular bone matrices. In the dental tissues, the mesenchymally derived cells of the papilla exhibited an intracellular staining for type V collagen. In odontoblasts, increased immunostaining over that of other pulpal cells was observed just prior to or coinciding with the onset of predentin secretion and reactivity remained high in fully differentiated odontoblasts. A weak staining was observed in predentin but only after the onset of mineralization. As was the case for bone, after demineralization the dentin matrix stained intensely for type V collagen. The results demonstrate that type V collagen is actively synthesized by mesenchymal cells of developing hard tissues and that this type of collagen is an intrinsic component of hard connective tissue matrices. The data suggest that in developing tooth germs type V collagen is not involved in the differentiation process of either odontoblasts or ameloblasts.

Animals↗