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PubMed1997

Inhibition of migration of endothelial cells by type V collagen and high molecular weight kininogens.

The failure of synthetic vascular grafts in humans is complex and related not only to the type of material but also to the accumulation of cellular and noncellular components onto or within the material. Proteins that adsorb on biomaterials such as vascular grafts may be involved in modulating cell function. Of these components, type V collagen and high molecular weight kininogens (HMWKs) are known to localize on the surface of vascular grafts. We have investigated the effect of type V collagen and HMWKs in the prevention of endothelialization of vascular prostheses by inhibiting cell migration. Inhibition of endothelial cell migration may lead to incomplete endothelialization and thus, failure of these devices. Various concentrations of type V collagen and HMWK solutions were placed at the bottom of 24 well tissue culture plates with porous membrane inserts (8 microns pore size) placed on top. Suspended human umbilical vein endothelial cells (HUVECs) were placed on top of the insert and incubated at 37 degrees C for 2 hours. Following incubation, the inserts were fixed and the cells that migrated through the pores were counted by microscopy. Our results showed that migration of endothelial cells was significantly inhibited in a dose dependent manner by type V collagen and HMWKs.

Cell Movement↗
PubMed1992

Adhesion of 8701-BC breast cancer cells to type V collagen and 67 kDa receptor.

Ductal infiltration carcinomas (d.i.c.) of the breast are potentially highly metastatic tumours, associated with drastic alterations of the architecture and molecular composition of the extracellular matrix at the tumour-host interface. 8701-BC, a recently characterized cell line, isolated from primary d.i.c., was used to study different aspects of tumor cell-substratum interactions. Since type V collagen deposition is augmented in d.i.c. we have examined the ability of 8701-BC cells to interact with this collagen species. We have found that cell binding to type V collagen was mediated by protein homologous to the 67 kDa laminin receptor (67-R). This conclusion is substantiated by the following observations: (a) a major band having an apparent molecular mass of 67 kDa and immunoreactive to the anti-67 R antibody was detectable by SDS-PAGE of the membrane proteins; (b) the antibody inhibited cellular adhesion to type V collagen in a dose-dependent way; (c) membrane proteins purified by affinity chromatography on type V collagen were immunoreactive to anti-67 R antibody, but not to anti-VLA1, VLA2 and VLA3 integrin antibodies. This receptor appears to have prominent carbohydrate-binding properties, since lactose competes with cell adhesion to type V collagen.

Animals↗
PubMed1997

Increase in the relative level of type V collagen in the placentae of patients with pre-eclampsia.

To obtain some insight into the extracellular matrix in the human placenta, we investigated the composition of collagens purified from the placentae of patients with pre-eclampsia and compared it with normal placentae. Collagen was extracted from the placentae of both normal and pre-eclampsia pregnancies during the third trimester. The relative amounts of various collagens were evaluated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The ratio of the intensity of the band corresponding to the alpha 1 (III) chain with that of the alpha 1 (I) chain in placentae of pre-eclampsia was significantly lower than in normal placentae (P < 0.05). In contrast, the ratio of the intensity of the band corresponding to the alpha 1 (V) chain with that of the alpha 1 (I) chain in placentae of pre-eclampsia was significantly higher than in normal placentae (P < 0.05). The results suggest that an increased level of type V collagen relative to type I collagen in the placentae of pre-eclampsia might be closely associated with the disturbance to trophoblastic cell functions and the supply of nutrients to the developing fetus necessary for the maintenance of pregnancy.

Adult↗
PubMed1984

Extracellular matrices in the developing avian eye: type V collagen in corneal and noncorneal tissues.

We have used immunofluorescence histochemistry to examine the temporal and spatial deposition of type V collagen in the extracellular matrices of the developing chick cornea and other selected ocular structures. Tissue sections from animals ranging in age from 4-day-old embryos to 1-day post-hatching were examined by indirect immunofluorescence employing monoclonal antibodies specific for conformational dependent sites in this molecule. In eyes from embryos younger than 6 days of development, no type V staining could be detected. Thus, the epithelially derived primary corneal stroma, which is already well formed at this time, contains little if any of this molecule. Its appearance was concomitant with the physical swelling of the primary stroma and invasion of pericorneal mesenchymal cells. Staining was initially localized in the anterior cornea; subsequently, all corneal matrices showed intense reactions, including the stroma proper and Bowman's and Descemet's membranes. In adjacent noncorneal tissues, the appearance of type V collagen occurred later in development. In some of these, such as in the ciliary body, the pattern of acquisition involved initial deposition at an epithelial-mesenchymal interface with subsequent progression of fibrous strands out into the surrounding mesenchymal tissue. Eventually, all ocular structures with a dense connective tissue component showed staining, but the intensity was appreciably less than that within the cornea. We have previously reported that in all mature tissues except Bowman's membrane, type V collagen is present in an "antigenically masked" form, and that unmasking can be achieved by pretreatment of the tissue sections with dilute acetic acid.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1982

Type V collagens of the human placenta: trimer alpha-chain composition, ultrastructural morphology and peptide analysis.

The alpha-chain trimer composition of type V collagen preparations from human placental membrane and villi was determined by two-dimensional electrophoresis on a non-denaturing polyacrylamide gel system followed by electrophoresis in the presence of sodium dodecylsulfate. In preparations isolated from placental membranes pure type V collagen was found with the alpha-chain composition [alpha 1(V)]2 alpha 2(V). In preparations from placental villi two different collagen trimers could be identified with alpha-chain compositions [alpha 1(V)]2 alpha 2(V) and [alpha 3(V)]3. Two-dimensional peptide maps after chymotryptic digestion of the various alpha-chain revealed distinct patterns for alpha 1(V), alpha 2(V) and alpha 3(V) suggesting unique structures for all three alpha-chains. Shadowing of the two collagen preparations with carbon-platinum by the rotary shadowing technique allowed the visualization of the individual molecules. In the placental membrane preparations, a uniform species of molecules was present while in placental villi preparations the same elongated form of collagen was found together with larger aggregates presumably containing molecules with the alpha 3-chain component. These data are interpreted to indicate that so-called type V collagen, at least in preparations from placental villi, contain two distinct collagen molecules.

Chymotrypsin↗
PubMed1987

Type V collagen in splenic reticular fibers of the macaque monkey.

The distribution of type I, III and V collagens in the monkey spleen was examined by indirect immunofluorescent microscopy and immunoelectron microscopy, and compared with that of reticular fibers revealed by a silver impregnation method. Type I collagen was localized on reticular fibers in the white pulps and on coarse reticular fibers in the splenic cords. Type III collagen was localized on the reticular fibers in the white pulps, and on the coarse reticular fibers and a limited number of fine reticular fibers, in the splenic cords. The anti-type V collagen antibody reacted with annular reticular fibers around the splenic sinuses, as well as with the reticular fibers in the white pulps and with the coarse and fine reticular fibers in the splenic cords. Thus, the distribution pattern of fibers that reacted with the anti-type V collagen antibody was very similar to that of the reticular fibers revealed by the silver impregnation method. Electron-microscopically, the fine reticular fibers in the splenic cords were composed of collagen fibrils, 30-50 nm in diameter, and amorphous substances. They were covered by reticular cell processes. By immunoperoxidase labeling with the anti-type V collagen antibody, electron-dense reaction products were found over the collagen fibrils with a banding pattern. These results indicate that type V collagen is an indispensable component of the reticular fibers.

Animals↗
PubMed1989

Bone type V collagen: chain composition and location of a trypsin cleavage site.

The component alpha-chains of type V collagen from bovine bone were isolated and structurally characterized by gel electrophoresis, high performance liquid chromatography (HPLC) and amino acid sequence analysis. Three distinct alpha-chains were identified. Two of these were the well described alpha 1 (V) and alpha 2 (V) chains; the third proved to be identical to the cartilage alpha 1 (XI) chain. In adult bone the ratio between the three chains was about 1:1:1. Native type V collagen was cleaved by trypsin at 33 degrees C or 37 degrees C into 3/5 fragments. Aminoterminal sequence analysis of the alpha 1 (V) and alpha 1 (XI) fragments showed they both resulted from trypsin cleavage between residue 434 and 435. Trypsin apparently cleaves the type V molecule within a relatively unstable domain of the triple helix which presumably may also be a natural site of initial cleavage by a protease in vivo.

Amino Acid Sequence↗
PubMed1987

Skin tumor promotion is associated with increased type V collagen content in the dermis.

Tumor promotion in mouse skin depends upon establishment of hyperproliferation as well as inflammation and involves disturbance of normal communication between dermis and epidermis. As the collagenous matrix of the dermis is known to play an important role in the maintenance of normal dermal-epidermal interactions, alterations of the dermal collagen types during tumor promotion with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) were investigated. In TPA-treated samples no difference between the relative content of type I and III collagen was observed, whereas the content of type V was significantly increased. When TPA treatment was discontinued before tumor development no increase of type V collagen was observed. Furthermore, treatment with the non-promoting mitogens 4-O-methyl-TPA and Ca-ionophore A 23187 did not result in any alterations of the matrix composition. These data indicate that the increase of type V collagen content is part of the disturbed tissue interactions between dermis and epidermis that facilitate tumor development.

Animals↗
PubMed1982

Collagen metabolism in rat incisor predentine in vivo: synthesis and maturation of type I, alpha 1 (I) trimer, and type V collagens.

Collagen synthesis and deposition in the predentine of the continuously erupting rat incisor was analyzed in vivo following a single intraperitoneal injection of [14C]glycine. Newly synthesized collagen was extracted from the dissected predentine with a solution of 1.0 m sodium chloride containing proteolytic enzyme inhibitors. Mature, cross-linked collagen was solubilized by limited pepsin digestion following extractions with 0.5 M acetic acid or 0.1 M penicillamine. Analysis of the radiolabeled collagens by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography showed that over 97% of collagen synthesized migrated in the alpha 1 (I) and alpha 2 positions following pepsin digestion; the remaining 3% migrated in the positions of alpha 1 (V) and alpha 3 (V) collagens. However, from the ratio of the alpha 1 (I): alpha 2 it was estimated that approximately 30% of the salt-extractable collagen was alpha 1 (I) trimer. The presence of this collagen was confirmed by salt-fractionation and cyanogen bromide digestion patterns. Type I, alpha 1 (I) trimer, and type V collagens were also found in the salt-insoluble tissue residue. In this fraction the alpha 1 (I) trimer comprised 10-15% of the collagen measured as radioactivity but was difficult to discern colorimetrically. Type III collagen could not be detected in any of the fractions analyzed. From the profiles of isotope incorporation into collagens and collagen precursors, it was evident that collagen synthesis and processing was rapid. Processing of type I collagen and probably also alpha 1 (I) trimer proceeded almost entirely through procollagen intermediates. Rapid maturation of the types I and V collagens in the salt-insoluble fraction and the appearance of beta and gamma chains as early as 30 min after isotope administration. Radiolabeled procollagens were also extracted with acetic acid and penicillamine, indicating that cross-linking of collagen precursors may be involved in fiber formation.

Animals↗
PubMed1998

Decreased type V collagen expression in human decidual tissues of spontaneous abortion during early pregnancy.

AIM: To provide some insight into the aetiology of spontaneous abortion, the contents of type V collagen was investigated in human decidual tissues in spontaneous abortion and normal pregnancy. METHODS: Collagens were extracted from decidual tissues in spontaneous abortion (n = 19) and normal pregnancy (n = 25). The different types of collagen alpha chains were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), stained with Coomassie brilliant blue, and measured by densitometry. The relative amounts of the alpha 1 (III) and alpha 1 (V) chains were calculated by dividing the band intensities of the alpha 1 (III) and alpha 1 (V) chains by that of the alpha 1 (I) chain. RESULTS: The ratio of the alpha 1 (V) chain to that of the alpha 1 (I) chain in decidual tissues in spontaneous abortion was significantly lower than that found in normal pregnancy (p < 0.05). CONCLUSIONS: These results suggest that type V collagen might play an important role in the maintenance of pregnancy and that decreased expression of this collagen could be associated with spontaneous abortion.

Abortion, Spontaneous↗
PubMed2003

Simple and rapid chromatographic purification of type V collagen from a pepsin digest of porcine intestinal connective tissue, an unmanageable starting material for conventional column chromatography.

A chromatographic method is described for purification of type V collagen, a minor constituent in extracellular matrix, from a pepsin digest of porcine intestinal connective tissue. The starting material was a viscous and turbid solution even after centrifugation. Direct application of the sample to a commercially available DEAE-cellulose column resulted in clogging. On the other hand, type V collagen, [alpha1(V)](2)alpha2(V) form, was successfully captured by a filter paper-based DEAE-cellulose column chromatography and purified by a subsequent commercially available cation-exchange medium without clogging. This is a vast improvement over previously described salt fractionation methods.

Animals↗
PubMed2006

Anti-type V collagen lymphocytes that express IL-17 and IL-23 induce rejection pathology in fresh and well-healed lung transplants.

Immunity to collagen V [col(V)] contributes to lung 'rejection.' We hypothesized that ischemia reperfusion injury (IRI) associated with lung transplantation unmasks antigenic col(V) such that fresh and well-healed lung grafts have differential susceptibility to anti-col(V)-mediated injury; and expression of the autoimmune cytokines, IL-17 and IL-23, are associated with this process. Adoptive transfer of col(V)-reactive lymphocytes to WKY rats induced grade 2 rejection in fresh isografts, but induced worse pathology (grade 3) when transferred to isograft recipients 30 days post-transplantation. Immunhistochemistry detected col(V) in fresh and well-healed isografts but not native lungs. Hen egg lysozyme-reactive lymphocytes (HEL, control) did not induce lung disease in any group. Col(V), but not HEL, immunization induced transcripts for IL-17 and IL-23 (p19) in the cells utilized for adoptive transfer. Transcripts for IL-17 were upregulated in fresh, but not well-healed isografts after transfer of col(V)-reactive cells. These data show that IRI predisposes to anti-col(V)-mediated pathology; col(V)-reactive lymphocytes express IL-17 and IL-23; and anti-col(V)-mediated lung disease is associated with local expression of IL-17. Finally, because of similar histologic patterns, the pathology of clinical rejection may reflect the activity of autoimmunity to col(V) and/or alloimmunity.

Animals↗
PubMed2006

Structural requirements for heparin/heparan sulfate binding to type V collagen.

Collagen-proteoglycan interactions participate in the regulation of matrix assembly and in cell-matrix interactions. We reported previously that a fragment (Ile824-Pro950) of the collagen alpha1(V) chain, HepV, binds to heparin via a cluster of three major basic residues, Arg912, Arg918, and Arg921, and two additional residues, Lys905 and Arg909 (Delacoux, F., Fichard, A., Cogne, S., Garrone, R., and Ruggiero, F. (2000) J. Biol. Chem. 275, 29377-29382). Here, we further characterized the binding of HepV and collagen V to heparin and heparan sulfate by surface plasmon resonance assays. HepV bound to heparin and heparan sulfate with a similar affinity (KD approximately 18 and 36 nM, respectively) in a cation-dependent manner, and 2-O-sulfation of heparin was shown to be crucial for the binding. An octasaccharide of heparin and a decasaccharide of heparan sulfate were required for HepV binding. Studies with HepV mutants showed that the same basic residues were involved in the binding to heparin, to heparan sulfate, and to the cell surface. The contribution of Lys905 and Arg909 was found to be significant. The triple-helical peptide GPC(GPP)5G904-R918(GPP)5GPC-NH2 and native collagen V molecules formed much more stable complexes with heparin than HepV, and collagen V bound to heparin/heparan sulfate with a higher affinity (in the nanomolar range) than HepV. Heat and chemical denaturation strongly decreased the binding, indicating that the triple helix plays a major role in stabilizing the interaction with heparin. Collagen V and HepV may play different roles in cell-matrix interactions and in matrix assembly or remodeling mediated by their specific interactions with heparan sulfate.

Amino Acid Sequence↗
PubMed1983

Monoclonal antibodies against chicken type V collagen: production, specificity, and use for immunocytochemical localization in embryonic cornea and other organs.

Two monoclonal antibodies have been produced against chick type V collagen and shown to be highly specific for separate, conformational dependent determinants within this molecule. When used for immunocytochemical tissue localization, these antibodies show that a major site for the in situ deposition of type V is within the extracellular matrices of many dense connective tissues. In these, however, it is largely in a form unavailable to the antibodies, thus requiring a specific "unmasking" treatment to obtain successful immunocytochemical staining. The specificity of these two IgG antibodies was determined by inhibition ELISA, in which only type V and no other known collagen shows inhibition. In ELISA, mixtures of the two antibodies give an additive binding reaction to the collagen, suggesting that each is against a different antigenic determinant. That both antigenic determinants are conformational dependent, being either in, or closely associated with, the collagen helix is demonstrated by the loss of antibody binding to molecules that have been thermally denatured. The temperature at which this occurs, as assayed by inhibition ELISA, is very similar to that at which the collagen helix melts, as determined by optical rotation. This gives strong additional evidence that the antibodies are directed against the collagen. The antibodies were used for indirect immunofluorescence analyses of cryostat sections of corneas and other organs from 17 to 18-day-old chick embryos. Of all tissues examined only Bowman's membrane gave a strong staining reaction with cryostat sections of unfixed material. Staining in other areas of the cornea and in other tissues was very light or nonexistent. When, however, sections were pretreated with pepsin dissolved in dilute HAc or, surprisingly, with the dilute HAc itself dramatic new staining by the antibodies was observed in most tissues examined. The staining, which was specific for the anti-type V collagen antibodies, was largely confined to extracellular matrices of dense connective tissues. Experiments using protease inhibitors suggested that the "unmasking" did not involve proteolysis. We do not yet know the mechanism of this unmasking; however, one possibility is that the dilute acid causes swelling or conformational changes in a type-V collagen-containing supramolecular structure. Further studies should allow us to determine whether this is the case.

Animals↗
PubMed1989

Phorbol ester stimulates platelet spreading and thrombi-like aggregate formation on the surface of immobilized type V collagen.

We have studied the effect of the tumor-promoting phorbol ester, 4 beta-phorbol-12 beta-myristate-13 a-acetate (PMA), and of the stable prostaglandin endoperoxide analogue U46619 on the interaction of human blood platelets with surfaces coated with monomeric human type V collagen (CV) and on free calcium concentration in platelet cytoplasm. It was shown by scanning electron microscopy that native resting platelets sparingly attach to CV and fail to spread or aggregate on the collagenous substrate in the absence of PMA and U46619. Addition of 0.15-1.5 nM PMA or 1.5 microM U46619 stimulates platelet spreading and formation of multilayer (thrombi-like) platelet aggregates on the per se non-thrombogenic type V collagen substrate. It was further demonstrated using the fluorescent indicator quin2 that U46619 (0.1 microM) increases cytoplasmic free calcium concentration from basal level (100-120 nM) up to 600 nM, whereas PMA (0.75-15 nM) exerts only a minor effect, increasing free calcium level by 30-40 nM. These results indicate that the tumor-promoting phorbol ester PMA induces massive platelet spreading and aggregation on surfaces coated with non-thrombogenic type V collagen via activation of protein kinase C with little or no apparent change in free cytoplasmic calcium.

15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5↗
PubMed2006

MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen.

Matrix metalloproteinase-20 (MMP-20, enamelysin) has a highly restricted pattern of expression. In healthy tissues, MMP-20 is observed in the enamel organ and pulp organ of developing teeth and is present only as an activated enzyme. To identify other tissues that may express MMP-20, we performed a systematic mouse tissue expression screen. Among the non-tooth tissues assayed, MMP-20 transcripts were identified only in minute quantities within the large intestine. The murine Mmp20 promoter was cloned, sequenced, and assessed for potential tooth-specific regulatory elements. In silico analysis identified four promoter modules that were common to Mmp20 and at least two of three coregulated predominantly tooth-specific genes that encode ameloblastin, amelogenin, and enamelin. We asked if the highly restricted MMP-20 expression pattern was associated with a broad substrate specificity that might preclude its expression in other tissues. An iterative mixture-based random doedecamer peptide library screen with Edman sequencing of MMP-20 cleavage products revealed that, among MMPs previously screened, MMP-20 had unique substrate preferences. These preferences indicate that MMP-20 has a deep and wide catalytic pocket that can accommodate substrates with large aromatic residues in the P1' position. On the basis of matrices derived from the peptide library data, we identified and then confirmed that type V collagen is an MMP-20 substrate. Since type V collagen is not present in dental enamel but is an otherwise widely distributed collagen, and since only active MMP-20 has been observed in teeth, our data suggest that control of MMP-20 activity is primarily regulated by transcriptional means.

Animals↗
PubMed1995

Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly.

The tissue-specific organization of collagen molecules into tridimensional macroaggregates determines the physiomechanical properties of most connective tissues, but the factors and mechanisms controlling this process are unknown. It has been postulated that quantitatively minor types V and XI collagen regulate the growth of type I and II collagen fibrils, respectively. To test this hypothesis, we created mice that produce a structurally abnormal alpha 2(V) collagen chain. Homozygous mutant mice survive poorly, possibly because of complications from spinal deformities, and exhibit skin and eye abnormalities caused by disorganized type I collagen fibrils. Our results demonstrate that type V collagen is a key determinant in the assembly of tissue-specific matrices, and provide an animal model for human connective tissue disorders.

Animals↗