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PubMed1996

Increased expression of type VI collagen genes in cutis laxa fibroblasts.

Type VI collagen gene expression in cutis laxa was studied by measuring messenger RNA (mRNA) and protein production levels in four fibroblast strains from patients with congenital cutis laxa and comparing them with those in fibroblasts obtained from age-matched healthy subjects. Levels of type VI collagen mRNA were increased in all cutis laxa fibroblast strains and the levels of alpha 1 (VI) and alpha 3 (VI) chain mRNAs increased in parallel. Increases in type VI collagen mRNAs correlated well with production levels of the corresponding proteins, as determined by immunological assay. These results suggest that increased type VI collagen gene expression is one of the characteristics of cutis laxa dermal fibroblasts and that this abnormality may be related to the skin changes in cutis laxa.

Child, Preschool↗
PubMed1994

Immunofluorescence and biochemical studies of the type VI collagen expression by human glioblastoma cells in vitro.

The human glioblastoma cell line U-87 MG was found to express a 140 kD polypeptide which was recognized on immunoblot analysis by a monoclonal antibody to type VI collagen. This polypeptide was digestible by a highly purified bacterial collagenase. After treatment of U-87 MG cells by pepsin, the protein profile revealed the two major pepsin-resistant fragments identical in Mr to those of collagen VI extracted from human placenta. The respective peptide maps from V8 protease one-dimensional gels of these two fragments were identical to those obtained with human collagen VI. Immunofluorescent staining by antibodies to type VI collagen was observed in the extracellular matrix. Moreover, U-87 MG cells were found to be positive for A2B5, a cell surface marker specific for O-2A type glial precursor cells. These data indicate that the human glioblastoma cell line U-87 MG exhibits the properties of glial precursor cells and expresses collagen type VI in vitro. This cell line therefore may prove valuable for comparative investigations of the regulation of type VI collagen synthesis, and may be useful as a model to study the function and pathological importance of type VI collagen in human brain tumours, both in vitro and in vivo.

Biomarkers↗
PubMed1993

Microfibrillar assemblies of foetal bovine skin. Developmental expression and relative abundance of type VI collagen and fibrillin.

Intact type VI collagen microfibrils and fibrillin-containing microfibrils were isolated from foetal bovine skin and investigated immunochemically and ultrastructurally. Substantial variations were detected in the abundance and macromolecular assembly of these structures at progressive stages of gestation. Microfibrils of collagen VI were increasingly abundant in skin through foetal development from late first trimester to term. The pattern of expression of fibrillin-containing microfibrils in foetal skin differed from that of collagen VI. Fibrillin-containing microfibrils were particularly sparse in first trimester skin, and present only as short assemblies. However, by early second trimester there had been a sharp increase in the abundance and length of these fibrillin-containing microfibrils. These observations are consistent with early second trimester being a key phase of fibrillin assembly. In the third trimester, fibrillin-containing microfibrils were frequently isolated in association with amorphous material. This information on the pattern of expression and assembly of collagen VI microfibrils and fibrillin-containing microfibrils in foetal skin implies temporally and functionally distinct contributions of these two components to the establishment of the fibrous dermal matrix.

Animals↗
PubMed1997

Association of type VI collagen with D-periodic collagen fibrils in developing tail tendons of mice.

The process of the arrangement of D-periodic collagen fibrils and their growth in maturing tail tendon of mice were studied with the association of type VI collagen, from fetal day 10 to 10 weeks after birth. In tail tendons, the amount of collagen fibers gradually increased along with the diameters of D-periodic collagen fibrils during maturation. Type VI collagens first appeared on fetal day 10, when D-periodic collagen fibrils were not recognizable. Type VI collagens were observed around the fibroblastic cells in early stages of development, but were among thick collagen fibrils in the adult tendon. While the periodic distances of type VI collagen fibrils were over 100 nm at fetal days, they were packed to 80-90 nm after birth. The periodic bands were stained well with ruthenium red in adult but not in young tendons, indicating the close association of proteoglycans or glycosaminoglycans (PGs/GAGs) with maturing type VI collagens. Since type VI collagen in native form is known to associate with D-periodic collagen fibrils via PGs/ GAGs, ruthenium red-stainability on the surface of D-periodic collagen fibrils was also examined; results showed that ruthenium red-stainable elements were D-periodically associated. When the surface morphology of D-periodic collagen fibrils in adult animals was examined by atomic force microscopy, a large depth of the groove between elevated and depressed surfaces became prominent when the fibril surface was digested with hyaluronidase. Thus, it is possible to observe topologically the association of PGs/GAGs and probably that of type VI collagens with D-periodic collagen fibrils.

Animals↗
PubMed1995

Immunohistochemical expression of type VI collagen in superficial fibromatoses.

The expression of type VI collagen was studied immunohistochemically in 26 cases of superficial fibromatoses (palmar, plantar and penile) using an immunoperoxidase method for light microscopic visualization. The polyclonal antibody against type VI collagen used in this study was isolated from human placenta and its specifity was tested by immunoblotting assay. All cases consisted of multiple nodules showing a variable degree of cellularity and fibrosis. Depending on the predominant histological appearance of these nodules, each case was assigned to the three following phases: proliferative, involutional and residual. Morphologically normal palmar and plantar aponeuroses were included as controls. Immunohistochemical findings showed that type VI collagen was present as longitudinal thin fibers in normal palmar and plantar aponeuroses. A differential expression of this collagen was found in the different stages of superficial fibromatoses. Type VI collagen was markedly expressed as a distinct fibrillar network in the extracellular matrix (ECM) surrounding proliferating stromal cells in proliferative and involutional phases. Its expression completely disappeared from the connective tissue undergoing fibrotic transformation during involutional and residual phases. The results of the present study suggest that type VI collagen is an extracellular marker of stromal tissue proliferation and is involved in the early phases of tissue remodelling occurring in the superficial fibromatoses.

Collagen↗
PubMed2002

Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A).

The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure.

Amino Acid Motifs↗
PubMed1991

Immunolocalisation of type VI collagen in the intervertebral disc.

Type VI collagen has been isolated from many connective tissues, including the intervertebral disc. Distribution of this collagen, however, varies considerably within different tissues. In adult mammalian nasal and articular cartilage it is localised preferentially in the matrix immediately surrounding the cell. Intervertebral discs from various species and of various ages were studied and a similar pericellular localisation was found. When antisera to type VI collagen were used staining was seen around the cells of all sections of intervertebral disc, being particularly prominent in the nucleus pulposus. Staining on or around the cells was also seen in the adjacent cartilaginous end plate and bone.

Adult↗
PubMed1998

Increased content of type-VI collagen epitopes in human osteoarthritic cartilage: quantitation by inhibition ELISA.

Type-VI collagen is an integral part of the extracellular cartilage matrix. However, the exact amounts of type-VI collagen in normal and osteoarthritic human cartilage still are not known. In this study, we describe an inhibition enzyme-linked immunosorbent assay that was developed to quantitate type-VI collagen epitopes found in guanidinium chloride extracts from normal and osteoarthritic human cartilage. In 31 cartilage samples from various localizations of healthy adult human knees, type-VI collagen epitopes accounted for approximately 0.40% of the total collagen content. Interestingly, type-VI collagen epitopes increased about 4-fold in osteoarthritic cartilage. A statistically significant increase of type-VI collagen epitopes was found during early stages of the disease, with only a superficial roughening of the cartilage surface and a loss of proteoglycans. Thus, these findings indicate that type-VI collagen is a minor component of normal human articular cartilage and that the amount of type-VI collagen epitopes increases significantly during early stages of osteoarthritis.

Adult↗
PubMed1998

Severe disturbance of the distribution and expression of type VI collagen chains in osteoarthritic articular cartilage.

OBJECTIVE: The aim of this study was to evaluate the messenger RNA (mRNA) expression and distribution of the major pericellular type VI collagen in normal and osteoarthritic (OA) cartilage. METHODS: Conventional and confocal laser scanning immunohistochemistry, as well as in situ hybridization experiments, were performed for all 3 collagen type VI chains in sections of normal and OA articular cartilage. RESULTS: Normal adult articular chondrocytes were surrounded by a type VI collagen-positive pericellular matrix and showed significant levels of mRNA expression for all 3 type VI collagen chains. In OA cartilage, the expression and overall distribution of type VI collagen was largely increased in the lower middle and upper deep zones. In contrast, the upper zones showed a significant loss of pericellular type VI collagen staining. CONCLUSION: Our results suggest that there is a significant basic turnover of type VI collagen in normal articular cartilage. In OA cartilage, the chondrocytes of the lower middle and upper deep zones account for a net increase in type VI collagen synthesis. The loss of type VI collagen staining in the upper zones is most likely the result of increased protein degradation rather than reduced synthetic activity.

Aged↗
PubMed2002

Ultrastructural localization of type VI collagen in normal adult and osteoarthritic human articular cartilage.

OBJECTIVE: Type VI collagen is a major component of the pericellular matrix compartment in articular cartilage and shows severe alterations in osteoarthritic cartilage degeneration. In this study, we analysed the exact localization of type VI collagen in its relationship to the chondrocyte and the (inter)territorial cartilage matrix. Additionally, we were interested in its ultrastructural appearance in normal and osteoarthritic cartilage. DESIGN: Distribution and molecular appearance was investigated by conventional immunostaining, by multilabeling confocal scanning microscopy, conventional transmission, and immunoelectron microscopy. RESULTS: Our analysis confirmed the pericellular concentration of type VI collagen in normal and degenerated cartilage. Type VI collagen formed an interface in between the cell surface and the type II collagen network. The type VI collagen and the type II collagen networks appeared to have a slight physical overlap in both normal and diseased cartilage. Additionally, some epitope staining was observed in the cell-associated interterritorial cartilage matrix, which did not appear to have an immediate relation to the type II collagen fibrillar network as evaluated by immunoelectron microscopy. In osteoarthritic cartilage, significant differences were found compared with normal articular cartilage: the overall dimension of the lacunar volume increased, and a significantly increased type VI collagen epitope staining was observed in the interterritorial cartilage matrix. Also, the banded isoform of type VI collagen was found around many chondrocytes. CONCLUSIONS: Our study confirms the close association of type VI collagen with both, the chondrocyte cell surface and the territorial cartilage matrix. They show severe alterations in type VI collagen distribution and appearance in osteoarthritic cartilage. Our immunohistochemical and ultrastructural data are compatible with two ways of degradation of type VI collagen in osteoarthritic cartilage: (1) the pathologically increased physiological molecular degradation leading to the complete loss of type VI collagen filaments from the pericellular chondrocyte matrix and (2) the transformation of the fine filaments to the band-like form of type VI collagen. Both might implicate a significant loss of function of the pericellular microenvironment in osteoarthritic cartilage.

Adult↗
PubMed1998

Immunohistochemical distribution of type VI collagen in normal and glaucomatous human trabecular meshwork.

BACKGROUND: An abnormally increased presence of type VI collagen has been shown in the lamina cribrosa of patients with primary and secondary glaucoma. This study was undertaken to investigate the pattern of type VI collagen within the aqueous outflow structures of glaucoma patients. METHODS: Trabecular meshwork samples of eight normal donor eyes and trabeculectomy specimens of 21 patients with different types of glaucoma were processed for either cryo-sectioning or for paraffin embedding. Immunohistochemical staining was conducted by use of polyclonal rabbit antibodies against human collagen type VI. RESULTS: Immunoreactivity for type VI collagen was evident in the cores of all trabecular beams. The strongest staining was detected in the uveal region of the human trabecular meshwork. Immunohistochemical labelling for type VI collagen was not more pronounced in the aqueous outflow structures of glaucoma patients than in normal eyes. CONCLUSION: Collagen type VI is a ubiquitous structural component of the extracellular matrix in the human trabecular meshwork. However, type VI collagen does not appear to be of greater importance for the increased trabecular outflow resistance in glaucoma patients than in normal eyes.

Adolescent↗
PubMed1992

Light microscopic and ultrastructural distribution of type VI collagen in human liver: alterations in chronic biliary disease.

We have investigated the distribution of type VI collagen in normal human liver obtained from cadaveric renal transplant donors, using a peroxidase-antiperoxidase method for light microscopic visualization, and an immunogold labelling method for ultrastructural localization. The distribution was compared with that of the more abundant interstitial collagen type III, using antibodies to amino terminal procollagen type III. Staining for type VI collagen was identified in Glisson's capsule, in portal tract stroma and within the space of Disse. Perisinusoidal staining showed intra-acinar heterogeneity with the intensity in acinar zones 2 and 3 being greater than in zone 1. Type III collagen was also found in the space of Disse although no significant intra-acinar variation in staining intensity was noted. Immuno-gold labelling for type VI collagen was demonstrated on amorphous or microfilamentous material lying between, and occasionally appearing to interconnect, cross-striated collagen fibrils, whereas labelling for amino terminal procollagen type III was exclusively on fibrils. Intracellular staining for type VI collagen was noted in perisinusoidal (lto) cells. These results confirm that type VI collagen is a ubiquitous constituent of the normal hepatic extracellular matrix and suggest that it may be synthesized by perisinusoidal (lto) cells. The distribution of type VI collagen was also studied in biopsy material from patients with different histological stages of primary biliary cirrhosis. Intense staining was noted around proliferating bile ductules within developing fibrous septa and in established septa of cirrhotic liver. These observations indicate that this 'minor' matrix component may play an important role in hepatic fibrogenesis.

Chronic Disease↗
PubMed1990

Immunolocalization of type VI collagen in developing and healing rabbit cornea.

We have localized type VI collagen in normal developing and corneal scar tissue. Indirect immunofluorescence showed that type VI collagen was distributed throughout the normal stroma and most of the scar. No fluorescence was detected along the posterior margin of the scar and in a retrocorneal membrane continuous with the scar. Since the corneal endothelium in rabbits contributes to the formation of scar tissue and retrocorneal membrane, our observations suggest that the endothelium does not synthesize type VI collagen. Indirect immunoelectron microscopy showed that type VI collagen was located abundantly between collagen fibrils as fine filamentous structures containing beads with a periodicity of 100 nm, consistent with published observations of other tissues. Because these filaments are more prominent when stained with ruthenium red, and predigestion of tissue with Chondroitinase ABC enhances binding of monoclonal antibody to type VI collagen, proteoglycans probably are associated with this collagen in the cornea. Ultrastructural observations supported by previous biochemical analyses show that the proportion of type VI collagen to fibrillar collagen is smaller in scar tissue compared with fetal cornea. The abundance of type VI collagen and its distribution and association with proteoglycans in rabbit corneal tissues suggest that this macromolecule plays a role in the tensile strength and transparency of the stroma.

Animals↗
PubMed1997

A central segment of the NG2 proteoglycan is critical for the ability of glioma cells to bind and migrate toward type VI collagen.

Previous studies have established that the NG2 proteoglycan binds directly to type VI collagen. To further our understanding of the biochemical and functional significance of this interaction we have used NG2 cDNA to construct a series of NG2 mutants with deletions spaced throughout the entire length of the 260-kDa NG2 core protein. Following transfection of these mutant cDNAs into B28 glioma cells, we determined the ability of mutant NG2 molecules to anchor type VI collagen on the cell surface. Eight of 11 transfectant populations were able to anchor type VI collagen. The three NG2 variants incapable of anchoring type VI collagen have deletions clustered within the central one-third of the NG2 ectodomain. These deletions identify a 469-amino-acid domain of NG2 responsible for binding of type VI collagen. Functional consequences of the NG2-type VI collagen interaction were explored by testing the relative ability of NG2-transfected and untransfected glioma cells to migrate toward type VI collagen. NG2-expressing cells exhibited a greater migratory response toward type VI collagen than their NG2-negative counterparts. This enhanced migration could be specifically inhibited with NG2 antibodies. Furthermore, glioma cells expressing NG2 in which the collagen-binding domain was deleted failed to exhibit this enhanced migration, whereas NG2 mutants in which non-collagen-binding regions were deleted continued to exhibit increased chemotaxis toward the type VI collagen. These comparisons confirm the importance of the central collagen-binding domain in mediating functionally important interactions between NG2 and type VI collagen.

Animals↗
PubMed1996

Immunohistochemical distribution of type VI collagen in developing human kidney.

The distribution of type VI collagen was investigated immunohistochemically in the developing human kidney from 15 to 32 weeks gestational age and it was compared with that observed in the normal infantile and adult human kidney. In fetal kidney, type VI collagen was widely distributed as a fibrillar network in the subcapsularly undifferentiated mesenchyme and intertubular interstitium, and as a basement membrane-like structure around the ureteral bud branches, tubules, and collecting ducts. During nephrogenesis, type VI collagen disappeared from the induced mesenchyme close to the tips of ureteral branches, while it formed a distinct basement membrane-like structure around the early stages of nephron differentiation (comma-shaped and S-shaped bodies) and later along Bowman's capsule of capillary loop and maturing glomeruli A strong immureactivity for type VI collagen was also found in the glomerular basement membrane and mesangial areas of capillary loop and maturing glomeruli. In infantile kidney, type VI collagen showed a distribution pattern similar to that observed during the fetal period. In adult human kidney, glomerular basement membrane showed a weak positivity for type VI collagen and the basement membrane-like staining around Bowman's capsule, tubules, and collecting ducts was less evident than in fetal and infantile kidney. Our immunohistochemical findings suggest that type VI collagen is a normal component of the glomerular and extraglomerular extracellular matrix of developing human kidney and that it undergoes changes in the expression during maturation.

Adult↗
PubMed1994

Expression and distribution of type VI collagen in gynecomastia.

We investigated the distribution of type VI collagen in 36 cases of routinely fixed and paraffin-embedded gynecomastia using an immunoperoxidase method for light microscopic visualization. Four samples of normal male mammary gland tissue were also included as controls. A protease predigestion was essential for the visualization of this extracellular matrix (ECM) glycoprotein. In normal male breast, no immunoreaction for type VI collagen was detected in the stroma surrounding the ducts. Gynecomastia was classified into three histological types: florid (type I), fibrous (type II), and intermediate (type III). Type VI collagen was differentially expressed in the periductal stroma of all types. This collagen was markedly expressed at the early disease stage (type I) when the periductal stroma is highly cellular and vascular. Its expression decreased when periductal stroma undergoing fibrotic transformation (type III) and completely disappeared from the dense periductal stroma of fibrous stage (type II). These findings suggest that type VI collagen is involved in the ECM remodelling occurring in gynecomastia.

Adult↗
PubMed1990

Type VI collagen. In situ hybridizations and immunohistochemistry reveal abundant mRNA and protein levels in human neurofibroma, schwannoma and normal peripheral nerve tissues.

Cutaneous neurofibromas contain an extensive extracellular matrix composed of collagenous and non-collagenous macromolecules. In this study, the expression of type VI collagen genes in cutaneous neurofibromas was examined by a combination of in situ hybridizations and immunohistochemistry. In situ hybridizations with a 32P-labeled human type VI collagen-specific cDNA revealed that the majority of cells within neurofibromas expressed the gene for alpha 2(VI) collagen chain. The number of cells expressing clearly detectable levels of alpha 2(VI) collagen mRNA was considerably higher than that of cells actively expressing the pro alpha 1(I) or pro alpha 1(III) collagen genes. The presence of type VI collagen epitopes within the neurofibromas was also demonstrated by immunostaining with specific polyclonal antibodies. The expression of type VI collagen genes in neural tissues was further examined by immunostaining of a benign schwannoma tissue specimen consisting of Schwann cells. The results indicated close association of type VI collagen epitopes with the neoplastic Schwann cells. Immunolocalization of type VI collagen epitopes within normal human peripheral nerve revealed pericellular staining of perineurial cells and Schwann cells, suggesting synthesis of type VI collagen by these cell types. These results suggest that the expression of type VI collagen gene is active in nerve-derived tissues, and that type VI collagen may be a major component of the extracellular matrix in neural connective tissues.

Collagen↗
PubMed1990

Type VI collagen in healing rabbit corneal wounds.

A type-specific monoclonal antibody was used to examine the localization of type VI collagen in healing full-thickness corneal wounds (3 mm in diameter) in rabbits. By immunofluorescence, in 1-week-old wounds, type VI collagen was found only at the wound periphery. Subsequently, type VI collagen showed a rapid increase throughout the wounded area. In 3-week-old wounds, type VI collagen immunofluorescence had a laminar pattern as seen in normal corneal stroma, although it was irregular in arrangement. By electron-microscopic immunohistochemistry, type VI collagen was found in the pericellular region of fibroblastic cells possibly derived from keratocytes. These results suggest that type VI collagen might originate from the fibroblastic cells and play an important role in the regeneration of the corneal lamellar structure.

Animals↗