Type VI collagen of the intervertebral disc. Biochemical and electron-microscopic characterization of the native protein

Wu, Jiann Jiu; Eyre, David R.; Slayter, Henry S.

doi:10.1042/bj2480373

Cited by 132 publications

(75 citation statements)

References 40 publications

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“…40 ' 43 The beaded filaments described in our study appear to be similar to those described by Brans et al 35 and Keene et al 33 However, Keene et al 33 have shown that type VI collagen is a component of a ruthenium red-stainable network. Furthermore, Wu et al 36 have suggested the interaction between type VI collagen and a component of the proteoglycan complex in the tissue. Therefore, it seems likely that the beaded filamentous structure of type VI collagen shown in Figure 15 is intimately associated with or entrapped in the proteoglycan complex.…”

Section: Discussionmentioning

confidence: 99%

Collagens in human atherosclerosis. Immunohistochemical analysis using collagen type-specific antibodies.

Katsuda

Okada

Minamoto

et al. 1992

Arterioscler Thromb

183

126

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This study represents a systematic analysis of the distribution of collagen types in human atherosclerotic lesions. Formalin-fixed, paraffin-embedded aortic tissues of 40 lesions from 16 different individuals ranging in age from 1 month to 84 years were examined immunohistochemically using antibodies to type I, III, IV, V, and VI collagens. Preembedding immunoelectron microscopy was used to simultaneously localize type V and VI collagens within the lesions. Localization of type HI collagen was very similar to that of type L and type VI collagen appeared together with these two types of collagen in the thickened intlmas of all stages of the lesion. Type V collagen was not detected in either fatty streaks or the mild Intimal thickening of the aortas of children. With advancing age and lesion progression, the immunoreactivity with anti-type V collagen antibody became more intense. Type IV collagen was detected in the basement membrane region of intimal cells. In advanced lesions thick deposits of type IV collagen were found around the elongated smooth muscle cells. Using immunoelectron microscopy, type V collagen was found to be localized to cross-banded collagen fibers, and type VI collagen was found to be localized to beaded filaments present throughout the interstitium of the thickened intima. These findings suggest that collagens preserve the pathophysiological and functional integrity of the vascular wall by providing mechanical support as well as assuring the proper interaction of cells during the formation of atherosclerotic lesions. (Arteriosclerosis and Thrombosis 1992;12:494-502) KEYWORDS • atherosclerosis • collagen • immunohistochemistryA therosclerosis is a disease of large and medium-/ \ sized arteries and is characterized by focal X A . thickening of the inner portion of the artery wall in association with fatty deposits.1 -2 The common underlying events responsible for lesion formation are intimal smooth muscle cell proliferation, formation of new extracellular matrix by these cells, and the possible accumulation of lipid. Collagens are regarded as important in this disease not only because they represent the major extracellular component in the atherosclerotic plaque and thereby contribute to the occlusive nature of the disease but also because they may play an important role in hemostasis and thrombosis through stimulation of blood platelets. 3 In addition, recent studies have indicated that collagens can influence the proliferation and state of differentiation of smooth muscle cells in vitro.4 -6 Thus, it seems likely that collagens could play a vital role in the pathogenesis of this disease.Collagen is now recognized as a family of proteins of at least 13 genetically distinct subtypes, each of which has a unique tissue specificity. -9 Of these 13 collagen types, six (I, III, IV, V, VI, and VIII) are present in blood vessels. 10 All of these collagen types except type VIII collagen are known to be synthesized by smooth From the Department of Pathology, School of Medicine, Kanazawa University, K...

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Section: Discussionmentioning

confidence: 99%

Collagens in human atherosclerosis. Immunohistochemical analysis using collagen type-specific antibodies.

Katsuda

Okada

Minamoto

et al. 1992

Arterioscler Thromb

183

126

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“…In most cases, predigestion of the sections with testicular hyaluronidase (Wu et al, 1987) was neccessary for optimal immunoreactivity for Col VI, whereas a number of other enzymatic pretreatments were ineffective.…”

Section: Distribution Of Col VI During Neural Crest Cell Migration Inmentioning

confidence: 99%

“…For purification of human Col VI microfilaments, human amnion was solubilized by digestion with bacterial collagenase from Clostridium histolyticum (Washington Biochemicals Corp., containing minor trypsin and clostripain activities), 2 x 5,000 U/200 g washed tissue, at room temperature for 48 hours (Rousselle et al, 1991) to liberate the microfibrillar matrix components (Wu et al, 1987;Kielty et al, 1990Kielty et al, ,1992Kuo et al, in preparation). After removal of the Kalinin-Klaminin complex (which is a primary contaminant of Col VI placental preparations) from the digest using antibody affinity columns (Rousselle et al, 1991), material in the unbound fraction was concentrated by a 50% saturated ammonium sulfate precipitation.…”

Section: Experimental Procedures Purification Of Col VImentioning

confidence: 99%

“…For this purpose, we isolated microfilaments, composed of numerous linearly arranged tetramers, and tested these microfilaments or the single tetramers for their ability to promote neural crest cell attachment and migration in vitro. Isolation and characterization of fibrillar structures of Col VI has previously been described and these structures have been considered to represent the most native forms of the collagen extractable from tissues (Wu et al, 1987;Fleischmajer et al, Kielty et al, l990,1992a,b). Both microfilaments and single Col VI tetramers showed a pronounced ability to stimulate neural crest cell attachment and migration in a manner comparable to that seen for fibronectin.…”

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Collagen type VI in neural crest development: Distribution in situ and interaction with cells in vitro

Perris

Kuo

Glanville

et al. 1993

Developmental Dynamics

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We have examined the spatiotemporal distribution of collagen type VI (Col VI) during neural crest development in vivo and its ability to promote neural crest cell attachment and migration in vitro. An affinity purified antiserum and chain-specific monoclonal antibodies against chicken Col VI were employed to immunolocalize the collagen in tissue sections and by immunoblotting. At stages of initial neural crest cell migration, the al(V1) and 012(VI) chains were immunolocalized in apposition with basement membranes of the neural tube, somites, notochord and ectoderm, whereas no immunoreactivity was seen for the cw3(VI) chain. Immunoblotting analysis confirmed the expression of cwl(V1) and a2(VI) chains and the lack of detectable immunoreactivity for the cw3(VI) chain at these early phases of neural crest development. Conversely, at advanced phases of migration and following gangliogenesis, expression of cw3(VI) chain coincided with that of cul(V1) and a2(VI) chains in apposition with basement membranes, around the dorsal root ganglia, and in fibrillar arrangements within the developing dermis and ventral sclerotome. The ability of Col VI to promote neural crest cell attachment and migration was tested in vitro using quantitative assays for these processes. Both native microfilaments and isolated tetramers of Col VI strongly promoted neural crest cell attachment and migration. Optimal stimulation of neural crest cell adhesion and migration was dependent upon structural integrity of Col VI since unfolded and disassembled (Y chains only weakly promoted cell attachment and were virtually inactive in supporting cell movement. The importance of a native macromolecular organization of Col VI further was analyzed in experiments in which dissociated tetramers were reassociated by Ca2+-and temperature-dependent self-aggregation. In contrast to native microfilaments, these oligomeric complexes were less effective in promoting neural crest cell movement, but still retained the ability to stimulate maximal cell attachment. The results indicate that Col VI is a primary component of the extracellular matrix deposited along neural crest migratory pathways, where it mayparticipate in the regulation of cell movement by functioning as a migratory substrate. The ability of Col VI to promote neural crest cell adhesion and motility is highly dependent upon maintainance of a native macromolecular arrangement.0 1993 Wiley-Liss, Inc.

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“…8,9) Collagen VI appears to be involved in the structural stabilization of the extracellular matrix via a direct interaction with other macromolecules, including collagen I. 10) Collagen VI has been reported to be a signiˆcant constituent of cartilaginous matrices 11) and fetal bone. 12) Although the amount of collagen VI has been found to be low in mature bone, 13) decreased levels have been reported in some cases of osteoporosis.…”

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confidence: 99%

Antisense Suppression of Collagen VI Synthesis Results in Reduced Expression of Collagen I in Normal Human Osteoblast-like Cells

Harumiya¹,

Gibson²,

Koshihara³

2002

Bioscience, Biotechnology, and Biochemistry

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Type VI collagen of the intervertebral disc. Biochemical and electron-microscopic characterization of the native protein

Cited by 132 publications

References 40 publications

Collagens in human atherosclerosis. Immunohistochemical analysis using collagen type-specific antibodies.

Collagens in human atherosclerosis. Immunohistochemical analysis using collagen type-specific antibodies.

Collagen type VI in neural crest development: Distribution in situ and interaction with cells in vitro

Antisense Suppression of Collagen VI Synthesis Results in Reduced Expression of Collagen I in Normal Human Osteoblast-like Cells

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