Type VI collagen is a major component of the human cornea

Zimmermann, Dieter R.; Trüeb, Beat; Winterhalter, Kaspar H.; Witmer, R; Fischer, Roland

doi:10.1016/0014-5793(86)80297-6

Cited by 117 publications

(65 citation statements)

References 15 publications

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“…Type VI collagen has previously been reported to be a constituent of perimysium and endomysium in skeletal muscle from adult chickens (Swasdison and Mayne 1989). The distribution of Type VI collagen found in the other tissues was also in agreement with previous studies Zimmermann et al 1986;Timpl and Engel 1987;Amenta et al 1988;Rittig et al 1990;Zhu et al 1994). The distribution of MP78/70 in fetal bovine skin ( Figure 3D) appeared to be similar to that described for ␤ig-h3 in human tissue (LeBaron et al 1995), with the highest signal being in the matrix close to the dermal/epidermal junction.…”

Section: Discussionsupporting

confidence: 91%

Immunohistochemical and Ultrastructural Localization of MP78/70 (βig-h3) in Extracellular Matrix of Developing and Mature Bovine Tissues

Gibson

Kumaratilake

Cleary

1997

J Histochem Cytochem.

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SUMMARY MP78/70 is a matrix protein, with 78-kD and 70-kD isoforms, which was initially identified in bovine tissue extracts designed to solubilize elastin-associated microfibrils. Peptide analysis has shown that MP78/70 is closely related to the human protein, ␤ ig-h3. In the present study an antibody raised to a synthetic ␤ ig-h3 peptide was shown specifically to identify MP78/70 in purified form and in bovine tissue extracts. This is consistent with MP78/70 and ␤ ig-h3 being the bovine and human forms, respectively, of the same protein. The antibody was further affinity-purified on MP78/70 bound to Sepharose and used to localize the protein in a range of bovine tissues. Immunofluorescence showed that MP78/70 was localized to collagen fibers in tissues such as developing nuchal ligament, aorta and lung, and mature cornea; to reticular fibers in fetal spleen; and to capsule and tubule basement membranes in developing kidney. No general localization to elastic fibers was observed. The staining pattern in most tissues more closely resembled that of Type VI collagen, which occurs as collagen fiber-associated microfibrils, than that of fibrillin-1, a component of elastin-associated microfibrils. However, MP78/70 appeared to be less widely distributed than Type VI collagen. Immunoelectron microscopy showed that MP78/70 was predominantly found in loose association with collagen fibers in most tissues examined and was also located on the surface of the capsule basement membrane in developing kidney. Double labeling experiments indicated that MP78/70 is co-distributed with Type VI collagen microfibrils located in these regions. In some elastic tissues significant immunolabel was detected in regions of interface between collagen fibers and fibrillin-containing microfibrils of adjacent elastic fibers, and at the outer margins of the latter structures. Overall, the evidence points to MP78/70 having a bridging function, perhaps in association with Type VI collagen microfibrils, linking or stabilizing the interaction between interstitial collagen fibrils and other matrix structures, including some basement membranes and elastin-associated microfibrils.

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Section: Discussionsupporting

confidence: 91%

Immunohistochemical and Ultrastructural Localization of MP78/70 (βig-h3) in Extracellular Matrix of Developing and Mature Bovine Tissues

Gibson

Kumaratilake

Cleary

1997

J Histochem Cytochem.

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“…While it has long been recognized that myocardium contains types I and III collagen [33][34][35] and the presence of type IV in myocyte basement membranes and capillary walls has also been shown [35,36], it is only recently that type VI collagen has been demonstrated in this tissue [5]. The present data which quantitate the amounts of several matrix components indicate that for rat heart as has been found for cornea [37] and several other tissues [38], type VI collagen may be considered a major extracellular constituent.…”

Section: Discussionsupporting

confidence: 62%

Increased rat myocardial type VI collagen in diabetes mellitus and hypertension

Spiro

Crowley

1993

Diabetologia

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Summary. Diabetic cardiomyopathy, a condition characterized by the accumulation of carbohYdrate-containing material surrounding the myocardial small blood vessels, has been studied in alloxan-diabetic normotensive and hypertensive rats. Immunochemical techniques were used to monitor several extracellular matrix constituents present in extracts of cardiac tissue, namely types I, IV and VI collagen, laminin and fibronectin, as well as myosin. These studies have indicated that after induction of diabetes, type VI collagen but none of the other matrix components studied, was significantly increased (from 2.29 + 0.04 mg/g in normal to 2.85 + 0.18 mg/g in diabetic ventricles, p < 0.01). Hypertension, whether induced by the clipping of one renal artery or genetically determined (spontaneously hypertensive rats), resulted in a similar elevation in type VI collagen (2.71 + 0.12 rag/g, p < 0.005 compared to normal rats). In the presence of diabetes plus hypertension the effect was not additive, the type VI collagen level being 2.93 + 0.15 (p < 0.001 compared to normal rats). Basement membrane collagen (type IV) in the myocardium appeared to be unaffected by diabetes or hypertension and the myosin contents of the hearts of the four experimental groups were similar. Quantitative determinations indicate that compared to type IV collagen, laminin or fibronectin, type VI collagen represents the major periodic acid-Schiff-reactive extracellular constituent of the rat ventricle. Its preferential increase in the heart in diabetes may provide insight into the molecular mechanisms of the diabetic microvascular disease.

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“…This would be consistent with the maintenance of small diameter fibrils observed in the mutant tendons. Collagen VI is also a major component of cornea and is closely associated with cornea fibroblasts (47). However, we found that collagen fibrillogenesis in the cornea is not affected by the absence of collagen VI.…”

Section: Volume 288 • Number 20 • May 17 2013mentioning

confidence: 53%

COL6A3 Protein Deficiency in Mice Leads to Muscle and Tendon Defects Similar to Human Collagen VI Congenital Muscular Dystrophy

Pan

Zhang

Markova

et al. 2013

Journal of Biological Chemistry

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Background:The collagen VI COL6A3 subunit may serve critical biological functions independent of the COL6A1 and COL6A2 subunits. Results: A Col6a3 mouse mutant displays muscle and tendon abnormalities resembling the Col6a1-null mouse. Conclusion:The primary role of the COL6A3 subunit is in assembling collagen VI microfibrils. Significance: The Col6a3 mutant mouse represents an animal model for collagen VI disorders.

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Type VI collagen is a major component of the human cornea

Cited by 117 publications

References 15 publications

Immunohistochemical and Ultrastructural Localization of MP78/70 (βig-h3) in Extracellular Matrix of Developing and Mature Bovine Tissues

Immunohistochemical and Ultrastructural Localization of MP78/70 (βig-h3) in Extracellular Matrix of Developing and Mature Bovine Tissues

Increased rat myocardial type VI collagen in diabetes mellitus and hypertension

COL6A3 Protein Deficiency in Mice Leads to Muscle and Tendon Defects Similar to Human Collagen VI Congenital Muscular Dystrophy

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