The immunohistochemical localisation of microfibril‐associated glycoprotein (MAGP) in elastic and non‐elastic tissues

Gibson, Mark; Cleary, Eimear

doi:10.1038/icb.1987.39

Cited by 61 publications

(35 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Fibrillin-containing microfibrils are thought to serve as a framework for the deposition of elastin and thus forming the elastic fiber superstructure (Rosenbloom et al, 1993;Kielty and Shuttleworth, 1995). Fibrillin-containing fibers are also found without elastin in some tissues (Gibson and Cleary, 1987;Wright et al, 1994;Zhang et al, 1995).…”

mentioning

confidence: 99%

Distribution of the elastic fiber and associated proteins in flexor tendon reflects function

2002

View full text Add to dashboard Cite

The elastic fiber is known to be an important component of skin, lung, and vasculature. Much less is known about the distribution of elastin and elastic fiber-related proteins in connective tissues, yet genetic defects of elastic fiber constituents can lead to deficiencies in these tissues. For the first time, we determine the distribution of elastin, fibrillins 1 and 2, and microfibril-associated glycoproteins (MAGPs) 1 and 2 in the flexor digitorum profundus (FDP) tendon. Three functionally distinct regions of the FDP tendon, the fibrocartilagenous (FC) region, avascular/tensional (AV/T) region, and insertion region, were evaluated by immunohistochemical methods for these five proteins. Biochemical analysis of desmosine content, an elastin-specific cross-link, demonstrated the presence of elastin in each region, and this was verified histochemically. The fibrillins were found with elastin and also pericellularly with internal fibroblasts where elastin was not detected. Although there was overlapping distribution, fibrillin 2 was more prominent in the interior of the tendon while fibrillin 1 was prominent in outer cell layers that contained elastic fibers. Both MAGP-1 and -2 were found throughout the tendon, although the greatest abundance was near the tendon insertion to bone. Surprisingly, MAGP-1 demonstrated a filamentous appearance within the fibrocartilage that did not correspond to the fibrillin 1 or 2 or MAGP-2 staining pattern. Lastly, we have shown that a vincular membrane located along the dorsal surface of the tendon near the insertion has a very high elastin content and a unique interface with the tendon that consists of an elastic anchor within the tendon body. Anat Rec 268: 430 -440, 2002.

show abstract

mentioning

confidence: 99%

Distribution of the elastic fiber and associated proteins in flexor tendon reflects function

2002

View full text Add to dashboard Cite

show abstract

“…Sections (4 m thick) were cut using a cryostat and incubated with primary antibody, followed by an appropriate secondary antibody coupled to fluorescein as described previously (Gibson and Cleary 1987). For optimal activity the anti-MP78/70 antibodies and the anti-fibrillin-1 monoclonal antibody A5 required pretreatment of the tissue sections with 6 M GuHCl and 6 M GuHCl/DTT, respectively, indicating that the epitopes are masked.…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

“…Antibodies were eluted with 0.2 M glycine, pH 2.8, and recovered as described previously (Gibson and Cleary 1987). Monoclonal anti-fibrillin-1 antibody A5 and polyclonal anti-tropoelastin antibodies have been described previously (Gibson and Cleary 1987;Gibson et al 1995). Polyclonal antibodies to purified pepsin-treated Type VI collagen were prepared in rabbits and affinity-purified on columns of the protein coupled to Sepharose CL-4B.…”

Section: Antibody Productionmentioning

confidence: 99%

“…The resulting antibodies were purified by affinity chromatography on columns of MP78/70 coupled to CNBractivated Sepharose CL-4B using the method of Kohn and Wilcheck (1982). Antibodies were eluted with 0.2 M glycine, pH 2.8, and recovered as described previously (Gibson and Cleary 1987). Monoclonal anti-fibrillin-1 antibody A5 and polyclonal anti-tropoelastin antibodies have been described previously (Gibson and Cleary 1987;Gibson et al 1995).…”

Section: Antibody Productionmentioning

confidence: 99%

See 1 more Smart Citation

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.

View full text Add to dashboard Cite

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.

show abstract

“…these cells contain both MAGP and fibrillin-1, and that tropoelastin is tightly associated with microfibrils [19][20][21].…”

Section: Figure 2 Antibody To the C-terminus Of Tropoelastin (Ct E ) mentioning

confidence: 99%

Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly

BROWN-AUGSBURGER¹,

BROEKELMANN²,

ROSENBLOOM³

et al. 1997

Biochemical Journal

View full text Add to dashboard Cite

Studies in itro suggest that the C-terminus of tropoelastin mediates elastin polymerization through an interaction with microfibril-associated proteins. In this study we have used cultured auricular chondrocytes as a model system to examine whether this interaction is critical for elastic fibre formation in i o. Auricular chondrocytes, which deposit an abundant elastic fibre matrix, were cultured in the presence of Fab fragments of antibodies directed against the C-terminus (CT e ) or an N-terminal domain (AT e ) of tropoelastin. Immunofluorescent staining of the extracellular matrix deposited by the cells showed that the CT e antibody inhibited the deposition of elastin without affecting microfibril structure. Cells grown under identical conditions in the presence of AT e , however, formed fibres that stained normally for both elastin and microfibril proteins. Chondrocytes cultured in the presence of microfibril-associated glycoprotein (MAGP) : 21-35, an antibody directed against a domain near the

show abstract

The immunohistochemical localisation of microfibril‐associated glycoprotein (MAGP) in elastic and non‐elastic tissues

Cited by 61 publications

References 22 publications

Distribution of the elastic fiber and associated proteins in flexor tendon reflects function

Distribution of the elastic fiber and associated proteins in flexor tendon reflects function

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

Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly

Contact Info

Product

Resources

About