Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/5707
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Type: Journal article
Title: Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues
Other Titles: Immunohistochemical and ultrastructural localization of MP78/70 (beta ig-h3) in extracellular matrix of developing and mature bovine tissues
Author: Gibson, M.
Kumaratilake, J.
Cleary, E.
Citation: Journal of Histochemistry and Cytochemistry, 1997; 45(12):1683-1696
Publisher: HISTOCHEMICAL SOC INC
Issue Date: 1997
ISSN: 0022-1554
1551-5044
Statement of
Responsibility: 
Mark A. Gibson, Jaliya S. Kumaratilake, and Edward G. Cleary
Abstract: 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, βig-h3. In the present study an antibody raised to a synthetic βig-h3 peptide was shown specifically to identify MP78/70 in purified form and in bovine tissue extracts. This is consistent with MP78/70 and βig-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.
Keywords: Ligaments; Lung; Kidney; Aorta; Cornea; Spleen; Extracellular Matrix; Skin; Animals; Cattle; Collagen; Microfilament Proteins; Transforming Growth Factor beta; Neoplasm Proteins; Extracellular Matrix Proteins; Antibodies; Microscopy, Immunoelectron; Fluorescent Antibody Technique, Indirect; Immunoblotting; Enzyme-Linked Immunosorbent Assay; Tissue Distribution; Fibrillin-1; Fibrillins
Rights: Copyright © by The Histochemical Society
RMID: 0030006163
DOI: 10.1177/002215549704501212
Appears in Collections:Pathology publications

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