Immunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues

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dc.contributor.authorGibson, M.
dc.contributor.authorKumaratilake, J.
dc.contributor.authorCleary, E.
dc.date.issued1997
dc.description.abstractMP78/70 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.
dc.description.statementofresponsibilityMark A. Gibson, Jaliya S. Kumaratilake, and Edward G. Cleary
dc.identifier.citationJournal of Histochemistry and Cytochemistry, 1997; 45(12):1683-1696
dc.identifier.doi10.1177/002215549704501212
dc.identifier.issn0022-1554
dc.identifier.issn1551-5044
dc.identifier.orcidKumaratilake, J. [0000-0001-5904-7629]
dc.identifier.urihttp://hdl.handle.net/2440/5707
dc.language.isoen
dc.publisherHISTOCHEMICAL SOC INC
dc.rightsCopyright © by The Histochemical Society
dc.source.urihttps://doi.org/10.1177/002215549704501212
dc.subjectLigaments
dc.subjectLung
dc.subjectKidney
dc.subjectAorta
dc.subjectCornea
dc.subjectSpleen
dc.subjectExtracellular Matrix
dc.subjectSkin
dc.subjectAnimals
dc.subjectCattle
dc.subjectCollagen
dc.subjectMicrofilament Proteins
dc.subjectTransforming Growth Factor beta
dc.subjectNeoplasm Proteins
dc.subjectExtracellular Matrix Proteins
dc.subjectAntibodies
dc.subjectMicroscopy, Immunoelectron
dc.subjectFluorescent Antibody Technique, Indirect
dc.subjectImmunoblotting
dc.subjectEnzyme-Linked Immunosorbent Assay
dc.subjectTissue Distribution
dc.subjectFibrillin-1
dc.subjectFibrillins
dc.titleImmunohistochemical and ultrastructural localization of MP78/70 (βig-h3) in extracellular matrix of developing and mature bovine tissues
dc.title.alternativeImmunohistochemical and ultrastructural localization of MP78/70 (beta ig-h3) in extracellular matrix of developing and mature bovine tissues
dc.typeJournal article
pubs.publication-statusPublished

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