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Titolo:
IMMUNOHISTOCHEMICAL AND ULTRASTRUCTURAL-LOCALIZATION OF MP78 70 (BETA-IG-H3) IN EXTRACELLULAR-MATRIX OF DEVELOPING AND MATURE BOVINE-TISSUES/
Autore:
GIBSON MA; KUMARATILAKE JS; CLEARY EG;
Indirizzi:
UNIV ADELAIDE,DEPT PATHOL ADELAIDE SA 5005 AUSTRALIA
Titolo Testata:
The Journal of histochemistry and cytochemistry
fascicolo: 12, volume: 45, anno: 1997,
pagine: 1683 - 1696
SICI:
0022-1554(1997)45:12<1683:IAUOM7>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELASTIN-ASSOCIATED MICROFIBRILS; GROWTH-FACTOR-BETA; VI COLLAGEN; CONNECTIVE-TISSUE; CORNEAL EPITHELIUM; GLYCOPROTEIN MAGP; MOLECULAR-CLONING; CL GLYCOPROTEIN; IN-VITRO; COMPONENT;
Keywords:
MP78/70; BETA-IG-H3; FIBRILLIN-1; TYPE VI COLLAGEN; IMMUNOELECTRON MICROSCOPY; IMMUNOFLUORESCENCE; BOVINE TISSUES;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
M.A. Gibson et al., "IMMUNOHISTOCHEMICAL AND ULTRASTRUCTURAL-LOCALIZATION OF MP78 70 (BETA-IG-H3) IN EXTRACELLULAR-MATRIX OF DEVELOPING AND MATURE BOVINE-TISSUES/", The Journal of histochemistry and cytochemistry, 45(12), 1997, pp. 1683-1696

Abstract

MP78/70 is a matrix protein, with 78-kD and 70-kD isoforms, which wasinitially identified in bovine tissue extracts designed to solubilizeelastin-associated microfibrils. Peptide analysis has shown that MP78/70 is closely related to the human protein, beta ig-h3. In the present study an antibody raised to a synthetic beta ig-h3 peptide was shownspecifically to identify MP78/70 in purified form and in bovine tissue extracts. This is consistent with MP78/70 and beta ig-h3 being the bovine and human forms, respectively, of the same protein. The antibodywas 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; toreticular 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 thatMP78/70 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 theinteraction between interstitial collagen fibrils and other matrix structures, including some basement membranes and elastin-associated microfibrils.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 03:11:11