Immunolocalisation of BPTI-like serine proteinase inhibitory proteins in mast cells, chondrocytes and intervertebral disc fibrochondrocytes of ovine and bovine connective tissues. An immunohistochemical and biochemical study

Melrose, J; Smith, S; Rodgers, K; Little, C; Burkhardt, D; Ghosh, P

Immunolocalisation of BPTI-like serine proteinase inhibitory proteins in mast cells, chondrocytes and intervertebral disc fibrochondrocytes of ovine and bovine connective tissues. An immunohistochemical and biochemical study

Melrose, J Smith, S Rodgers, K

Little, C Burkhardt, D Ghosh, P

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Publication Type:: Journal Article
Citation:: Histochemistry and Cell Biology, 2000, 114 (2), pp. 137 - 146
Issue Date:: 2000-09-25

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Field	Value	Language
dc.contributor.author	Melrose, J	en_US
dc.contributor.author	Smith, S	en_US
dc.contributor.author	Rodgers, K https://orcid.org/0000-0002-3627-9651	en_US
dc.contributor.author	Little, C	en_US
dc.contributor.author	Burkhardt, D	en_US
dc.contributor.author	Ghosh, P	en_US
dc.date.issued	2000-09-25	en_US
dc.identifier.citation	Histochemistry and Cell Biology, 2000, 114 (2), pp. 137 - 146	en_US
dc.identifier.issn	0948-6143	en_US
dc.identifier.uri	http://hdl.handle.net/10453/15631
dc.description.abstract	A polyclonal anti-bovine pancreatic trypsin inhibitor (BPTI) IgY was raised in chickens immunised with aprotinin. The anti-BPTI IgY was subsequently isolated from egg yolks and purified to homogeneity by affinity chromatography on immobilised aprotinin and by Superose 6 size exclusion fast protein liquid chromatography (FPLC). Immunoblotting with the chicken IgY demonstrated its specificity for BPTI; 3.9 ng BPTI could be detected by this technique. There was no crossreactivity against α1-proteinase inhibitor (human and sheep), inter-α-trypsin inhibitor (human and sheep), secretory leucocyte proteinase inhibitor or a range of serine proteinase inhibitory proteins (SPIs) isolated from plant sources (soybean and lima bean trypsin inhibitor, potato trypsin and chymotrypsin inhibitors) or serum SPIs (antithrombin-III, α2-macroglobulin). Immunoblotting using the anti-BPTI IgY identified the 6- to 12- and 58-kDa forms of endogenous ovine cartilage SPIs in cartilage extracts, confirming the interrelationship of the ovine cartilage SPIs with BPTI. BPTI-domain SPIs were immunolocalised within mast cells of ovine and bovine duodenum, lung and pancreas, and in ovine and bovine bronchial cartilage chondrocytes, chondrocytes of the superficial and intermediate zones of articular cartilage and in the fibrochondrocytes/chondrocytes of the nucleus pulposus and annulus fibrosus of the ovine intervertebral disc.	en_US
dc.relation.ispartof	Histochemistry and Cell Biology	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Aprotinin	en_US
dc.subject.mesh	Cattle	en_US
dc.subject.mesh	Chondrocytes	en_US
dc.subject.mesh	Connective Tissue	en_US
dc.subject.mesh	Immunoblotting	en_US
dc.subject.mesh	Intervertebral Disc	en_US
dc.subject.mesh	Mast Cells	en_US
dc.subject.mesh	Serine Proteinase Inhibitors	en_US
dc.subject.mesh	Sheep	en_US
dc.subject.mesh	Trypsin Inhibitors	en_US
dc.title	Immunolocalisation of BPTI-like serine proteinase inhibitory proteins in mast cells, chondrocytes and intervertebral disc fibrochondrocytes of ovine and bovine connective tissues. An immunohistochemical and biochemical study	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.citation.volume	114	en_US
utslib.for	1199 Other Medical and Health Sciences	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	1101 Medical Biochemistry and Metabolomics	en_US
utslib.for	1116 Medical Physiology	en_US
dc.location.activity	ISI:000089211900006	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	closed_access
pubs.issue	2	en_US
pubs.publication-status	Published	en_US
pubs.volume	114	en_US

Abstract:

A polyclonal anti-bovine pancreatic trypsin inhibitor (BPTI) IgY was raised in chickens immunised with aprotinin. The anti-BPTI IgY was subsequently isolated from egg yolks and purified to homogeneity by affinity chromatography on immobilised aprotinin and by Superose 6 size exclusion fast protein liquid chromatography (FPLC). Immunoblotting with the chicken IgY demonstrated its specificity for BPTI; 3.9 ng BPTI could be detected by this technique. There was no crossreactivity against α1-proteinase inhibitor (human and sheep), inter-α-trypsin inhibitor (human and sheep), secretory leucocyte proteinase inhibitor or a range of serine proteinase inhibitory proteins (SPIs) isolated from plant sources (soybean and lima bean trypsin inhibitor, potato trypsin and chymotrypsin inhibitors) or serum SPIs (antithrombin-III, α2-macroglobulin). Immunoblotting using the anti-BPTI IgY identified the 6- to 12- and 58-kDa forms of endogenous ovine cartilage SPIs in cartilage extracts, confirming the interrelationship of the ovine cartilage SPIs with BPTI. BPTI-domain SPIs were immunolocalised within mast cells of ovine and bovine duodenum, lung and pancreas, and in ovine and bovine bronchial cartilage chondrocytes, chondrocytes of the superficial and intermediate zones of articular cartilage and in the fibrochondrocytes/chondrocytes of the nucleus pulposus and annulus fibrosus of the ovine intervertebral disc.

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http://hdl.handle.net/10453/15631