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https://hdl.handle.net/2440/92947
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Type: | Journal article |
Title: | Isolation and characterization of ovine IGFBP-4: protein purification and cDNA sequence |
Author: | CARR, J.M. GRANT, P.A. FRANCIS, G.L. OWENS, J.A. WALLACE, J.C. WALTON, P.E. |
Citation: | Journal of Molecular Endocrinology, 1994; 13(2):219-236 |
Publisher: | BioScientifica |
Issue Date: | 1994 |
ISSN: | 1479-6813 1479-6813 |
Statement of Responsibility: | J M Carr, P A Grant, G L Francis, J A Owens, J C Wallace and P E Walton |
Abstract: | Three different molecular mass forms of IGF-binding proteins (IGFBPs) were purified from ovine plasma by IGF-I affinity chromatography and reverse-phase HPLC: a 46 kDa doublet and 29 kDa and 24 kDa forms. Amino-terminal sequence analysis confirmed that these proteins were ovine (o)IGFBP-3 (46 kDa) and two molecular size variants of oIGFBP-4. oIGFBP-3 and the 29 kDa form of oIGFBP-4 were shown to be N-glycosylated. Isoelectric points were determined to be at approximately pH 6 for oIGFBP-3 and at pH 7 and pH 7.5 for the 29 and 24 kDa forms of oIGFBP-4 respectively. The two different molecular mass variants of oIGFBP-4 had similar IGF-binding properties. Compared with human IGFBP-3 and oIGFBP-3, the two variants of oIGFBP-4 exhibited lower relative binding to amino-terminally modified IGF-I analogues in a competitive IGF-binding assay. The full protein sequence of oIGFBP-4, as deduced from the cDNA sequence, showed a high degree of identity with rat (90%), human (96%) and bovine (98%) IGFBP-4. The cDNA sequence also showed homology over regions of the 3' non-coding sequence, particularly in comparison with bovine IGFBP-4 (96%). Northern analysis of mRNA for oIGFBP-4 indicated a 2.6 kb major transcript and two minor transcripts of approximately 2.1 and 1.8 kb. oIGFBP-4 mRNA transcripts were detected in adult ewe liver > kidney > lung >> heart and also in several fetal tissues, thus suggesting tissue-specific and developmental regulation. The availability of purified oIGFBP-4 and oIGFBP-3 as well as DNA probes for oIGFBP-4 will enable further study of the properties and functions of these proteins, as well as the establishment of specific assays for these IGFBPs. |
Keywords: | Animals Cattle Sheep Humans Rats Somatomedins Insulin-Like Growth Factor Binding Proteins Insulin-Like Growth Factor Binding Protein 4 Cloning, Molecular Base Sequence Sequence Homology, Amino Acid Glycosylation Species Specificity Amino Acid Sequence Molecular Sequence Data DNA, Complementary Carrier Proteins Molecular Weight RNA, Messenger |
Rights: | ©1994 Journal of Endocrinology |
DOI: | 10.1677/jme.0.0130219 |
Published version: | http://dx.doi.org/10.1677/jme.0.0130219 |
Appears in Collections: | Aurora harvest 7 Paediatrics publications |
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