Isolation and characterization of circulating complex between human pregnancy-associated plasma protein-A and proform of eosinophil major basic protein

Oxvig, Claus; Sand, Ole; Kristensen, Torsten Nygaard; Kristensen, Lene Juel; Sottrup‐Jensen, Lars

doi:10.1016/0304-4165(94)90071-x

Cited by 119 publications

(108 citation statements)

References 42 publications

Supporting

Mentioning

107

Contrasting

Order By: Relevance

“…Primary Antibodies-For Western blotting, the following antibodies were used: rabbit polyclonal anti-(human PAPP-A) (35); mouse monoclonal anti-(c-Myc) (9E10, ATCC); goat polyclonal anti-(human STC2) (R&D Systems, AF2830); mouse monoclonal PY99 (Santa Cruz Biotechnology, sc-7020) for detection of phosphotyrosine residues; mouse monoclonal CT-1 (GroPep Bioreagents, MAJ1) for detection of human IGF receptor (IGF1R); mouse monoclonal AC-74 (Sigma, A5316) for detection of ␤-actin, and mouse monoclonal D8-mIgG2a (36) for detection of murine PAPP-A. For use in ELISA and for immunoprecipitation, monoclonal antibodies (STC216, STC220, STC221, STC225, STC239, and STC243) against human STC2 4 were used.…”

Section: Methodsmentioning

confidence: 99%

Stanniocalcin-2 Inhibits Mammalian Growth by Proteolytic Inhibition of the Insulin-like Growth Factor Axis

Jepsen¹,

Kløverpris²,

Mikkelsen³

et al. 2015

Journal of Biological Chemistry

Self Cite

126

125

View full text Add to dashboard Cite

Background:The biological function and biochemical activity of mammalian stanniocalcin-2 are unknown. Results: Stanniocalcin-2 inhibits proteolytic release of insulin-like growth factor (IGF), and its ability to cause growth retardation upon transgenic overexpression in mice depends on its proteinase inhibitory function. Conclusion: Stanniocalcin-2 is a novel component of the IGF axis. Significance: Altered stanniocalcin-2 expression may affect IGF signaling under pathological conditions.

show abstract

Section: Methodsmentioning

confidence: 99%

Stanniocalcin-2 Inhibits Mammalian Growth by Proteolytic Inhibition of the Insulin-like Growth Factor Axis

Jepsen¹,

Kløverpris²,

Mikkelsen³

et al. 2015

Journal of Biological Chemistry

Self Cite

126

125

View full text Add to dashboard Cite

show abstract

“…In pregnancy, the protein is primarily present in circulation as a 500-kDa disulfide-linked 2:2 complex, with two subunits of the 206-residue glycosylated proform of the eosinophil major basic protein that acts as a covalent proteinase inhibitor. Outside pregnancy, PAPP-A circulates as a 400-kDa homodimer (Oxvig et al, 1993Lawrence et al, 1999). PAPP-A is the biochemically most thoroughly studied specific IGFBPP and has been shown to specifically hydrolyse human IGFBP-4 in an IGF-dependent manner.…”

Section: Introductionmentioning

confidence: 99%

Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease

Tallant

García‐Castellanos

Marrero

et al. 2007

BCHM

View full text Add to dashboard Cite

Human growth and development are conditioned by insulin-like growth factors (IGFs), which have also implications in pathology. Most IGF molecules are sequestered by IGF-binding proteins (IGFBPs) so that exertion of IGF activity requires disturbance of these complexes. This is achieved by proteolysis mediated by IGFBP proteases, among which the best characterised is human PAPP-A, the first member of the pappalysin family of metzincins. We have previously identified and studied the only archaeal homologue found to date, Methanosarcina acetivorans ulilysin. This is a proteolytically functional enzyme encompassing a pappalysin catalytic domain and a pro-domain involved in maintenance of latency of the zymogen, proulilysin. Once activated, the protein hydrolyses IGFBP-2 to -6 and insulin chain b in vitro. We report here that ulilysin is also active against several other substrates, viz (azo)casein, azoalbumin, and extracellular matrix components. Ulilysin has gelatinolytic but not collagenolytic activity. Moreover, the proteolysis-resistant skeletal proteins actin and elastin are also cleaved, as is fibrinogen, but not plasmin and a1-antitrypsin from the blood coagulation cascade. Ulilysin develops optimal activity at pH 7.5 and strictly requires peptide bonds preceding an arginine residue, as determined by means of a novel fluorescence resonance energy transfer assay, thus pointing to biotechnological applications as an enzyme complementary to trypsin.These two authors contributed equally to this work. a

show abstract

“…In reducing SDS-PAGE, the PAPP-A subunit has an apparent molecular mass of 200 kDa (7), and its 1547-residue sequence is known from cloned cDNA (8). PAPP-A shows no global homology to any protein, but it contains sequence motifs, including an elongated zinc binding motif (HEXXHXXGXXH) at position 482-492 (8).…”

mentioning

confidence: 99%

Expression of Recombinant Human Pregnancy-associated Plasma Protein-A and Identification of the Proform of Eosinophil Major Basic Protein as Its Physiological Inhibitor

Overgaard¹,

Haaning²,

Boldt³

et al. 2000

Journal of Biological Chemistry

Self Cite

169

160

View full text Add to dashboard Cite

show abstract

Isolation and characterization of circulating complex between human pregnancy-associated plasma protein-A and proform of eosinophil major basic protein

Cited by 119 publications

References 42 publications

Stanniocalcin-2 Inhibits Mammalian Growth by Proteolytic Inhibition of the Insulin-like Growth Factor Axis

Stanniocalcin-2 Inhibits Mammalian Growth by Proteolytic Inhibition of the Insulin-like Growth Factor Axis

Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease

Expression of Recombinant Human Pregnancy-associated Plasma Protein-A and Identification of the Proform of Eosinophil Major Basic Protein as Its Physiological Inhibitor

Contact Info

Product

Resources

About