Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Query: EC:3.4.21.7 (
plasmin
)
9,023
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Positive affinity chromatography on heparin-Sepharose has proved a most crucial step in the purification of
pregnancy-associated plasma protein A
(
PAPP-A
). In this chromatographic procedure,
PAPP-A
was purified almost 500-fold from term pregnancy serum. Further purification was achieved by gel filtration and negative immunoaffinity chromatography. Both
PAPP-A
and free heparin inhibited granulocyte elastase (HGE) activity. Whereas free heparin inhibited only in hypotonic buffers,
PAPP-A
inhibited HGE in hypertonic buffers also. However,
PAPP-A
did not inhibit other proteases (trypsin, chymotrypsin,
plasmin
, fibroblast collagenase) or proteolytic cascades (complement activation). Since heparin was not detected in the purified
PAPP-A
, the inhibition of HGE was not due to desorbed or leeched heparin ligand.
...
PMID:Pregnancy-associated plasma protein A interaction with heparin: a critical appraisal. 172 Oct 35
A number of proteins previously thought to be specific for the placenta or pregnancy have been identified in the fluids bathing both the oocyte and the sperm. In many cases their concentrations in follicular fluid and seminal plasma greatly exceeded those in the serum of nonpregnant women or men, and sometimes they even exceeded the levels in pregnancy sera. We report here the occurrence of PP5, PP12, PP14 and
PAPP-A
in follicular fluid and seminal plasma. In follicular fluid, the levels of PP5, PP12, and
PAPP-A
correlate with the estrogen concentration of the same fluid, and the PP12 and
PAPP-A
levels also bear a positive correlation to the progesterone concentration. The levels of PP12 and
PAPP-A
increase as the follicle grows, as do the levels of many steroid hormones. Therefore, the apparent correlations observed may be merely coincidental. However, circumstantial evidence from other reproductive organs indicates that the synthesis of PP12 and
PAPP-A
is stimulated by progesterone. Results of immunohistochemical staining show that PP12 and
PAPP-A
are localized in the luteinized granulosa cells and the corpus luteum. Previous studies indicate that PP5 and
PAPP-A
inhibit the action of proteolytic enzymes
plasmin
and elastase, which are believed to be involved in the mechanisms of ovulation. The study of the significance of these various placental proteins for human reproduction is only at its beginning. Clearly, elucidation of their function is the key to a more fundamental understanding of their role in the events governing ovulation and implantation.
...
PMID:Pregnancy proteins in seminal plasma, seminal vesicles, preovulatory follicular fluid, and ovary. 389 67
Human
pregnancy-associated plasma protein A
(
PAPP-A
) inhibited significantly the proteolytic activity of bovine trypsin and human
plasmin
. Trypsin or
plasmin
treatment of
PAPP-A
resulted in the generation of a major 85 kDa component and the rapid cleavage of internal thiol esters. The results indicated that both of these serine proteinases bound in a 1:1 stoichiometry to
PAPP-A
. The
PAPP-A
-bound enzymes were found to be enzymatically active towards small synthetic substrates and inaccessible to inactivation by soybean trypsin inhibitor and alpha 1-proteinase inhibitor. The mechanism of proteinase inhibition was likely to be entrapment, as described for alpha 2-macroglobulin.
...
PMID:Interaction of human pregnancy-associated plasma protein-A with serine proteinases. 758 86
A study was made of the influence of
plasmin
(PL) complexes with alpha 2-macroglobulin (MG) and alpha 2-antiplasmin on secretion of MG, pregnancy-associated alpha 2-glycoprotein (PAG), and
pregnancy-associated plasma protein A
(
PAPP-A
) by mononuclear cells (MC), obtained from human peripheral blood. It has been shown that incubation of the MG-PL complexes with MC resulted in the increase in concentrations of all these macroglobulins (MG, PAG, and
PAPP-A
) in supernatants of cultured MC. We revealed the same effects of AP-PL with regard to the secretion of PZP and
PAPP-A
. However, this complex was found to suppress MG production by cultured MC. The effects found were dose dependent and some of them differed greatly in men and women, resp.
...
PMID:[The effect of plasmin-modified proteinase inhibitors on macroglobulin production by human blood mononuclear cells in culture]. 765 33
Hepatocyte receptors have been found for such complexes as alpha 2-macroglobulin-
plasmin
,
pregnancy-associated plasma protein A
-
plasmin
, and pregnancy-associated alpha 2-glycoprotein-
plasmin
, molecular masses of these receptors being estimated. The proteinaceous component of hepatocyte membranes contains heavy chains of
plasmin
and a 50 kDa fragment of
plasmin
molecule. These chains and the fragment are able to bind the native alpha 2-antiplasmin. Using immunoblotting no hepatocyte receptors for native macroglobulins, and alpha 2-antiplasmin-
plasmin
, alpha 1-proteinase inhibitor were detected.
...
PMID:[Hepatocyte receptors for proteinase inhibitor complexes with plasmin]. 768 97
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 beta 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 alpha1-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.
...
PMID:Activity of ulilysin, an archaeal PAPP-A-related gelatinase and IGFBP protease. 1797 18
