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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03019naa a2200241 4500 | |
| 001 | oai:DiVA.org:umu-59918 | |
| 003 | SwePub | |
| 008 | 120926s1996 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-599182 URI |
| 040 | a (SwePub)umu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Mikus, P4 aut |
| 245 | 1 0 | a Intracellular polymerization of the serpin plasminogen activator inhibitor type 2. |
| 264 | 1 | c 1996 |
| 338 | a print2 rdacarrier | |
| 520 | a Plasminogen activator inhibitor type 2 (PAI-2) is synthesized in two molecular forms: an intracellular, nonglycosylated form and an extracellular, glycosylated form. The bitopological distribution of PAI-2 is caused by an inefficient internal secretion signal. In addition, the secretion efficiency of PAI-2 seems to differ, depending on the cell type, differentiation state, and culture conditions. In recombinant cell clones designed for the synthesis of the secreted form of PAI-2, the fraction of secreted PAI-2 decreased with increasing expression levels. Subcellular fractionation of cell clones with higher expression levels revealed that PAI-2 accumulating in the cell was mainly associated with the organelles of the secretory pathway. Electrophoresis under nondenaturating conditions revealed that the PAI-2 retained at higher expression levels was mainly polymerized. Polymers of PAI-2 were also detected in cytosolic extracts prepared from human placenta and phorbol ester-stimulated U 937 cells, indicating that intracellular polymerization of PAI-2 may occur in the cytosols of cells that normally express PAI-2 under physiological conditions. When purified PAI-2 or cellular extracts were incubated at 37 degrees C for 24 h most of the PAI-2 protein was found to polymerize. Polymer formation was prevented by the addition of synthetic peptides with sequences corresponding to residues P2 to P14 in the reactive center loop of PAI-2 and antithrombin. These synthetic peptides also caused dissociation of prepolymerized purified PAI-2 and PAI-2 polymers in cellular extracts. Incubation with unrelated peptides of the same size had no effect on polymer formation or dissociation of preformed polymers, indicating that polymerization of PAI-2 occurs by the loop-sheet mechanism. Taken together, our data suggest that the wild-type form of PAI-2, like some natural pathological genetic variants of alpha1-antitrypsin, antithrombin, and C1 inhibitor readily polymerizes intracellularly and that polymerization may lead to a reduced secretion efficiency. | |
| 700 | 1 | a Ny, Toru Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)tony0001 |
| 710 | 2 | a Umeå universitetb Institutionen för medicinsk kemi och biofysik4 org |
| 773 | 0 | t Journal of Biological Chemistryg 271:17, s. 10048-53q 271:17<10048-53x 0021-9258x 1083-351X |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-59918 |
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