Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor

1990 ◽  
Vol 262 (1) ◽  
pp. 143-148 ◽  
Author(s):  
H. P. Els�sser ◽  
D. Puplat ◽  
G. Adler ◽  
H. F. Kern
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Secretory Process ◽  
Low Molecular Weight ◽  
Stimulation Of

Stimulation of pancreatic secretory process in the rat by low-molecular weight proteinase inhibitor

1987 ◽  
Vol 247 (1) ◽  
pp. 187-193 ◽  
Author(s):  
U. Rausch ◽  
G. Adler ◽  
H. Weidenbach ◽  
F. Weidenbach ◽  
D. Rudolff ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Secretory Process ◽  
Low Molecular Weight ◽  
Stimulation Of

Low-molecular-weight proteinase inhibitor of human epidermis inhibiting papain and trypsin activity

1986 ◽  
Vol 278 (3) ◽  
pp. 194-198 ◽  
Author(s):  
I. Takiuchi ◽  
H. Takagi ◽  
H. Goi ◽  
M. Kawamura ◽  
D. Higuchi
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Human Epidermis ◽  
Low Molecular Weight ◽  
Trypsin Activity

scholarly journals CD80 Expression Correlates with IL-6 Production in THP-1-Like Macrophages Costimulated with LPS and Dialyzable Leukocyte Extract (Transferon®)

2019 ◽  
Vol 2019 ◽  
pp. 1-9 ◽  
Author(s):  
Alexis P. Jiménez-Uribe ◽  
Hugo Valencia-Martínez ◽  
Gregorio Carballo-Uicab ◽  
Luis Vallejo-Castillo ◽  
Emilio Medina-Rivero ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Flow Cytometry ◽  
Viral Infections ◽  
Surface Expression ◽  
Low Molecular Weight ◽  
Activated Macrophages ◽  
Therapeutic Properties ◽  
And Function ◽  
Complex Drug ◽  
Stimulation Of

Transferon® is a complex drug based on a mixture of low molecular weight peptides. This biotherapeutic is employed as a coadjuvant in clinical trials of several diseases, including viral infections and allergies. Given that macrophages play key roles in pathogen recognition, phagocytosis, processing, and antigen presentation, we evaluated the effect of Transferon® on phenotype and function of macrophage-like cells derived from THP-1 monocytes. We determined the surface expression of CD80 and CD86 by flow cytometry and IL-1β, TNF-α, and IL-6 levels by ELISA. Transferon® alone did not alter the steady state of PMA-differentiated macrophage-like THP-1 cells. On the contrary, simultaneous stimulation of cells with Transferon® and LPS elicited a significant increase in CD80 (P≤0.001) and CD86 (P≤0.001) expression, as well as in IL-6 production (P≤0.05) compared to the LPS control. CD80 expression and IL-6 production exhibited a positive correlation (r=0.6, P≤0.05) in cells exposed to Transferon® and LPS. Our results suggest that the administration of Transferon® induces the expression of costimulatory molecules and the secretion of cytokines in LPS-activated macrophages. Further studies are necessary to determine the implication of these findings in the therapeutic properties of Transferon®.

scholarly journals Characterization of 83-kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin.

1988 ◽  
Vol 106 (6) ◽  
pp. 1973-1983 ◽  
Author(s):  
S Yamashiro-Matsumura ◽  
F Matsumura
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Actin Filaments ◽  
Binding Constant ◽  
Reducing Agents ◽  
Actin Binding ◽  
Low Molecular Weight ◽  
Tropomyosin Isoforms ◽  
Apparent Binding Constant ◽  
Stimulation Of

Nonmuscle caldesmon purified from cultured rat cells shows a molecular weight of 83,000 on SDS gels, Stokes radius of 60.5 A, and sedimentation coefficient (S20,w) of 3.5 in the presence of reducing agents. These values give a native molecular weight of 87,000 and a frictional ratio of 2.04, suggesting that the molecule is a monomeric, asymmetric protein. In the absence of reducing agents, the protein is self-associated, through disulfide bonds, into oligomers with a molecular weight of 230,000 on SDS gels. These S-S oligomers appear to be responsible for the actin-bundling activity of nonmuscle caldesmon in the absence of reducing agents. Actin binding is saturated at a molar ratio of one 83-kD protein to six actins with an apparent binding constant of 5 X 10(6) M-1. Because of 83-kD nonmuscle caldesmon and tropomyosin are colocalized in stress fibers of cultured cells, we have examined effects of 83-kD protein on the actin binding of cultured cell tropomyosin. Of five isoforms of cultured rat cell tropomyosin, tropomyosin isoforms with high molecular weight values (40,000 and 36,500) show higher affinity to actin than do tropomyosin isoforms with low molecular weight values (32,400 and 32,000) (Matsumura, F., and S. Yamashiro-Matsumura. 1986. J. Biol. Chem. 260:13851-13859). At physiological concentration of KCl (100 mM), 83-kD nonmuscle caldesmon stimulates binding of low molecular weight tropomyosins to actin and increases the apparent binding constant (Ka from 4.4 X 10(5) to 1.5 X 10(6) M-1. In contrast, 83-kD protein has slight stimulation of actin binding of high molecular weight tropomyosins because high molecular weight tropomyosins bind to actin strongly in this condition. As the binding of 83-kD protein to actin is regulated by calcium/calmodulin, 83-kD protein regulates the binding of low molecular weight tropomyosins to actin in a calcium/calmodulin-dependent way. Using monoclonal antibodies to visualize nonmuscle caldesmon along microfilaments or actin filaments reconstituted with purified 83-kD protein, we demonstrate that 83-kD nonmuscle caldesmon is localized periodically along microfilaments or actin filaments with similar periodicity (36 +/- 4 nm) as tropomyosin. These results suggest that 83-kD protein plays an important role in the organization of microfilaments, as well as the control of the motility, through the regulation of the binding of tropomyosin to actin.

STIMULATION OF GROWTH OF CONNECTIVE TISSUE BY LOW-MOLECULAR-WEIGHT CONSTITUENTS FROM RAPIDLY GROWING TISSUES

The Lancet ◽  
1977 ◽  
Vol 309 (8024) ◽  
pp. 1225-1228 ◽  
Author(s):  
M.I. Lerman ◽  
N.G. Kucenko ◽  
O.Y. Abakumova ◽  
E.M. Kobrina ◽  
A.B. Schechter ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Connective Tissue ◽  
Low Molecular Weight ◽  
Stimulation Of

Phosphoinositides and Other Glycerophospholipids Interact with Protein C Inhibitor (PCI) and Modify Its Activity towards Activated Protein C (APC).

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 2122-2122
Author(s):  
Felix Wahlmüller ◽  
Margareta Furtmüller ◽  
Barbora Sokolikova ◽  
Bernd R Binder ◽  
Margarethe Geiger
Keyword(s):  
Molecular Weight ◽  
Phosphatidic Acid ◽  
Serine Protease ◽  
Protein C ◽  
Activated Protein C ◽  
Low Molecular Weight ◽  
Native Page ◽  
Stimulatory Activity ◽  
Protein C Inhibitor ◽  
Stimulation Of

Abstract Abstract 2122 Poster Board II-99 Protein C Inhibitor (PCI, SERPINA5, PAI3) is a non-specific, secreted serine protease inhibitor (serpin) which circulates at low levels (5μg/mL or 90nM) in blood plasma (review: Geiger 2007, Suzuki 2008). First described as an inhibitor of activated protein C (APC) an anticoagulant serine protease in human plasma, it has been shown that PCI inactivates a variety of other proteases and has a wide tissue distribution. Some compounds like glycosaminoglycans (e.g. heparin, heparan sulfate) and certain phospholipids can modify PCI activity. Recently it was shown that single-stranded DNA aptamers stimulates the inhibitory activity of PCI towards APC in a glycosaminoglycan-like fashion (Müller 2009). In 2007 Malleier et al. analyzed the interaction of PCI with phosphatidylserine (PS), oxidized PS (OxPS) and oxidized phosphatidylethanolamin (OxPE). PS, OxPS and OxPE bind to PCI and enhance the stimulation of APC-inhibition 130 to 190-fold. In addition, PE supports the internalization of PCI by cells, and internalized PCI promotes phagocytosis of bacteria (Baumgärtner et al. 2007). JFC1 (synaptotagmin-like protein 1) was identified by our group as a new intracellular interaction partner of PCI and colocalization of PCI and CSN6, a subunit of the COP9 signalosome could be observed in lymphocytes. Here, we analyzed the interaction of PCI with phosphatidic acid (PA), phosphatidylglycerol (PG), cardiolipin (CL), phosphoinositides and derived second messengers like inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). To identify lipid-regions which are important for PCI binding we were focusing on differences in fatty acid composition and headgroup phosphorylation. The binding was studied by native PAGE, protein overlay assays (dot blot analysis) or ELISA. The stimulation of PCI activity towards APC was analyzed in functional assays using a low molecular weight substrate (S-2366). IP3 and inositol-1,3,4,5-tetrakisphosphate (IP4) did neither interact with PCI nor stimulate its activity towards APC. PCI bound to saturated, unsaturated and oxidized PA. The oxidized form of 1-palmitoyl-2-arachidonoyl-phosphatidic acid (OxPAPA) exhibited lower binding to PCI, but higher stimulatory activity on APC inhibition, as compared to unoxidized PAPA. Saturated dipalmitoyl-PA did not modulate PCI activity. From all studied lipids 1-palmitoyl-2-arachidonoyl-PG (PAPG) had the strongest stimulatory effect on APC-inhibition similar to 0.1μM low molecular weight heparin. Oxidation of PAPG led to a slight decrease and saturation to a complete loss in stimulatory activity. Also tetra-oleoyl-CL bound to PCI with high affinity and had a similar effect as oxidized PAPG and OxPAPA. All mono- and diphosphorylated phosphoinositides as well as phosphatidylinositol-3,4,5-triphosphate (PI3,4,5P3) bound to PCI as judged from binding assays. A mobility shift of PCI antigen on native PAGE was observed when PCI was incubated with phosphatidylinositol-3,5-diphosphate and phosphatidylinositol-4,5-diphosphate (PI4,5P2). Therefore different phospholipids modulate the activity of PCI, but on the other hand PCI may as well effect lipid signaling. As PI4,5P2 plays an important role as substrate for PI3-kinase we will take a closer look at the effect of PCI on the PI3K/PTEN system and on the activation of AKT (PKB) by PDK1. We will also study the influence of PCI on the generation of IP3 and DAG and its possible role in calcium signaling and protein kinase activation. So far we conclude that phosphoinositides and other glycerophospholipids may function as additional intracellular interaction partners of PCI. Disclosures: No relevant conflicts of interest to declare.

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