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Journal articles on the topic 'Membrane cofactor protein; Glycoproteins'

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Published: 4 June 2021

Last updated: 12 February 2022

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1

Herbert, A., J. O'Leary, M. Krych-Goldberg, J. P. Atkinson, and P. N. Barlow. "Three-dimensional structure and flexibility of proteins of the RCA family — a progress report." Biochemical Society Transactions 30, no. 6 (2002): 990–96. http://dx.doi.org/10.1042/bst0300990.

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Members of the regulator of complement activation (RCA) protein family perform a vital role in health and disease. In this report we describe our efforts to solve the structures of human membrane cofactor protein (CD46), the vaccinia virus complement control protein, which mimics mammalian RCA proteins, and human complement receptor type 1 (CD35). These examples illustrate that, despite good progress over the last decade, the regulators of complement, as extracellular multiple domain glycoproteins, still pose formidable problems to structural biologists. Many important questions remain unanswe

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2

Wu, Eugene, Sunia A. Trauger, Lars Pache, et al. "Membrane Cofactor Protein Is a Receptor for Adenoviruses Associated with Epidemic Keratoconjunctivitis." Journal of Virology 78, no. 8 (2004): 3897–905. http://dx.doi.org/10.1128/jvi.78.8.3897-3905.2004.

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ABSTRACT Subgroup D adenovirus (Ad) types 8, 19, and 37 (Ad8, -19, and -37, respectively) are causative agents of epidemic keratoconjunctivitis and genital tract infections. Previous studies showed that Ad37 binds to a 50-kDa membrane glycoprotein expressed on human ocular (conjunctival) cells. To identify and characterize the role of the 50-kDa glycoprotein in Ad37 infection, we partially purified this molecule from solubilized Chang C conjunctival cell membranes by using lentil lectin chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Liquid chromatogra

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3

Seya, T., J. R. Turner, and J. P. Atkinson. "Purification and characterization of a membrane protein (gp45-70) that is a cofactor for cleavage of C3b and C4b." Journal of Experimental Medicine 163, no. 4 (1986): 837–55. http://dx.doi.org/10.1084/jem.163.4.837.

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Based on preliminary evidence indicating that a cell-associated protein of U937 (a human monocyte-like cell line) possessed cofactor activity and was not the C3b/C4b receptor, we sought to further characterize this protein. A sequential four-column purification procedure was devised that includes C3(H2O) affinity chromatography to isolate in reasonable yields and purity a cell-associated protein of U937 and several other human cell lines. Based on its pattern and Mr on SDS-PAGE, acidic pI, and ligand specificity, it is identical to a recently described C3(H2O) or C3b-binding membrane glycoprot

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4

Kraus, Damian, M. Edward Medof, and Carolyn Mold. "Complementary Recognition of Alternative Pathway Activators by Decay-Accelerating Factor and Factor H." Infection and Immunity 66, no. 2 (1998): 399–405. http://dx.doi.org/10.1128/iai.66.2.399-405.1998.

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ABSTRACT The alternative complement pathway (ACP) functions as a surveillance mechanism by which microorganisms are opsonized with C3b in the absence of specific antibodies. The effectiveness of the ACP relies on its ability to distinguish self from non-self. This recognition function is mediated by C3 regulatory proteins including serum factor H, membrane cofactor protein (MCP), and membrane decay-accelerating factor (DAF). H activity against bound C3b can be increased by host components such as sialic acid and decreased by microbial polysaccharides. DAF and MCP may also recognize cell surfac

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5

Pfueller, Sharron L., Margaret A. Howard, James G. White, Chandrasekhara Menon, and Elizabeth W. Berry. "Shortening of Bleeding Time by 1-Deamino-8-Arginine Vasopressin (DDAVP) in the Absence of Platelet von Willebrand Factor in Gray Platelet Syndrome." Thrombosis and Haemostasis 58, no. 04 (1987): 1060–63. http://dx.doi.org/10.1055/s-0038-1646056.

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SummaryThe Gray platelet syndrome is a rare disorder characterised by the absence of platelet a-granules and their contents. We describe a new patient and the effects of infusions of l-deainino-8-aiginine vasopressin (DDAVP). The patient had a prolonged skin bleeding time and his platelets had reduced numbers of a-granules, increased vacuolation and reduced retention on glass beads. Flatelet von Willebrand factor antigen (vWf:Ag) was undetectable and levels of platelet fibrinogen, p-thioniboglobulin, platelet factor 4 and thrombospondin were reduced. All tests of plasma coagulation factors wer

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6

Zhou, Quansheng, Peter J. Sims, and Therese Wiedmer. "Expression of Proteins Controlling Transbilayer Movement of Plasma Membrane Phospholipids in the B Lymphocytes From a Patient With Scott Syndrome." Blood 92, no. 5 (1998): 1707–12. http://dx.doi.org/10.1182/blood.v92.5.1707.417k15_1707_1712.

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Scott syndrome is a rare inherited bleeding disorder in which platelets and other blood cells fail to promote normal assembly of the membrane-stabilized proteases of the plasma coagulation system. The defect in Scott blood cells is known to reflect inability to mobilize phosphatidylserine from inner plasma membrane leaflet to the cell surface in response to an elevation of Ca2+ at the endofacial surface. To gain insight into the molecular basis of this membrane defect, we examined the expression in Scott cells of plasma membrane proteins that have been implicated to participate in the accelera

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7

Bora, N. S., D. M. Lublin, B. V. Kumar, R. D. Hockett, V. M. Holers, and J. P. Atkinson. "Structural gene for human membrane cofactor protein (MCP) of complement maps to within 100 kb of the 3' end of the C3b/C4b receptor gene." Journal of Experimental Medicine 169, no. 2 (1989): 597–602. http://dx.doi.org/10.1084/jem.169.2.597.

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The structural gene for membrane cofactor protein (MCP), a widely distributed C3b/C4b binding regulatory glycoprotein of the complement system, has been mapped to the same locus as the structural genes for CR1, CR2, DAF, and C4bp. The order of the genes within an approximately 800-kb DNA fragment on the long arm of chromosome 1 is MCP-CR1-CR2-DAF-C4bp. Further, the MCP gene maps to within 100 kb of 3' end of the CR1 gene.

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8

Wijnen, Merel van, Jeanette G. Stam, Cornells van't Veer, et al. "The Interaction of Protein S with the Phospholipid Surface Is Essential for the Activated Protein C-independent Activity of Protein S." Thrombosis and Haemostasis 76, no. 03 (1996): 397–403. http://dx.doi.org/10.1055/s-0038-1650590.

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SummaryProtein S is a vitamin-K dependent glycoprotein involved in the regulation of the anticoagulant activity of activated protein C (APC). Recent data showed a direct anticoagulant role of protein S independent of APC, as demonstrated by the inhibition of prothrombinase and tenase activity both in plasma and in purified systems. This anticoagulant effect of protein S can be explained either by a direct interaction of protein S with one of the components of the complexes and/or by the interference with the binding of these components to phospholipid surfaces.During our investigation we noted

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9

Zhou, Quansheng, Peter J. Sims, and Therese Wiedmer. "Expression of Proteins Controlling Transbilayer Movement of Plasma Membrane Phospholipids in the B Lymphocytes From a Patient With Scott Syndrome." Blood 92, no. 5 (1998): 1707–12. http://dx.doi.org/10.1182/blood.v92.5.1707.

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Abstract Scott syndrome is a rare inherited bleeding disorder in which platelets and other blood cells fail to promote normal assembly of the membrane-stabilized proteases of the plasma coagulation system. The defect in Scott blood cells is known to reflect inability to mobilize phosphatidylserine from inner plasma membrane leaflet to the cell surface in response to an elevation of Ca2+ at the endofacial surface. To gain insight into the molecular basis of this membrane defect, we examined the expression in Scott cells of plasma membrane proteins that have been implicated to participate in the

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10

Post, T. W., M. K. Liszewski, E. M. Adams, I. Tedja, E. A. Miller, and J. P. Atkinson. "Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlate with protein phenotype." Journal of Experimental Medicine 174, no. 1 (1991): 93–102. http://dx.doi.org/10.1084/jem.174.1.93.

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Membrane cofactor protein (MCP) is a complement regulatory protein that is expressed on human cells and cell lines as two relatively broad species with Mr of 58,000-68,000 and 48,000-56,000. The structure of a previously reported cDNA clone indicated that MCP was a type 1 membrane glycoprotein and a member of the regulators of complement activation gene/protein cluster. However, it did not provide an explanation for the unusual phenotypic pattern of MCP. Therefore, in parallel with an analysis of the gene, additional cDNAs were cloned and characterized. Six different MCP cDNA classes were iden

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11

Youn, Soonjeon, Hyelim Cho, Daved H. Fremont, and Michael S. Diamond. "A Short N-Terminal Peptide Motif on Flavivirus Nonstructural Protein NS1 Modulates Cellular Targeting and Immune Recognition." Journal of Virology 84, no. 18 (2010): 9516–32. http://dx.doi.org/10.1128/jvi.00775-10.

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ABSTRACT Flavivirus NS1 is a versatile nonstructural glycoprotein, with intracellular NS1 functioning as an essential cofactor for viral replication and cell surface and secreted NS1 antagonizing complement activation. Even though NS1 has multiple functions that contribute to virulence, the genetic determinants that regulate the spatial distribution of NS1 in cells among different flaviviruses remain uncharacterized. Here, by creating a panel of West Nile virus-dengue virus (WNV-DENV) NS1 chimeras and site-specific mutants, we identified a novel, short peptide motif immediately C-terminal to t

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12

Kunapuli, Satya P., Raul A. DeLa Cadena, and Robert W. Colman. "Bacterial Expression of Biologically Active High Molecular Weight Kininogen Light Chain." Thrombosis and Haemostasis 67, no. 04 (1992): 428–33. http://dx.doi.org/10.1055/s-0038-1648465.

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SummaryHuman high molecular weight kininogen (HK), a single chain plasma glycoprotein, serves as a cofactor in the contact system of blood coagulation. After cleavage by human plasma kallikrein, the nonapeptide bradykinin is released. The HK light chain (LC) contains coagulant activity, which requires both the ability to bind the contact system zymogens, prekallikrein and factor XI, and the ability to interact with negatively charged surfaces. Since bacterial expression might not be successful if carbohydrate was required for activity, we evaluated that possibility by incubating plasma HK with

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13

Freyssinet, J. M., A. Beretz, C. Klein-Soyer, J. Gauchy, S. Schuhler, and J. P. Cazenave. "Interference of blood-coagulation vitamin K-dependent proteins in the activation of human protein C. Involvement of the 4-carboxyglutamic acid domain in two distinct interactions with the thrombin-thrombomodulin complex and with phospholipids." Biochemical Journal 256, no. 2 (1988): 501–7. http://dx.doi.org/10.1042/bj2560501.

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Human protein C is the precursor of a serine proteinase in plasma which contains nine 4-carboxyglutamic acid residues and functions as a potent anticoagulant. It is activated by thrombin in the presence of an essential endothelial-cell-membrane glycoprotein cofactor, thrombomodulin. In a purified human system, vitamin K-dependent proteins such as factor X, prothrombin and prothrombin fragment 1 were able to inhibit protein C activation by the thrombin-thrombomodulin complex, using either detergent-solubilized thrombomodulin or thrombomodulin reconstituted into vesicles consisting of phosphatid

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14

Kumar, Shekhar, Steven Stayrook, James A. Huntington, Rodney M. Camire, and Sriram Krishnaswamy. "High Resolution X-Ray Structure of Snake Venom Factor V: Evolution of a Hemostatic Cofactor to a Toxin Poised to Inflict Maximal Damage to Mammalian Blood Coagulation." Blood 118, no. 21 (2011): 375. http://dx.doi.org/10.1182/blood.v118.21.375.375.

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Abstract Abstract 375 Poisonous snakes frequently harbor activators of mammalian coagulation as part of the toxin repertoire in their venom. The venom of Pseudonaja textilis (Ptex, common brown snake) contains an efficient activator of human prothrombin comprised of a Xa-like protein tightly bound to a Va-like protein. The constituents of this complex exhibit high sequence homology to the corresponding activated coagulation factors in mammalian blood. Factors Xa and Va are produced in blood upon proteolytic activation of their precursors, complex with each other in membrane-dependent reactions

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15

Freyssinet, J. M., J. Gauchy, and J. P. Cazenave. "The effect of phospholipids on the activation of protein C by the human thrombin-thrombomodulin complex." Biochemical Journal 238, no. 1 (1986): 151–57. http://dx.doi.org/10.1042/bj2380151.

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Human thrombomodulin, an endothelial-cell-membrane glycoprotein, has been purified from placenta by Triton X-100 extraction and by affinity chromatography on concanavalin A-Sepharose and thrombin-Sepharose. It has been characterized by its ability to promote the activation of human protein C by human alpha-thrombin in the presence of Ca2+ and fulfilled the requirements of a cofactor. Reconstitution of thrombomodulin into phospholipid vesicles containing anionic phospholipids resulted in an increased rate of activation of protein C. Cardiolipin and vesicles containing phosphatidylcholine/phosph

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16

Edwards, J. G., H. Hameed, and G. Campbell. "Induction of fibroblast spreading by Mn2+: a possible role for unusual binding sites for divalent cations in receptors for proteins containing Arg-Gly-Asp." Journal of Cell Science 89, no. 4 (1988): 507–13. http://dx.doi.org/10.1242/jcs.89.4.507.

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Mn2+ at low (microM) concentrations fulfils the divalent cation requirement for spreading of BHK21 cells on fibronectin. At much higher concentrations, Mn2+ (and to a small extent also Mg2+) induces spreading on haemoglobin, not normally an adhesive protein. Since high Mn2+ also induces spreading of BHK variants unresponsive to exogenous fibronectin, it is unlikely to be acting as a cofactor for secreted cellular fibronectin or by stimulating its secretion. High Ca2+, but not Mg2+, inhibits the induction of spreading by Mn2+ on haemoglobin. Pre-treatment of cells with high concentrations of tr

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17

Beretz, A., J. M. Freyssinet, J. Gauchy, et al. "Stability of the thrombin-thrombomodulin complex on the surface of endothelial cells from human saphenous vein or from the cell line EA.hy 926." Biochemical Journal 259, no. 1 (1989): 35–40. http://dx.doi.org/10.1042/bj2590035.

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Protein C activation by alpha-thrombin on the surface of endothelial cells depends on an essential membrane-glycoprotein cofactor, thrombomodulin. In the present study we have monitored the activity of thrombin-thrombomodulin complexes on human saphenous-vein endothelial cells (HSVEC) or on the endothelial cell line EA.hy 926. Cell monolayers were exposed for 5 min to 8.5 nM human alpha-thrombin and then washed to remove unbound thrombin. The cells were then incubated at 37 degrees C for 5-180 min. At the end of the respective incubation periods, purified human protein C (120 nM) was added in

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18

LIZCANO, José M., Keith F. TIPTON, and Mercedes UNZETA. "Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase (SSAO) from bovine lung." Biochemical Journal 331, no. 1 (1998): 69–78. http://dx.doi.org/10.1042/bj3310069.

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Semicarbazide-sensitive amine oxidase (SSAO) has been purified from bovine lung microsomes in a form which is catalytically active and stable to storage. The enzyme, an integral membrane protein, was solubilized with Triton X-100 and purification was achieved, in the presence of detergent, by chromatography with Cibacron Blue 3GA-agarose, hydroxylapatite, Lens culinaris-agarose, Resource Q-FPLC and gel filtration on Superdex 200 HR-FPLC. This is the first reported procedure for the extensive purification of a membrane-bound SSAO. The purified enzyme had an apparent Mr of 400000 but exhibited m

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19

Brisson, Christine, Gisèle Archipoff, Marie-Louise Hartmann, et al. "Antibodies to Thrombomodulin Induce Receptor-Mediated Endocytosis in Human Saphenous Vein Endothelial Cells." Thrombosis and Haemostasis 68, no. 06 (1992): 737–43. http://dx.doi.org/10.1055/s-0038-1646353.

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SummaryThe membrane glycoprotein thrombomodulin (TM) is an essential endothelial cell (EC) cofactor, which forms a 1:1 stoichiometric complex with thrombin. Binding of thrombin to the high affinity TM receptor transforms its procoagulant activity into an anticoagulant potential, by activating protein C. The fate of TM in the presence of thrombin is still unclear: some authors claim that the thrombin-TM complex is internalized in EC, while others find this complex to be stable for at least 2 h at 37° C on the EC surface. In the present study, we investigated the interactions of thrombin and Fab

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20

Cheng, Heather H., Maria M. Anderson, F. Claire Hankenson, Lily Johnston, Chitra V. Kotwaliwale, and Julie Overbaugh. "Envelope Determinants for Dual-Receptor Specificity in Feline Leukemia Virus Subgroup A and T Variants." Journal of Virology 80, no. 4 (2006): 1619–28. http://dx.doi.org/10.1128/jvi.80.4.1619-1628.2006.

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ABSTRACT Gammaretroviruses, including the subgroups A, B, and C of feline leukemia virus (FeLV), use a multiple-membrane-spanning transport protein as a receptor. In some cases, such as FeLV-T, a nonclassical receptor that includes both a transport protein (Pit1) and a soluble cofactor (FeLIX) is required for entry. To define which regions confer specificity to classical versus nonclassical receptor pathways, we engineered mutations found in either FeLV-A/T or FeLV-T, individually and in combination, into the backbone of the transmissible form of the virus, FeLV-A. The receptor specificities o

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21

Delvaeye, Mieke, Astrid DeVriese, Michael Moons, Naomi Esmon, Charles Esmon, and Edward M. Conway. "Regulation of Complement Activation by Thrombomodulin." Blood 114, no. 22 (2009): 5127. http://dx.doi.org/10.1182/blood.v114.22.5127.5127.

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Abstract Abstract 5127 Thrombomodulin (TM) is an integral membrane glycoprotein, ubiquitously expressed by vascular endothelial cells. Its epidermal growth factor (EGF)-like repeats amplify thrombin-mediated generation of activated protein C and activated thrombin activatable fibrinolysis inhibitor, thereby suppressing coagulation, inflammation and fibrinolysis, and inactivating the anaphylatoxins, C3a and C5a. TM also has direct anti-inflammatory properties, interfering with leukocyte adhesion, and preventing complement activation via its lectin-like domain. We recently established that TM is

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22

Aihara, Morio, Ken Tamura, Ryuko Kawarada, Keizou Okawa, and Yutaka Yoshida. "Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction." Thrombosis and Haemostasis 60, no. 02 (1988): 182–87. http://dx.doi.org/10.1055/s-0038-1647026.

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SummaryThe adhesion of human fixed washed platelets (FWP) to collagen was decreased after treatment with Serratia marcescens protease (SP), which removed 95% of the glycocalicin from platelet membrane glycoprotein (GP) lb. However, the diminished adhesion of SP treated FWP to collagen could still be increased in the presence of purified von Willebrand factor (vWF). This ability of vWF to increase FWP adhesion to collagen is defined as collagen cofactor (CCo). The adhesion of FWP to collagen was not affected by a monoclonal antibody (MAb) to GP Ilb/IIIa (10E5), that inhibits ADP and collagen in

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23

Li, Yi-Heng, Shu-Lin Liu, Guey-Yueh Shi, Guan-Hsiung Tseng, Ping-Yen Liu, and Hua-Lin Wu. "Thrombomodulin plays an important role in arterial remodeling and neointima formation in mouse carotid ligation model." Thrombosis and Haemostasis 95, no. 01 (2006): 128–33. http://dx.doi.org/10.1160/th05-06-0415.

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SummaryThrombomodulin (TM) is a cell membrane-bound glycoprotein that functions as a thrombin cofactor in the activation of protein C. Its protein structure includes a N-terminal lectin-like domain (D1), 6 epidermal growth factor repeats (D2), a serine-threonine-rich region (D3), a transmembrane domain (D4) and a short cytoplasmic tail (D5). Recent studies have demonstrated the direct effect ofTM on cellular proliferation, adhesion and inflammation. In the study, we investigated the role of TM in vascular remodeling and neointima formation in a mouse carotid ligation model. TM expressions on t

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Cheng, Ee-chun, Matthew J. Renda, Lin Wang, and Diane S. Krause. "MKL1 Promotes Megakaryocytic Differentiation Via Stimulation of Serum Response Factor Target Genes." Blood 110, no. 11 (2007): 871. http://dx.doi.org/10.1182/blood.v110.11.871.871.

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Abstract Our studies demonstrate a critical role for MKL1 (megakaryoblastic leukemia 1) in the molecular regulation of megakaryocytopoiesis. MKL1 is part of the fusion protein formed by the t (1; 22) translocation, which is found uniquely in Acute Megakaryoblastic Leukemia (AMKL). The translocation fuses the RBM15 (also known as OTT) gene on chromosome 1 with the MKL1 (also known as MAL) gene on chromosome 22. Previous studies in muscle cells show that MKL1 is a positive cofactor for the transcription factor serum response factor (SRF), and works via the Rho-A pathway to turn on immediate earl

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25

Vlot, André, Stefan Koppelman, Bonno Bouma, and Jan Sixma. "Factor VIII and von Willebrand Factor." Thrombosis and Haemostasis 79, no. 03 (1998): 456–65. http://dx.doi.org/10.1055/s-0037-1614927.

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IntroducationFactor VIII and von Willebrand factor are plasma glycoproteins whose deficiency or structural defects cause hemophilia A and von Willebrand disease, respectively (1). These diseases are the most common inherited bleeding disorders of man. Factor VIII and vWF are synthesized by different cell types and circulate in plasma as a tightly bound complex. Factor VIII is synthesized in the liver (2), and functions as a cofactor for activated factor IX in the intrinsic activation of factor X on a membrane surface (3). vWF is synthesized in endothelial cells (4, 5) and megakaryocytes (6). v

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26

Freyssinet, J. M., M. L. Wiesel, L. Grunebaum, et al. "Activation of human protein C by blood coagulation factor Xa in the presence of anionic phospholipids. Enhancement by sulphated polysaccharides." Biochemical Journal 261, no. 2 (1989): 341–48. http://dx.doi.org/10.1042/bj2610341.

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The activation of protein C by thrombin is thought to occur at the endothelial cell surface in the presence of an essential membrane glycoprotein cofactor, thrombomodulin. In the present study it is demonstrated that, in the presence of hirudin, the most potent known inhibitor of thrombin, human protein C can be activated by human factor Xa (20 nM), but by a thrombomodulin-independent mechanism requiring only the presence of Ca2+ and phospholipid vesicles bearing a high proportion of negative charges (30-75% phosphatidylserine, depending on the conditions). At an optimal concentration of phosp

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27

Stroncek, DF, GM Vercellotti, DE Hammerschmidt, DJ Christie, RA Shankar, and HS Jacob. "Characterization of multiple quinine-dependent antibodies in a patient with episodic hemolytic uremic syndrome and immune agranulocytosis." Blood 80, no. 1 (1992): 241–48. http://dx.doi.org/10.1182/blood.v80.1.241.241.

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Abstract A 23-year-old woman experienced six distinct episodes of severe combined neutropenia and thrombocytopenia. At least one of the episodes was accompanied by hemodialysis-requiring acute renal failure and fragmentation hemolysis (hemolytic uremic syndrome [HUS]). In retrospect, all episodes were probably associated with the ingestion of quinine. Quinine-dependent antibodies to platelets, neutrophils, T lymphocytes, and red blood cells (RBCs) were detected in the patient's serum. By a monoclonal antibody antigen capture assay, the patient's serum contained IgG antibodies, which in the pre

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Stroncek, DF, GM Vercellotti, DE Hammerschmidt, DJ Christie, RA Shankar, and HS Jacob. "Characterization of multiple quinine-dependent antibodies in a patient with episodic hemolytic uremic syndrome and immune agranulocytosis." Blood 80, no. 1 (1992): 241–48. http://dx.doi.org/10.1182/blood.v80.1.241.bloodjournal801241.

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A 23-year-old woman experienced six distinct episodes of severe combined neutropenia and thrombocytopenia. At least one of the episodes was accompanied by hemodialysis-requiring acute renal failure and fragmentation hemolysis (hemolytic uremic syndrome [HUS]). In retrospect, all episodes were probably associated with the ingestion of quinine. Quinine-dependent antibodies to platelets, neutrophils, T lymphocytes, and red blood cells (RBCs) were detected in the patient's serum. By a monoclonal antibody antigen capture assay, the patient's serum contained IgG antibodies, which in the presence, bu

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29

Seya, T., and J. P. Atkinson. "Functional properties of membrane cofactor protein of complement." Biochemical Journal 264, no. 2 (1989): 581–88. http://dx.doi.org/10.1042/bj2640581.

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Membrane cofactor protein (MCP or gp45-70) of the complement system is a cofactor for factor I-mediated cleavage of fluid-phase C3b and C3b-like C3, which opens the thioester bond. In the present study the activity of MCP was further characterized. Unexpectedly, in the absence of factor I, MCP stabilized the alternative- and, to a lesser extent, the classical-pathway cell-bound C3 convertases and thereby enhanced C3b deposition. Soluble MCP, if added exogenously, hardly functioned as cofactor for the cleavage of erythrocyte-bound C3b to iC3b; i.e. its activity, compared with the cofactor activ

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30

Lenting, Peter J. "Cofactor and Cofactor Mimetics." Blood 134, Supplement_1 (2019): SCI—17—SCI—17. http://dx.doi.org/10.1182/blood-2019-121059.

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Many natural enzymes need the assistance of protein cofactors to catalyze chemical reactions at a physiologically relevant speed and several of the enzymes that make up for the coagulation cascade are no exception in this regard. Notably, activated factors VII, IX and X display relatively poor enzymatic activity towards their respective macromolecular substrates. The reason for their low proteolytic activity originates from a number of structural restrictions. For instance, not all enzymes are capable to efficiently fold their new amino-terminus into the active site pocket, leaving the catalyt

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Lewis, V., S. A. Green, M. Marsh, P. Vihko, A. Helenius, and I. Mellman. "Glycoproteins of the lysosomal membrane." Journal of Cell Biology 100, no. 6 (1985): 1839–47. http://dx.doi.org/10.1083/jcb.100.6.1839.

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Three glycoprotein antigens (120, 100, and 80 kD) were detected by mono- and/or polyclonal antibodies generated by immunization with highly purified rat liver lysosomal membranes. All of the antigens were judged to be integral membrane proteins based on the binding of Triton X-114. By immunofluorescence on normal rat kidney cells, a mouse monoclonal antibody to the 120-kD antigen co-stained with a polyclonal rabbit antibody that detected the 100- and 80-kD antigens as well as with antibodies to acid phosphatase, indicating that these antigens are preferentially localized in lysosomes. Few 120-

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Wang, Guixian, M. Kathryn Liszewski, Andrew C. Chan, and John P. Atkinson. "Membrane Cofactor Protein (MCP; CD46): Isoform-Specific Tyrosine Phosphorylation." Journal of Immunology 164, no. 4 (2000): 1839–46. http://dx.doi.org/10.4049/jimmunol.164.4.1839.

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Nomura, M., A. Tsujimura, K. Shida, M. Matsumoto, Y. Matsuda, and T. Seya. "Genomic analysis of the murine membrane cofactor protein (CD46)." Molecular Immunology 35, no. 6-7 (1998): 402. http://dx.doi.org/10.1016/s0161-5890(98)90818-5.

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Kemper, C., M. Leung, C. B. Stephensen, et al. "Membrane cofactor protein (MCP; CD46) expression in transgenic mice." Clinical & Experimental Immunology 124, no. 2 (2001): 180–89. http://dx.doi.org/10.1046/j.1365-2249.2001.01458.x.

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35

Bruser, Thomas, Takahiro Yano, Daniel C. Brune, and Fevzi Daldal. "Membrane targeting of a folded and cofactor-containing protein." European Journal of Biochemistry 270, no. 6 (2003): 1211–21. http://dx.doi.org/10.1046/j.1432-1033.2003.03481.x.

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36

Kavanagh, David, and Timothy Goodship. "Membrane Cofactor Protein and Factor I: Mutations and Transplantation." Seminars in Thrombosis and Hemostasis 32, no. 2 (2006): 155–59. http://dx.doi.org/10.1055/s-2006-939771.

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Lu, D., M. Kalafatis, KG Mann, and GL Long. "Loss of membrane-dependent factor Va cleavage: a mechanistic interpretation of the pathology of protein CVermont." Blood 84, no. 3 (1994): 687–90. http://dx.doi.org/10.1182/blood.v84.3.687.687.

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Abstract Clinical manifestations of arterial and venous thrombosis in a family with protein C deficiency was associated with two mutations in the light chain of protein C: Glu20-->Ala and Val34-->Met. Further studies showed that the mutation Glu20-->Ala which eliminated a gamma- carboxylation site was exclusively responsible for the anticoagulant defect of activated protein C (APC). Membrane-bound human factor Va is inactivated by APC after two sequential cleavages of the heavy chain at Arg506 and Arg306. Human factor Va inactivation by human recombinant APC (rAPC) and a mutant molecu

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38

Lu, D., M. Kalafatis, KG Mann, and GL Long. "Loss of membrane-dependent factor Va cleavage: a mechanistic interpretation of the pathology of protein CVermont." Blood 84, no. 3 (1994): 687–90. http://dx.doi.org/10.1182/blood.v84.3.687.bloodjournal843687.

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Clinical manifestations of arterial and venous thrombosis in a family with protein C deficiency was associated with two mutations in the light chain of protein C: Glu20-->Ala and Val34-->Met. Further studies showed that the mutation Glu20-->Ala which eliminated a gamma- carboxylation site was exclusively responsible for the anticoagulant defect of activated protein C (APC). Membrane-bound human factor Va is inactivated by APC after two sequential cleavages of the heavy chain at Arg506 and Arg306. Human factor Va inactivation by human recombinant APC (rAPC) and a mutant molecule with a

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39

Maisner, Andrea, Gert Zimmer, M. Kathryn Liszewski, Douglas M. Lublin, John P. Atkinson, and Georg Herrler. "Membrane Cofactor Protein (CD46) Is a Basolateral Protein That Is Not Endocytosed." Journal of Biological Chemistry 272, no. 33 (1997): 20793–99. http://dx.doi.org/10.1074/jbc.272.33.20793.

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40

Chen, J. W., T. L. Murphy, M. C. Willingham, I. Pastan, and J. T. August. "Identification of two lysosomal membrane glycoproteins." Journal of Cell Biology 101, no. 1 (1985): 85–95. http://dx.doi.org/10.1083/jcb.101.1.85.

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Two murine lysosome-associated membrane proteins, LAMP-1 of 105,000-115,000 D and LAMP-2 of 100,000-110,000 D, have been identified by monoclonal antibodies that bind specifically to lysosomal membranes. Both glycoproteins were distinguished as integral membrane components solubilized by detergent solutions but not by various chaotropic agents. The lysosome localization was demonstrated by indirect immunofluorescent staining, co-localization of the antigen to sites of acridine orange uptake, and immunoelectron microscopy. Antibody binding was predominantly located at the limiting lysosomal mem

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Wang, Jue, Usha Pendurthi, and L. Vijaya Mohan Rao. "Alterations in Sphingomyelin Metabolism Influences Tissue Factor Procoagulant Activity and the Release of TF-Positive Microvesicles." Blood 134, Supplement_1 (2019): 1103. http://dx.doi.org/10.1182/blood-2019-125933.

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Tissue factor (TF), an integral membrane glycoprotein, is a cofactor for coagulation factor VIIa (FVIIa) and primary cellular initiator of the coagulation. Upon vascular injury or in disease conditions, blood comes in contact with TF, and the formation of TF-FVIIa complex initiates activation of the coagulation cascade. While TF is critical for the maintenance of hemostasis, aberrant expression of TF activity could lead to thrombotic disorders. Typically, most of TF on cell surfaces exist in a cryptic, coagulant inactive state, and an "activation" step (decryption) is essential for the transfo

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42

Kemper, Claudia, Rebecca C. Riley, Marilyn Leung, and John P. Atkinson. "Characterization of human membrane cofactor protein (MCP, CD46) on spermatozoa." Immunopharmacology 49, no. 1-2 (2000): 66. http://dx.doi.org/10.1016/s0162-3109(00)80190-3.

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43

Seya, Tsukasa, Akiko Hirano, Misako Matsumoto, Midori Nomura, and Shigeharu Ueda. "Human membrane cofactor protein (MCP, CD46): multiple isoforms and functions." International Journal of Biochemistry & Cell Biology 31, no. 11 (1999): 1255–60. http://dx.doi.org/10.1016/s1357-2725(99)00092-8.

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XU, Dong, Shou-jian HUANG, Jin-qun WANG, and Chu-kun WU. "Protective effect of membrane cofactor protein against complement-dependent injury." Acta Pharmacologica Sinica 26, no. 8 (2005): 987–91. http://dx.doi.org/10.1111/j.1745-7254.2005.00147.x.

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Riley, Rebecca C., Claudia Kemper, Marilyn Leung, and John P. Atkinson. "Characterization of human membrane cofactor protein (MCP; CD46) on spermatozoa." Molecular Reproduction and Development 62, no. 4 (2002): 534–46. http://dx.doi.org/10.1002/mrd.10144.

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Seto, Nobuyuki, Shuhei Takemura, Sadanobu Nakanishi, et al. "Demonstration and characterization of CD46, membrane cofactor protein, in stomach." Japanese Journal of Clinical Immunology 19, no. 1 (1996): 81–86. http://dx.doi.org/10.2177/jsci.19.81.

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47

Liszewski, M. Kathryn, and John P. Atkinson. "Membrane cofactor protein (MCP; CD46): deficiency states and pathogen connections." Current Opinion in Immunology 72 (October 2021): 126–34. http://dx.doi.org/10.1016/j.coi.2021.04.005.

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Giannakis, E., D. A. Male, R. J. Ormsby, B. E. Loveland, and D. L. Gordon. "Identification of the streptococcal M-protein binding site on membrane cofactor protein (CD46)." Immunopharmacology 49, no. 1-2 (2000): 66. http://dx.doi.org/10.1016/s0162-3109(00)80188-5.

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Giannakis, Eleni, T. Sakari Jokiranta, Rebecca J. Ormsby, et al. "Identification of the Streptococcal M Protein Binding Site on Membrane Cofactor Protein (CD46)." Journal of Immunology 168, no. 9 (2002): 4585–92. http://dx.doi.org/10.4049/jimmunol.168.9.4585.

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Barry, Orla, and Garret FitzGerald. "Mechanisms of Cellular Activation by Platelet Microparticles." Thrombosis and Haemostasis 82, no. 08 (1999): 794–800. http://dx.doi.org/10.1055/s-0037-1615913.

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IntroductionEukaryotic cells, after activation, shed components of their plasma membranes into the extracellular space.1,2 Such fragments may include cytoplasmic elements and are known colloquially as microparticles (MPs). Monocytes,3 lymphocytes,4 endothelial cells,5 erythrocytes,6 and granulocytes7 have been shown to vesiculate either in vitro or in vivo. MPs from other sources have also been reported to exist in vivo.8,9 In addition, platelets have been found to vesiculate following activation by agonists.10,11 Platelets activated with collagen and/or thrombin, by the Ca2+ ionophore A23187

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