scholarly journals The Catenin p120ctnInteracts with Kaiso, a Novel BTB/POZ Domain Zinc Finger Transcription Factor

1999 ◽  
Vol 19 (5) ◽  
pp. 3614-3623 ◽  
Author(s):  
Juliet M. Daniel ◽  
Albert B. Reynolds
Keyword(s):  
Transcription Factor ◽  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Mammalian Cells ◽  
Yeast Two Hybrid ◽  
Amino Terminal ◽  
Juxtamembrane Region ◽  
Carboxy Terminal ◽  
Two Hybrid ◽  
E Cadherin

ABSTRACT p120 ctn is an Armadillo repeat domain protein with structural similarity to the cell adhesion cofactors β-catenin and plakoglobin. All three proteins interact directly with the cytoplasmic domain of the transmembrane cell adhesion molecule E-cadherin; β-catenin and plakoglobin bind a carboxy-terminal region in a mutually exclusive manner, while p120 binds the juxtamembrane region. Unlike β-catenin and plakoglobin, p120 does not interact with α-catenin, the tumor suppressor adenomatous polyposis coli (APC), or the transcription factor Lef-1, suggesting that it has unique binding partners and plays a distinct role in the cadherin-catenin complex. Using p120 as bait, we conducted a yeast two-hybrid screen and identified a novel transcription factor which we named Kaiso. Kaiso’s deduced amino acid sequence revealed an amino-terminal BTB/POZ protein-protein interaction domain and three carboxy-terminal zinc fingers of the C2H2 DNA-binding type. Kaiso thus belongs to a rapidly growing family of POZ-ZF transcription factors that include the Drosophila developmental regulators Tramtrak and Bric à brac, and the human oncoproteins BCL-6 and PLZF, which are causally linked to non-Hodgkins’ lymphoma and acute promyelocytic leukemia, respectively. Monoclonal antibodies to Kaiso were generated and used to immunolocalize the protein and confirm the specificity of the p120-Kaiso interaction in mammalian cells. Kaiso specifically coprecipitated with a variety of p120-specific monoclonal antibodies but not with antibodies to α- or β-catenin, E-cadherin, or APC. Like other POZ-ZF proteins, Kaiso localized to the nucleus and was associated with specific nuclear dots. Yeast two-hybrid interaction assays mapped the binding domains to Arm repeats 1 to 7 of p120 and the carboxy-terminal 200 amino acids of Kaiso. In addition, Kaiso homodimerized via its POZ domain but it did not heterodimerize with BCL-6, which heterodimerizes with PLZF. The involvement of POZ-ZF proteins in development and cancer makes Kaiso an interesting candidate for a downstream effector of cadherin and/or p120 signaling.

scholarly journals The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-alpha catenin fusion molecules.

1994 ◽  
Vol 127 (1) ◽  
pp. 235-245 ◽  
Author(s):  
A Nagafuchi ◽  
S Ishihara ◽  
S Tsukita
Keyword(s):  
Cell Adhesion ◽  
Cell Movement ◽  
Negative Regulator ◽  
Beta Catenin ◽  
Amino Terminal ◽  
Cytoplasmic Proteins ◽  
The Difference ◽  
Adhesion Activity ◽  
Carboxy Terminal ◽  
E Cadherin

The carboxyl terminus-truncated cadherin (nonfunctional cadherin) has no cell adhesion activity probably because of its failure to associate with cytoplasmic proteins called alpha and beta catenin. To rescue this nonfunctional cadherin as adhesion molecules, we constructed three cDNAs for fusion proteins between nonfunctional E-cadherin and alpha catenin, nE alpha, nE alpha N, and nE alpha C, where the intact, amino-terminal and carboxy-terminal half of alpha catenin, respectively, were directly linked to the nonfunctional E-cadherin, and introduced them into mouse L cells. The subcellular distribution and cell adhesion activity of nE alpha and nE alpha C molecules was similar to those of intact E-cadherin transfectants: they bound to cytoskeletons, were concentrated at cell-cell adhesion sites and showed strong cell adhesion activity. nE alpha N molecules, which also bound to cytoskeletons, showed very poor cell adhesion activity. Taken together, we conclude that in the formation of the cadherin-catenin complex, the mechanical association of alpha catenin, especially its carboxy-terminal half, with E-cadherin is a key step for the cadherin-mediated cell adhesion. Close comparison revealed that the behavior of nE alpha molecules during cytokinesis was quite different from that of intact E-cadherin, and that the intercellular motility, i.e., the cell movement in a confluent sheet, was significantly suppressed in nE alpha transfectants although it was facilitated in E-cadherin transfectants. Considering that nE alpha was not associated with endogenous beta catenin in transfectants, the difference in the nature of cell adhesion between nE alpha and intact E-cadherin transfectants may be explained by the function of beta catenin. The possible functions of beta catenin are discussed with a special reference to its role as a negative regulator for the cadherin-mediated cell adhesion system.

Functional and Genetic Characterization of the Oligomerization and DNA Binding Properties of the Drosophila Doublesex Proteins

Genetics ◽  
1996 ◽  
Vol 144 (4) ◽  
pp. 1639-1652 ◽  
Author(s):  
Scott E Erdman ◽  
Hui-Ju Chen ◽  
Kenneth C Burtis
Keyword(s):  
Dna Binding ◽  
Critical Role ◽  
Target Sequence ◽  
Yeast Two Hybrid ◽  
Specific Expression ◽  
Amino Terminal ◽  
Normal Differentiation ◽  
Carboxy Terminal ◽  
Two Hybrid

The doublesex (dsx) gene of Drosophila melanogaster encodes both male-specific (DSXM) and female-specific (DSXF) polypeptides, which are required for normal differentiation of numerous sexually dimorphic somatic traits. The DSX polypeptides are transcription factors and have been shown previously to bind through a zinc finger-like domain to specific sites in an enhancer regulating sex-specific expression of yolk protein genes. We have determined the consensus target sequence for this DNA binding domain to be a palindromic sequence NNACTAAGAATGTNNTC composed of two half-sites around a central (A/T) base pair. As predicted by the symmetric nature of this site, we have found that the DSX proteins exist as dimers in vivo and have mapped two independent dimerization domains by the yeast two-hybrid method; one in the non-sex-specific amino-terminal region of the protein and one that includes the partially sex-specific carboxy-terminal domains of both the male and female polypeptides. We have further identified a missense mutation that eliminates dsx function in female flies, and shown that the same mutation prevents dimerization of DSXF in the yeast two-hybrid system, indicating a critical role for dimerization in dsx function in vivo.

scholarly journals The git5 Gβ and git11 Gγ Form an Atypical Gβγ Dimer Acting in the Fission Yeast Glucose/cAMP Pathway

Genetics ◽  
2001 ◽  
Vol 157 (3) ◽  
pp. 1159-1168 ◽  
Author(s):  
Sheila Landry ◽  
Charles S Hoffman
Keyword(s):  
Fission Yeast ◽  
Mammalian Cells ◽  
Glucose Repression ◽  
Coiled Coil ◽  
Carboxy Terminus ◽  
Amino Terminal ◽  
Camp Pathway ◽  
Coiled Coil Domain ◽  
Mutational Activation ◽  
Two Hybrid

AbstractFission yeast adenylate cyclase, like mammalian adenylate cyclases, is regulated by a heterotrimeric G protein. The gpa2 Gα and git5 Gβ are both required for glucose-triggered cAMP signaling. The git5 Gβ is a unique member of the Gβ family in that it lacks an amino-terminal coiled-coil domain shown to be essential for mammalian Gβ folding and interaction with Gγ subunits. Using a git5 bait in a two-hybrid screen, we identified the git11 Gγ gene. Co-immunoprecipitation studies confirm the composition of this Gβγ dimer. Cells deleted for git11 are defective in glucose repression of both fbp1 transcription and sexual development, resembling cells lacking either the gpa2 Gα or the git5 Gβ. Overexpression of the gpa2 Gα partially suppresses loss of either the git5 Gβ or the git11 Gγ, while mutational activation of the Gα fully suppresses loss of either Gβ or Gγ. Deletion of gpa2 (Gα), git5 (Gβ), or git11 (Gγ) confer quantitatively distinct effects on fbp1 repression, indicating that the gpa2 Gα subunit remains partially active in the absence of the Gβγ dimer and that the git5 Gβ subunit remains partially active in the absence of the git11 Gγ subunit. The addition of the CAAX box from the git11 Gγ to the carboxy-terminus of the git5 Gβ partially suppresses the loss of the Gγ. Thus the Gγ in this system is presumably required for localization of the Gβγ dimer but not for folding of the Gβ subunit. In mammalian cells, the essential roles of the Gβ amino-terminal coiled-coil domains and Gγ partners in Gβ folding may therefore reflect a mechanism used by cells that express multiple forms of both Gβ and Gγ subunits to regulate the composition and activity of its G proteins.

scholarly journals Caenorhabditis elegans SMG-2 Selectively Marks mRNAs Containing Premature Translation Termination Codons

2007 ◽  
Vol 27 (16) ◽  
pp. 5630-5638 ◽  
Author(s):  
Lisa Johns ◽  
Andrew Grimson ◽  
Sherry L. Kuchma ◽  
Carrie Loushin Newman ◽  
Philip Anderson
Keyword(s):  
Caenorhabditis Elegans ◽  
Mammalian Cells ◽  
Translation Termination ◽  
Yeast Two Hybrid ◽  
Eukaryotic Mrnas ◽  
Nonsense Mediated Mrna Decay ◽  
Endogenous Genes ◽  
Alternatively Spliced ◽  
Two Hybrid ◽  
Premature Translation Termination

ABSTRACT Eukaryotic mRNAs containing premature translation termination codons (PTCs) are rapidly degraded by a process termed “nonsense-mediated mRNA decay” (NMD). We examined protein-protein and protein-RNA interactions among Caenorhabditis elegans proteins required for NMD. SMG-2, SMG-3, and SMG-4 are orthologs of yeast (Saccharomyces cerevisiae) and mammalian Upf1, Upf2, and Upf3, respectively. A combination of immunoprecipitation and yeast two-hybrid experiments indicated that SMG-2 interacts with SMG-3, SMG-3 interacts with SMG-4, and SMG-2 interacts indirectly with SMG-4 via shared interactions with SMG-3. Such interactions are similar to those observed in yeast and mammalian cells. SMG-2-SMG-3-SMG-4 interactions require neither SMG-2 phosphorylation, which is abolished in smg-1 mutants, nor SMG-2 dephosphorylation, which is reduced or eliminated in smg-5 mutants. SMG-2 preferentially associates with PTC-containing mRNAs. We monitored the association of SMG-2, SMG-3, and SMG-4 with mRNAs of five endogenous genes whose mRNAs are alternatively spliced to either contain or not contain PTCs. SMG-2 associates with both PTC-free and PTC-containing mRNPs, but it strongly and preferentially associates with (“marks”) those containing PTCs. SMG-2 marking of PTC-mRNPs is enhanced by SMG-3 and SMG-4, but SMG-3 and SMG-4 are not detectably associated with the same mRNPs. Neither SMG-2 phosphorylation nor dephosphorylation is required for selective association of SMG-2 with PTC-containing mRNPs, indicating that SMG-2 is phosphorylated only after premature terminations have been discriminated from normal terminations. We discuss these observations with regard to the functions of SMG-2 and its phosphorylation during NMD.

scholarly journals Minus end–directed motor KIFC3 suppresses E-cadherin degradation by recruiting USP47 to adherens junctions

2014 ◽  
Vol 25 (24) ◽  
pp. 3851-3860 ◽  
Author(s):  
Kyoko Sako-Kubota ◽  
Nobutoshi Tanaka ◽  
Shigenori Nagae ◽  
Wenxiang Meng ◽  
Masatoshi Takeichi
Keyword(s):  
Cell Adhesion ◽  
Proteasome Inhibitors ◽  
Adherens Junction ◽  
Ubiquitin Protein Ligase ◽  
Juxtamembrane Region ◽  
Specific Protease ◽  
Ubiquitin Specific Protease ◽  
Epithelial Sheets ◽  
E Cadherin ◽  
Cell Cell

The adherens junction (AJ) plays a crucial role in maintaining cell–cell adhesion in epithelial tissues. Previous studies show that KIFC3, a minus end–directed kinesin motor, moves into AJs via microtubules that grow from clusters of CAMSAP3 (also known as Nezha), a protein that binds microtubule minus ends. The function of junction-associated KIFC3, however, remains to be elucidated. Here we find that KIFC3 binds the ubiquitin-specific protease USP47, a protease that removes ubiquitin chains from substrates and hence inhibits proteasome-mediated proteolysis, and recruits it to AJs. Depletion of KIFC3 or USP47 promotes cleavage of E-cadherin at a juxtamembrane region of the cytoplasmic domain, resulting in the production of a 90-kDa fragment and the internalization of E-cadherin. This cleavage depends on the E3 ubiquitin protein ligase Hakai and is inhibited by proteasome inhibitors. E-cadherin ubiquitination consistently increases after depletion of KIFC3 or USP47. These findings suggest that KIFC3 suppresses the ubiquitination and resultant degradation of E-cadherin by recruiting USP47 to AJs, a process that may be involved in maintaining stable cell–cell adhesion in epithelial sheets.

The Four and a Half LIM Domain Protein 2 (FHL2) Interacts with CALM and Is Highly Expressed in AML with Complex Aberrant Karyotpes.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 4337-4337 ◽  
Author(s):  
Zlatana Pasalic ◽  
Belay Tizazu ◽  
Leticia Archangelo ◽  
Alexandre Krause ◽  
Greif Philipp ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Fusion Protein ◽  
Myeloid Leukemia ◽  
Fusion Gene ◽  
Luciferase Reporter ◽  
Lim Domain ◽  
Yeast Two Hybrid ◽  
Lim Domain Protein ◽  
Domain Protein ◽  
Two Hybrid

Abstract The balanced chromosomal translocation t(10;11)(p13;q14) results in the CALM/AF10 fusion gene. This translocation is found in acute myeloid leukemia (AML), T-cell acute lymphoblastic leukaemia (T-ALL) and malignant lymphoma. The CALM/AF10 fusion gene has recently been shown to cause an aggressive biphenotypic leukemia in a murine bone marrow transplant model. The CALM (Clathrin Assembly Lymphoid Myeloid leukemia gene) gene product is a clathrin assembly protein which plays a role in clathrin mediated endocytosis and trans Golgi network trafficking. AF10 is a putative transcription factor most likely involved in processes related to chromatin organization and has polycomb group gene like properties. To learn more about the function of the CALM/AF10 fusion protein, we searched for protein interaction partners of CALM. In a yeast two hybrid screen the four and a half LIM domain protein FHL2 was identified as putative CALM interacting partner. The CALM FHL2 interaction was confirmed by co-transformation assay in yeast and by GST-pulldown experiments. The FHL2 interaction domain of CALM was mapped to amino acids 294 to 335 of CALM using the yeast two hybrid assay. In co-localization studies with transiently expressed fluorescent protein tagged CALM and FHL2, both proteins showed cytoplasmatic localization. Expression analysis (Affymetrix based) in different AML subtypes showed a significantly higher expression of FHL2 in AML with complex aberrant karyotypes compared to AML with normal karyotypes or balanced chromosomal translocations like the t(8;21), inv(16) or t(15;17). FHL2, which is also known as DRAL (downregulated in rhabdomyosarcoma LIM protein), is a TP53 responsive gene known to interact with numerous proteins in both the nucleus and the cytoplasm and can function as a transcriptional cofactor. Known FHL2 interactors include TP53, BRCA1, PLZF (promyelocytic leukemia zinc finger protein), the proto-oncogene SKI1 and beta-catenin. High expression of FHL2 in breast cancer has recently been shown to be associated with an adverse prognosis. CALM has been shown to shuttle between the nucleus and the cytoplasm because inhibition of CREM-mediated nuclear export by leptomycin B leads to the accumulation of CALM in the nucleus. Reporter gene assays using a GAL4-DNA binding domain CALM fusion protein and a GAL4 responsive luciferase reporter were able to demonstrate a transcriptional activation function of CALM. We are currently investigation the effect of FHL2 co-expression on this aspect of the CALM function. It is thus conceivable that FHL2 is playing an important role in CALM/AF10-mediated leukemogenesis by tethering the CALM/AF10 fusion protein to various nuclear transcription factor complexes.

Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel)

2002 ◽  
Vol 361 (3) ◽  
pp. 443-450 ◽  
Author(s):  
Alesia M. HRUSKA-HAGEMAN ◽  
John A. WEMMIE ◽  
Margaret P. PRICE ◽  
Michael J. WELSH
Keyword(s):  
Ion Channel ◽  
Mammalian Cells ◽  
Hippocampal Neurons ◽  
Sequence Similarity ◽  
Expression System ◽  
Pdz Domain ◽  
Mammalian Brain ◽  
Na Channel ◽  
Yeast Two Hybrid ◽  
Two Hybrid

Neuronal members of the degenerin/epithelial Na+ channel (DEG/ENaC) family of cation channels include the mammalian brain Na+ channel 1 (BNC1), acid-sensing ion channel (ASIC) and dorsal-root acid-sensing ion channel (DRASIC). Their response to acidic pH, their sequence similarity to nematode proteins involved in mechanotransduction and their modulation by neuropeptides suggest that they may function as receptors for a number of different stimuli. Using the yeast two-hybrid assay, we found that the PDZ domain-containing protein PICK1 (protein interacting with C kinase) interacts specifically with the C-termini of BNC1 and ASIC, but not DRASIC or the related αENaC or βENaC. In both the yeast two-hybrid system and mammalian cells, deletion of the BNC1 and ASIC C-termini abolished the interaction with PICK1. Likewise, mutating the PDZ domain in PICK1 abolished its interaction with BNC1 and ASIC. In addition, in a heterologous expression system PICK1 altered the distribution of BNC1 channels; this effect was dependent on the PDZ domain of PICK1 and the C-terminus of BNC1. We found crude synaptosomal fractions of brain to be enriched in ASIC, suggesting a possible synaptic localization. Moreover, in transfected hippocampal neurons ASIC co-localized with PICK1 in a punctate pattern at synapses. These data suggest that PICK1 binds ASIC and BNC1 via its PDZ domain. This interaction may be important for the localization and/or function of these channels in both the central and peripheral nervous systems.

scholarly journals The Rotavirus Enterotoxin NSP4 Directly Interacts with the Caveolar Structural Protein Caveolin-1

2006 ◽  
Vol 80 (6) ◽  
pp. 2842-2854 ◽  
Author(s):  
Rebecca D. Parr ◽  
Stephen M. Storey ◽  
DeAnne M. Mitchell ◽  
Avery L. McIntosh ◽  
Minglong Zhou ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Laser Scanning ◽  
Nonstructural Protein ◽  
Direct Interaction ◽  
Cell Periphery ◽  
Structural Protein ◽  
Yeast Two Hybrid ◽  
Ussing Chambers ◽  
Caveolin 1 ◽  
Two Hybrid

ABSTRACT Rotavirus nonstructural protein 4 (NSP4) is known to function as an intracellular receptor at the endoplasmic reticulum (ER) critical to viral morphogenesis and is the first characterized viral enterotoxin. Exogenously added NSP4 induces diarrhea in rodent pups and stimulates secretory chloride currents across intestinal segments as measured in Ussing chambers. Circular dichroism studies further reveal that intact NSP4 and the enterotoxic peptide (NSP4114-135) that is located within the extended, C-terminal amphipathic helix preferentially interact with caveola-like model membranes. We now show colocalization of NSP4 and caveolin-1 in NSP4-transfected and rotavirus-infected mammalian cells in reticular structures surrounding the nucleus (likely ER), in the cytosol, and at the cell periphery by laser scanning confocal microscopy. A direct interaction between NSP4 residues 112 to 140 and caveolin-1 was determined by the Pro-Quest yeast two-hybrid system with full-length NSP4 and seven overlapping deletion mutants as bait, caveolin-1 as prey, and vice versa. Coimmunoprecipitation of NSP4-caveolin-1 complexes from rotavirus-infected mammalian cells demonstrated that the interaction occurs during viral infection. Finally, binding of caveolin-1 from mammalian cell lysates to Sepharose-bound, NSP4-specific synthetic peptides confirmed the yeast two-hybrid data and further delineated the binding domain to amino acids 114 to 135. We propose that the association of NSP4 and caveolin-1 contributes to NSP4 intracellular trafficking from the ER to the cell surface and speculate that exogenously added NSP4 stimulates signaling molecules located in caveola microdomains.

scholarly journals The Safflower bHLH Transcription Factor CtbHLH41 Negatively Regulates SA-induced Leaf Senescence Through Interaction with CtCP1

2021 ◽  
Author(s):  
Yingqi Hong ◽  
Jianyi Zhang ◽  
Yanxi Lv ◽  
Na Yao ◽  
Xiuming Liu
Keyword(s):  
Transcription Factor ◽  
Salicylic Acid ◽  
Leaf Senescence ◽  
Carthamus Tinctorius ◽  
Bhlh Transcription Factor ◽  
Yeast Two Hybrid ◽  
Hydrolysis Of ◽  
Two Hybrid ◽  
Insight Into ◽  
Hybrid Screening

Abstract BackgroundSalicylic acid (SA) plays an important role in regulating leaf senescence. However, the molecular mechanism of leaf senescence of safflower (Carthamus tinctorius) is still elusive. In this study we found that the bHLH transcription factor (TF) CtbHLH41 in Carthamus tinctorius significantly delayed leaf senescence and inhibited the expression of senescence-related genes.ResultsIn order to explore how CtbHLH41 promotes leaf senescence, we carried out yeast two-hybrid screening. In this study, by exploring the mechanism of CtbHLH41 regulating CtCP1, it was found that CtCP1 promoted the hydrolysis of CtbHLH41 protein, accelerated the transcriptional activities of salicylic acid-mediated senescence-related genes CtSAG12 and CtSAG29, chlorophyll degradation genes CtNYC1 and CtNYE1, and accelerated leaf senescence. We found a negative SA regulator CtANS1, which interacts with CtbHLH41 and regulates its stability, thereby inhibiting CtCP1-mediated leaf senescence.ConclusionsIn short, our results provide a new insight into the mechanism of CtbHLH41 actively regulating the senescence of safflower leaves induced by SA.

Immunologic Identification of the Cleavage Products from the Aα- and Bβ-Chains in the Early Stages of Plasmin Digestion of Fibrinogen

1986 ◽  
Vol 56 (01) ◽  
pp. 100-106 ◽  
Author(s):  
C Y Liu ◽  
Joan H Sobel ◽  
J I Weitz ◽  
Karen L Kaplan ◽  
H L Nossel
Keyword(s):  
Monoclonal Antibodies ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Small Peptides ◽  
Large Molecules ◽  
Amino Terminal ◽  
Specific Radioimmunoassay ◽  
Heterogenous Group ◽  
Reported Data ◽  
Carboxy Terminal

SummaryFragment X components (Mr 225,000 to 333,000) were distinguished on sodium dodecyl sulfate polyacrylamide gels. Western blotting with monoclonal antibodies to Aα-chain segments demonstrated that the Aα-chains of fibrinogen and the largest fragment X components (Mr 285,000-340,000) contained both Aα 259-276 and Aα 540-554. Fragment X components of Mr 270.000-285,000 contained Aα 259-276 but lacked Aα 540-554, whereas the smallest fragment X components (Mr 225.000-270,000) contained neither Aα 540-554 nor Aα 259-276. Studies of the small peptides generated during fragment X formation complemented the studies of the large molecules, by demonstrating peptides containing both Aα 259-276 and Aα 540-554 (Mr 41,600-41,800 and Mr 38,700-38,900), peptides containing Aα 540-554 but not Aα 259-276 (Mr 20,500-21,000 and Mr 17,300-17,500) and peptides containing only Aα 259-276 (Mr 23,600-24,000 and Mr 20,500-21,000). Cleavage of Bβ 1-42 from the amino terminal ends of the Bβ-chains, measured with a specific radioimmunoassay, was linear until 1.6 moles per mole of fibrinogen had been relased, and coincided with loss of the central and carboxy terminal Aα-chain regions, i. e. Aα 259-276 and Aα 540-554. Based on present and previously reported data, a model is proposed for the evolution of the heterogenous group of fragment X derivatives from fibrinogen with the simultaneous release of small peptides. Features of this model include1. asymmetric cleavage of the fibrinogen dimer and2. proteolyses of several different bonds occurring simultaneously but at distinct rates.

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