scholarly journals GPR56, a novel platelet collagen receptor that loves stress

2021 ◽  
Author(s):  
Ingeborg Hers ◽  
Stuart J. Mundell
Keyword(s):  
Collagen Receptor

scholarly journals Signal-transducing Mechanisms Involved in Activation of the Platelet Collagen Receptor Integrin α2β1

2000 ◽  
Vol 275 (11) ◽  
pp. 8016-8026 ◽  
Author(s):  
Stephanie M. Jung ◽  
Masaaki Moroi
Keyword(s):  
Collagen Receptor

scholarly journals DDR1 Affects Metabolic Reprogramming in Breast Cancer Cells by Cross-Talking to the Insulin/IGF System

Biomolecules ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 926
Author(s):  
Veronica Vella ◽  
Marika Giuliano ◽  
Maria Luisa Nicolosi ◽  
Maria Giovanna Majorana ◽  
Małgorzata Anna Marć ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Breast Cancer Cells ◽  
Cell Metabolism ◽  
Growth Factor Receptor ◽  
Metabolic Reprogramming ◽  
Atp Production ◽  
Igf System ◽  
Putative Target ◽  
Collagen Receptor ◽  
Discoidin Domain Receptor 1

The insulin receptor isoform A (IR-A), a dual receptor for insulin and IGF2, plays a role in breast cancer (BC) progression and metabolic reprogramming. Notably, discoidin domain receptor 1 (DDR1), a collagen receptor often dysregulated in cancer, is involved in a functional crosstalk and feed forward loop with both the IR-A and the insulin like growth factor receptor 1 (IGF1R). Here, we aimed at investigating whether DDR1 might affect BC cell metabolism by modulating the IGF1R and/or the IR. To this aim, we generated MCF7 BC cells engineered to stably overexpress either IGF2 (MCF7/IGF2) or the IR-A (MCF7/IR-A). In both cell models, we observed that DDR1 silencing induced a significant decrease of total ATP production, particularly affecting the rate of mitochondrial ATP production. We also observed the downregulation of key molecules implicated in both glycolysis and oxidative phosphorylation. These metabolic changes were not modulated by DDR1 binding to collagen and occurred in part in the absence of IR/IGF1R phosphorylation. DDR1 silencing was ineffective in MCF7 knocked out for DDR1. Taken together, these results indicate that DDR1, acting in part independently of IR / IGF1R stimulation, might work as a novel regulator of BC metabolism and should be considered as putative target for therapy in BC.

scholarly journals Protein Kinase B Is Regulated in Platelets by the Collagen Receptor Glycoprotein VI

2002 ◽  
Vol 277 (15) ◽  
pp. 12874-12878 ◽  
Author(s):  
Fiona A. Barry ◽  
Jonathan M. Gibbins
Keyword(s):  
Protein Kinase ◽  
Protein Kinase B ◽  
Glycoprotein Vi ◽  
Collagen Receptor

scholarly journals The inhibitory collagen receptor LAIR-1 (CD305)

2008 ◽  
Vol 83 (4) ◽  
pp. 799-803 ◽  
Author(s):  
L. Meyaard
Keyword(s):  
Collagen Receptor

scholarly journals Mice Lacking the Inhibitory Collagen Receptor LAIR-1 Exhibit a Mild Thrombocytosis and Hyperactive Platelets

2017 ◽  
Vol 37 (5) ◽  
pp. 823-835 ◽  
Author(s):  
Christopher W. Smith ◽  
Steven G. Thomas ◽  
Zaher Raslan ◽  
Pushpa Patel ◽  
Maxwell Byrne ◽  
...  
Keyword(s):  
Tyrosine Kinases ◽  
Kinase Activity ◽  
Thrombus Formation ◽  
Physiological Role ◽  
Src Family Kinase ◽  
Glycoprotein Vi ◽  
Collagen Receptor ◽  
Deficient Mice

Objective— Leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1) is a collagen receptor that belongs to the inhibitory immunoreceptor tyrosine-based inhibition motif–containing receptor family. It is an inhibitor of signaling via the immunoreceptor tyrosine-based activation motif–containing collagen receptor complex, glycoprotein VI-FcRγ-chain. It is expressed on hematopoietic cells, including immature megakaryocytes, but is not detectable on platelets. Although the inhibitory function of LAIR-1 has been described in leukocytes, its physiological role in megakaryocytes and in particular in platelet formation has not been explored. In this study, we investigate the role of LAIR-1 in megakaryocyte development and platelet production by generating LAIR-1–deficient mice. Approach and Results— Mice lacking LAIR-1 exhibit a significant increase in platelet counts, a prolonged platelet half-life in vivo, and increased proplatelet formation in vitro. Interestingly, platelets from LAIR-1–deficient mice exhibit an enhanced reactivity to collagen and the glycoprotein VI–specific agonist collagen-related peptide despite not expressing LAIR-1, and mice showed enhanced thrombus formation in the carotid artery after ferric chloride injury. Targeted deletion of LAIR-1 in mice results in an increase in signaling downstream of the glycoprotein VI–FcRγ-chain and integrin αIIbβ3 in megakaryocytes because of enhanced Src family kinase activity. Conclusions— Findings from this study demonstrate that ablation of LAIR-1 in megakaryocytes leads to increased Src family kinase activity and downstream signaling in response to collagen that is transmitted to platelets, rendering them hyper-reactive specifically to agonists that signal through Syk tyrosine kinases, but not to G-protein–coupled receptors.

Inhibition of Cell-Induced Vitreous Contraction by Synthetic Peptide Derived from the Collagen Receptor Binding Sequence

1996 ◽  
Vol 12 (3) ◽  
pp. 353-361
Author(s):  
CHANG-HAO YANG ◽  
TUR-FU HUANG ◽  
KWAN-RONG LIU ◽  
MUH-SHY CHEN ◽  
POR-TYING HUNG
Keyword(s):  
Receptor Binding ◽  
Synthetic Peptide ◽  
Binding Sequence ◽  
Collagen Receptor

scholarly journals Analysis of the Interaction of Platelet Collagen Receptor Glycoprotein VI (GPVI) with Collagen

2002 ◽  
Vol 277 (48) ◽  
pp. 46197-46204 ◽  
Author(s):  
Yoshiki Miura ◽  
Tsuyoshi Takahashi ◽  
Stephanie M. Jung ◽  
Masaaki Moroi
Keyword(s):  
Glycoprotein Vi ◽  
Collagen Receptor

scholarly journals The alpha 2 beta 1 integrin cell surface collagen receptor binds to the alpha 1 (I)-CB3 peptide of collagen.

1990 ◽  
Vol 265 (9) ◽  
pp. 4778-4781 ◽  
Author(s):  
W D Staatz ◽  
J J Walsh ◽  
T Pexton ◽  
S A Santoro
Keyword(s):  
Cell Surface ◽  
Beta 1 Integrin ◽  
Collagen Receptor

Role of Discoidin Domain Receptor 2 in Craniofacial Bone Regeneration

2021 ◽  
pp. 002203452110074
Author(s):  
A. Binrayes ◽  
C. Ge ◽  
F.F. Mohamed ◽  
R.T. Franceschi
Keyword(s):  
Bone Regeneration ◽  
Healing Process ◽  
Congenital Defects ◽  
Calvarial Bone ◽  
Discoidin Domain Receptor ◽  
Skeletal Defects ◽  
Discoidin Domain Receptor 2 ◽  
Collagen Receptor ◽  
Deficient Mice

Bone loss caused by trauma, neoplasia, congenital defects, or periodontal disease is a major cause of disability and human suffering. Skeletal progenitor cell–extracellular matrix interactions are critical for bone regeneration. Discoidin domain receptor 2 (DDR2), an understudied collagen receptor, plays an important role in skeletal development. Ddr2 loss-of-function mutations in humans and mice cause severe craniofacial and skeletal defects, including altered cranial shape, dwarfing, reduced trabecular and cortical bone, alveolar bone/periodontal defects, and altered dentition. However, the role of this collagen receptor in craniofacial regeneration has not been examined. To address this, calvarial subcritical-size defects were generated in wild-type (WT) and Ddr2-deficient mice. The complete bridging seen in WT controls at 4 wk postsurgery was not observed in Ddr2-deficient mice even after 12 wk. Quantitation of defect bone area by micro–computed tomography also revealed a 50% reduction in new bone volume in Ddr2-deficient mice. Ddr2 expression during calvarial bone regeneration was measured using Ddr2-LacZ knock-in mice. Expression was restricted to periosteal surfaces of uninjured calvarial bone and, after injury, was detected in select regions of the defect site by 3 d postsurgery and expanded during the healing process. The impaired bone healing associated with Ddr2 deficiency may be related to reduced osteoprogenitor or osteoblast cell proliferation and differentiation since knockdown/knockout of Ddr2 in a mesenchymal cell line and primary calvarial osteoblast cultures reduced osteoblast differentiation while Ddr2 overexpression was stimulatory. In conclusion, Ddr2 is required for cranial bone regeneration and may be a novel target for therapy.

Initiation of HeLa cell adhesion to collagen is dependent upon collagen receptor upregulation, segregation to the basal plasma membrane, clustering and binding to the cytoskeleton

1992 ◽  
Vol 101 (4) ◽  
pp. 873-883
Author(s):  
M.L. Lu ◽  
R.J. McCarron ◽  
B.S. Jacobson
Keyword(s):  
Plasma Membrane ◽  
Cell Attachment ◽  
Cell Spreading ◽  
Threshold Effect ◽  
Type I ◽  
Receptor Clustering ◽  
Collagen Receptors ◽  
Basal Plasma Membrane ◽  
Basal Plasma ◽  
Collagen Receptor

It was recently reported that HeLa cells have three Arg-Gly-Asp-dependent collagen receptors that do not appear to be in the integrin family of extracellular matrix receptors and bind to either type I or IV collagen or to type I gelatin. It was our goal to determine how these receptors function in HeLa cell-substratum adhesion. We report here that the sequence of events by which the receptors mediate adhesion to collagen or gelatin is: (1) induction of cell attachment by specific collagen receptor-substratum interactions with culture dishes covalently coated with either type I collagen or gelatin - attachment is inhibited by soluble gelatin; (2) stabilization of attachment by exocytotic upregulation of the receptors to the basal plasma membrane, which was demonstrated by analyzing, during cell adhesion, the redistribution of the collagen receptors among the apical plasma membrane exposed to the culture medium, the basal plasma membrane contacting the culture dish, and an intracellular pool of plasma membrane vesicles; (3) the initiation of cell spreading by receptor clustering and cytoskeletal association. Cell spreading is a threshold effect with regard to the surface concentration of gelatin, indicating that collagen receptor clustering is a precondition to the onset of spreading. Observations consistent with this interpretation of the threshold effect are that cells attach but spread more slowly on a substratum that retards receptor clustering, and that collagen receptors, when viewed by immunofluorescence microscopy, form a punctate pattern of fluorescence in the basal plasma membrane during cell spreading. It is also shown that more collagen receptors co-isolate with nondenaturing detergent-stable cytoskeletal preparations after the collagen receptors have been either clustered by antibodies or gelatin in solution, or by a collagen matrix. This indicates that clustering drives the receptors to bind to the cytoskeleton and is a necessary step in the transition from cell attachment to cell spreading.

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