Interaction of human platelets with laminin and identification of the 67 kDa laminin receptor on platelets

Tandon, Narendra N.; Holland, Errol Anthony; Kralisz, Urszula; Kleinman, Hynda K.; Robey, Frank A.; Jamieson, G.A.

doi:10.1042/bj2740535

Cited by 83 publications

(84 citation statements)

References 38 publications

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“…Sequence comparison revealed that the two independently identified glycoproteins are the same. FAT/ CD36 has been shown also to be involved in foam cell formation in early atherosclerosis (6,7), in apoptosis (8), and in angiogenesis (9) by recognizing a variety of ligands such as longchain fatty acid (10), anionic phospholipids (11), apoptotic cells (7), thrombospondin (12), and collagen (13).…”

Section: Fatmentioning

confidence: 99%

Dual Promoter Structure of Mouse and Human Fatty Acid Translocase/CD36 Genes and Unique Transcriptional Activation by Peroxisome Proliferator-activated Receptor α and γ Ligands

Sato

Kuriki

Fukui

et al. 2002

Journal of Biological Chemistry

144

128

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Section: Fatmentioning

confidence: 99%

Dual Promoter Structure of Mouse and Human Fatty Acid Translocase/CD36 Genes and Unique Transcriptional Activation by Peroxisome Proliferator-activated Receptor α and γ Ligands

Sato

Kuriki

Fukui

et al. 2002

Journal of Biological Chemistry

144

128

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“…Collagen-induced platelet responses can be induced by multiple collagen receptors, including glycoprotein VI (GPVI)/Fc receptor ␥ (FcR␥) complex, integrin ␣ 2 ␤ 1 , glycoprotein IV, etc. (2,3). GPVI/FcR␥ signals via the immunoreceptor tyrosine-based activation motif (ITAM)-Syk signaling pathway, and GPVI signaling can be stimulated by GPVI-selective agonists, collagen-related peptide (CRP), and convulxin (4 -6).…”

mentioning

confidence: 99%

An Important Role of the Src Family Kinase Lyn in Stimulating Platelet Granule Secretion

Zhang

Liu

et al. 2010

Journal of Biological Chemistry

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The Src family kinases (SFKs) have been proposed to play stimulatory and inhibitory roles in platelet activation. The mechanisms for these apparently contradictory roles are unclear. Here we show that SFK, mainly Lyn, is important in stimulating a common signaling pathway leading to secretion of platelet granules. Lyn knock-out or an isoform-nonselective SFK inhibitor, PP2, inhibited platelet secretion of both dense and ␣ granules and the secretion-dependent platelet aggregation induced by thrombin, collagen, and thromboxane A 2 . The inhibitory effect of Lyn knock-out on platelet aggregation was reversed by supplementing granule content ADP, indicating that the primary role of Lyn is to stimulate granule secretion. Inhibitory effect of PP2 on platelet aggregation induced by thrombin and thromboxane A 2 were also reversed by supplementing ADP. Furthermore, PP2 treatment or Lyn knock-out diminished agonist-induced Akt activation and cyclic GMP production. The inhibitory effect of PP2 or Lyn knock-out on platelet response can be corrected by supplementing cyclic GMP. These data indicate that Lyn stimulates platelet secretion by activating the phosphoinositide 3-kinase-Akt-nitric oxide (NO)-cyclic GMP pathway and also provide an explanation why Lyn can both stimulate and inhibit platelet activation.

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“…The role of additional collagen receptors (e.g. GPIV and P65) remains to be elucidated (5,6). On the other hand, thrombin activation of PAR1, but not PAR4, is involved with the formation of the signaling pathway necessary for exposure of negatively charged molecules that increase platelet pro-coagulant activity (7,8); in addition, GPIb and GPV seem to be a positive and a negative modulator of thrombin-induced platelet aggregation, respectively, by a mechanism not fully understood (9).…”

mentioning

confidence: 99%

Purification, Cloning, Expression, and Mechanism of Action of a Novel Platelet Aggregation Inhibitor from the Salivary Gland of the Blood-sucking Bug, Rhodnius prolixus

Francischetti

Ribeiro

Champagne

et al. 2000

Journal of Biological Chemistry

109

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Rhodnius prolixus aggregation inhibitor 1 (RPAI-1), a 19-kDa protein isolated from the salivary gland of R. prolixus, was purified by strong cation exchange and reverse-phase high performance liquid chromatographies. Based on 49 amino-terminal amino acid sequences of RPAI-1, primers were produced to generate probes to screen an R. prolixus salivary gland cDNA library. A phage containing the full-length clone of RPAI-1 codes for a mature protein of 155 amino acids. RPAI-1 shows sequence homology to triabin and pallidipin, lipocalins from Triatoma pallidipennis. The cDNA sequence was cloned in Pet17B Escherichia coli expression vector, producing an active peptide. RPAI-1 inhibits human platelet-rich plasma aggregation triggered by low concentrations of ADP, collagen, arachidonic acid, thromboxane A 2 mimetics (U46619), and very low doses of thrombin and convulxin. Here we show that ADP is the target of RPAI-1 since (i) RPAI-1 inhibits ADP-dependent large aggregation formation and secretion triggered by U46619, without affecting Ca 2؉ increase and shape change; (ii) ADP restored the inhibition of U46619-induced platelet aggregation by RPAI-1, (iii) PGE 1 -induced increase of cAMP (which is antagonized by U46619 in an ADP-dependent manner) was restored by RPAI-1, (iv) RPAI-1 inhibits low concentrations of ADP-mediated responses of indomethacintreated platelets, and (v) RPAI-1 binds to ADP, as assessed by large zone chromatography. RPAI-1 affects neither integrin ␣ 2 ␤ 1 -nor glycoprotein VI-mediated platelet responses. We conclude that RPAI-1 is the first lipocalin described that inhibits platelet aggregation by a novel mechanism, binding to ADP.Normal hemostasis is initiated when platelets are exposed to subendothelial matrix, where they adhere to collagen via specific cell-surface receptors. This adhesion step is followed by platelet activation that is accompanied by synthesis and release of pro-aggregatory molecules such as TXA 2 1 and ADP, which amplify platelet responses to collagen and recruit additional platelets to the site of injury, respectively (1). The concerted action of collagen, ADP, and TXA 2 activates specific signaling pathways, generating a number of second messengers and leading to the functional expression of integrin ␣ IIb ␤ 3 , the fibrinogen receptor on platelets (1). Binding of fibrinogen to platelets mediates platelet aggregation, the final common response of activated platelets to most agonists. In addition to platelet aggregation, normal hemostasis involves activation of the blood coagulation cascade and vasoconstriction, making it a very redundant system (2). Redundancy is also observed in terms of the receptors involved in platelet responses for each specific agonist. It has now become clear that physiologic platelet agonists stimulate platelets by more than one receptor, and specific platelet responses involve distinct receptors. Accordingly, it has been shown that integrin ␣ 2 ␤ 1 receptor mediates platelet adhesion to collagen, whereas GPVI induces most of the signal involved in plat...

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Interaction of human platelets with laminin and identification of the 67 kDa laminin receptor on platelets

Cited by 83 publications

References 38 publications

Dual Promoter Structure of Mouse and Human Fatty Acid Translocase/CD36 Genes and Unique Transcriptional Activation by Peroxisome Proliferator-activated Receptor α and γ Ligands

Dual Promoter Structure of Mouse and Human Fatty Acid Translocase/CD36 Genes and Unique Transcriptional Activation by Peroxisome Proliferator-activated Receptor α and γ Ligands

An Important Role of the Src Family Kinase Lyn in Stimulating Platelet Granule Secretion

Purification, Cloning, Expression, and Mechanism of Action of a Novel Platelet Aggregation Inhibitor from the Salivary Gland of the Blood-sucking Bug, Rhodnius prolixus

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