|
1
|
Davì G and Patrono C: Platelet activation
and atherothrombosis. N Eng J Med. 357:2482–2494. 2007. View Article : Google Scholar
|
|
2
|
Nieswandt B and Watson SP:
Platelet-collagen interaction: Is GPVI the central receptor? Blood.
102:449–461. 2003. View Article : Google Scholar : PubMed/NCBI
|
|
3
|
Moroi M and Jung SM: Platelet glycoprotein
VI: Its structure and function. Thromb Res. 114:221–233. 2004.
View Article : Google Scholar : PubMed/NCBI
|
|
4
|
Zheng YM, Liu C, Chen H, Locke D, Ryan JC
and Kahn ML: Expression of the platelet receptor GPVI confers
signaling via the Fc receptor gamma-chain in response to the snake
venom convulxin but not to collagen. J Biol Chem. 276:12999–13006.
2001. View Article : Google Scholar : PubMed/NCBI
|
|
5
|
Berlanga O, Tulasne D, Bori T, Snell DC,
Miura Y, Jung S, Moroi M, Frampton J and Watson SP: The Fc receptor
gamma-chain is necessary and sufficient to initiate signalling
through glycoprotein VI in transfected cells by the snake C-type
lectin, convulxin. Eur J Biochem. 269:2951–2960. 2002. View Article : Google Scholar : PubMed/NCBI
|
|
6
|
Blake RA, Schieven GL and Watson SP:
Collagen stimulates tyrosine phosphorylation of phospholipase
C-gamma 2 but not phospholipase C-gamma 1 in human platelets. FEBS
Lett. 353:212–216. 1994. View Article : Google Scholar : PubMed/NCBI
|
|
7
|
Yanaga F, Poole A, Asselin J, Blake R,
Schieven GL, Clark EA, Law CL and Watson SP: Syk interacts with
tyrosine-phosphorylated proteins in human platelets activated by
collagen and cross-linking of the Fc gamma-IIA receptor. Biochem J.
311:471–478. 1995. View Article : Google Scholar : PubMed/NCBI
|
|
8
|
Shattil SJ and Newman PJ: Integrins:
Dynamic scaffolds for adhesion and signaling in platelets. Blood.
104:1606–1615. 2004. View Article : Google Scholar : PubMed/NCBI
|
|
9
|
Hendrick JP and Hartl FU: Molecular
chaperone functions of heat-shock proteins. Annu Rev Biochem.
62:349–384. 1993. View Article : Google Scholar : PubMed/NCBI
|
|
10
|
Kampinga HH, Hageman J, Vos MJ, Kubota H,
Tanguay RM, Bruford EA, Cheetham ME, Chen B and Hightower LE:
Guidelines for the nomenclature of the human heat shock proteins.
Cell Stress Chaperones. 14:105–111. 2009. View Article : Google Scholar : PubMed/NCBI
|
|
11
|
Kato K, Ito H and Inaguma Y: Expression
and phosphorylation of mammalian small heat shock proteins. Prog
Mol Subcell Biol. 28:129–150. 2002. View Article : Google Scholar : PubMed/NCBI
|
|
12
|
Koteiche HA and McHaourab HS: Mechanism of
chaperone function in small heat-shock proteins.
Phosphorylation-induced activation of two-mode binding in alpha
B-crystallin. J Biol Chem. 278:10361–10367. 2003. View Article : Google Scholar : PubMed/NCBI
|
|
13
|
Acunzo J, Katsogiannou M and Rocchi P:
Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and
HSP22 (HspB8) as regulators of cell death. Int J Biochem Cell Biol.
44:1622–1631. 2012. View Article : Google Scholar : PubMed/NCBI
|
|
14
|
Merendino AM, Paul C, Vignola AM, Costa
MA, Melis M, Chiappara G, Izzo V, Bousquet J and Arrigo AP: Heat
shock protein-27 protects human bronchial epithelial cells against
oxidative stress-mediated apoptosis: Possible implication in
asthma. Cell Stress Chaperones. 7:269–280. 2002. View Article : Google Scholar : PubMed/NCBI
|
|
15
|
Rogalla T, Ehrnsperger M, Preville X,
Kotlyarov A, Lutsch G, Ducasse C, Paul C, Wieshe M, Arrigo AP,
Buchner J and Gaestel M: Regulation of Hsp27 oligomerization,
chaperone function, and protective activity against oxidative
stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem.
274:18947–18956. 1999. View Article : Google Scholar : PubMed/NCBI
|
|
16
|
Saklatvala J, Rawlinson L, Waller RJ,
Sarsfield S, Lee JC, Morton LF, Barnes MJ and Farndale RW: Role for
p38 mitogen-activated protein kinase in platelet aggregation caused
by collagen or a thromboxane analogue. J Biol Chem. 271:6586–6589.
1996. View Article : Google Scholar : PubMed/NCBI
|
|
17
|
Kato H, Adachi S, Doi T,
Matsushima-Nishiwaki R, Minamitani C, Akamatsu S, Enomoto Y, Tokuda
H, Otsuka T, Iwama T, et al: Mechanism of collagen-induced release
of 5-HT, PDGF-AB and sCD40L from human platelets: Role of HSP27
phosphorylation via p44/p42 MAPK. Thromb Res. 126:39–43. 2010.
View Article : Google Scholar : PubMed/NCBI
|
|
18
|
Hardie DG: AMP-activated protein kinase as
a drug target. Annu Rev Pharmacol Toxicol. 47:185–210. 2007.
View Article : Google Scholar : PubMed/NCBI
|
|
19
|
Steinberg GR and Kemp BE: AMPK in Health
and Disease. Physiol Rev. 89:1025–1078. 2009. View Article : Google Scholar : PubMed/NCBI
|
|
20
|
Wong AK, Howie J, Petrie JR and Lang CC:
AMP-activated protein kinase pathway: A potential therapeutic
target in cardiometabolic disease. Clin Sci (Lond). 116:607–620.
2009. View Article : Google Scholar : PubMed/NCBI
|
|
21
|
Zhang BB, Zhou G and Li C: AMPK: An
emerging drug target for diabetes and the metabolic syndrome. Cell
Metab. 9:407–416. 2009. View Article : Google Scholar : PubMed/NCBI
|
|
22
|
Liu Y, Oh SJ, Chang KH, Kim YG and Lee MY:
Antiplatelet effect of AMP-activated protein kinase activator and
its potentiation by the phosphodiesterase inhibitor dipyridamole.
Biochem Pharmacol. 86:914–925. 2013. View Article : Google Scholar : PubMed/NCBI
|
|
23
|
Cool B, Zinker B, Chiou W, Kifle L, Cao N,
Perham M, Dickinson R, Adler A, Gagne G, Iyengar R, et al:
Identification and characterization of a small molecule AMPK
activator that treats key components of type 2 diabetes and the
metabolic syndrome. Cell Metab. 3:403–416. 2006. View Article : Google Scholar : PubMed/NCBI
|
|
24
|
Kato K, Ito H, Hasegawa K, Inaguma Y,
Kozawa O and Asano T: Modulation of the stress-induced synthesis of
hsp27 and alpha B-crystallin by cyclic AMP in C6 rat glioma cells.
J Neurochem. 66:946–950. 1996. View Article : Google Scholar : PubMed/NCBI
|
|
25
|
Laemmli UK: Cleavage of structural
proteins during the assembly of the head of bacteriophage T4.
Nature. 227:680–685. 1970. View
Article : Google Scholar : PubMed/NCBI
|
|
26
|
Fusegawa Y and Handa S: Platelet
aggregation induced by ADP or epinephrine is enhanced in habitual
smokers. Thromb Res. 97:287–295. 2000. View Article : Google Scholar : PubMed/NCBI
|
|
27
|
Heldin CH and Westermark B: Mechanism of
action and in vivo role of platelet-derived growth factor. Physiol
Rev. 79:1283–1316. 1999.PubMed/NCBI
|
|
28
|
Hermann A, Rauch BH, Braun M, Schrör K and
Weber AA: Platelet CD40 ligand (CD40L)-subcellular localization,
regulation of expression, and inhibition by clopidogrel. Platelets.
12:74–82. 2001. View Article : Google Scholar : PubMed/NCBI
|
|
29
|
André P, Nannizi-Alaimo L, Prasad SK and
Phillips DR: Platelet-derived CD40L: The switch-hitting player of
cardiovascular disease. Circulation. 106:896–899. 2002. View Article : Google Scholar : PubMed/NCBI
|
|
30
|
Henn V, Slupsky JR, Gräfe M,
Anagnostopoulos I, Förster R, Müller-Berghaus G and Kroczek RA:
CD40 ligand on activated platelets triggers an inflammatory
reaction of endothelial cells. Nature. 391:591–594. 1998.
View Article : Google Scholar : PubMed/NCBI
|
|
31
|
Heeschen C, Dimmeler S, Hamm CW, van den
Vrand MJ, Boersma E, Zeiher AM and Simoons ML: CAPTURE study
Investigators: Soluble CD40 ligand in acute coronary syndrome. N
Eng J Med. 348:1104–1111. 2003. View Article : Google Scholar
|
|
32
|
Chang CH, Chang YC, Lin JW, Chen ST,
Chuang LM and Lai MS: Cardiovascular risk associated with acarbose
versus metformin as the first-line treatment in patients with type
2 diabetes: A Nationwide Cohort Study. J Clin Endocrinol Metab.
100:1121–1129. 2015. View Article : Google Scholar : PubMed/NCBI
|
|
33
|
Emerging Risk Factors Collaboration.
Sarwar N, Gao P, Seshasai SR, Gobin R, Kaptoge S, Di Angelantonio
E, Ingelsson E, Lawlor DA, Selvin E, et al: Diabetes mellitus,
fasting blood glucose concentration, and risk of vascular disease:
A collaborative meta-analysis of 102 prospective studies. Lancet.
375:2215–2222. 2010. View Article : Google Scholar : PubMed/NCBI
|
|
34
|
Hanai Y, Adachi S, Yasuda I, Takai S,
Matsushima-Nishiwaki R, Kato H, Enomoto Y, Akamatsu S, Sakakibara
S, Ogura S, et al: Collagen-induced p38 MAP kinase activation is a
biomarker of platelet hyper-aggregation in patients with diabetes
mellitus. Life Sci. 85:386–394. 2009. View Article : Google Scholar : PubMed/NCBI
|
