BIOMECHANICS AND FUNCTIONAL REGULATIONS OF CD44-LIGAND INTERACTIONS

Li Linda; Ding Qihan; Chen Shenbao; Lü Shouqin; Long Mian; Guo Xingming

doi:10.6052/0459-1879-20-313

Volume 53 Issue 2

Feb. 2021

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Chinese Journal of Theoretical and Applied Mechanics > 2021 > 53(2): 539-553. > DOI: 10.6052/0459-1879-20-313 CSTR: 32045.14.0459-1879-20-313

Li Linda, Ding Qihan, Chen Shenbao, Lü Shouqin, Long Mian, Guo Xingming. BIOMECHANICS AND FUNCTIONAL REGULATIONS OF CD44-LIGAND INTERACTIONS[J]. Chinese Journal of Theoretical and Applied Mechanics, 2021, 53(2): 539-553. DOI: 10.6052/0459-1879-20-313

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BIOMECHANICS AND FUNCTIONAL REGULATIONS OF CD44-LIGAND INTERACTIONS

Li Linda^*,
Ding Qihan^†,**,
Chen Shenbao^†,**,
Lü Shouqin^{†,**,2), ,},
Long Mian^†,**,
Guo Xingming^*,3), ,

^*Key Laboratory of Biorheology Science and Technology, Ministry of Education, College of Bioengineering, Chongqing University, Chongqing 400044, China
^†Beijing Key Laboratory of Engineered Construction and Mechanobiology, Key Laboratory of Microgravity (National Microgravity Laboratory), Center of Biomechanics and Bioengineering, Institute of Mechanics, Chinese Academy of Sciences, Beijing 100190, China
^**School of Engineering Science, University of Chinese Academy of Sciences, Beijing 101408, China

Received Date: July 30, 2020

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Abstract

Abstract

As a widely expressed cellular adhesion molecule, type I transmembrane glycoprotein CD44 is crucial in cell proliferation, differentiation, migration, angiogenesis and other biological processes to induce intracellular signal transduction and regulate tissue homeostasis. Especially, cell adhesion dynamics mediated by CD44-selectin and CD44-hyaluronic acid (HA) interactions play key roles in classic inflammatory cascade, tumor metastasis, or tissue-specific liver immunity. This review discussed the progresses and remaining issues of CD44 selectin and CD44-HA interactions in various aspects of cellular adhesion dynamics, two- and three-dimensional molecular reaction kinetics, atomic microstructural features, and intracellular signal transduction pathways. Nowadays, the importance of mechanical and physical factors to biological activities has been gradually accepted by scientific community. New concepts such as mechanomedicine, mechanoimmunology and mechanomics have been put forward one after another. Under physiological or pathological conditions, cell adhesion mediated by CD44-ligand interactions are regulated by in vivo mechanical and physical cues such as blood shear or tissue stiffness, but their regulatory mechanisms are still unclear. From that on, future perspectives related to CD44-ligand interaction were also proposed in this review as follows: how mechanical and physical factors regulate cellular adhesion dynamics and intrinsic mechanism mediated by CD44-ligand interactions; what the mechanical regulation features of molecular reaction kinetics of CD44-ligand interactions and corresponding structural bases are; and how the atomic-level microstructures of CD44-ligand binding evolve dynamically under mechanical forces. This review provides clues for further understanding the biological functions and structure-function relationship of CD44-ligand interactions.
- CD44,
- selectin,
- HA,
- cell adhesion,
- mechanical regulation,
- inflammation

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References

[1]	Babasola O, Rees-Milton KJ, Bebe S. et al. Chemically modified N-acylated hyaluronan fragments modulate proinflammatory cytokine production by stimulated human macrophages. Journal of Biological Chemistry, 2014,289(36):24779-24791
[2]	Katoh S, Maeda S, Fukuoka H. et al. A crucial role of sialidase Neu1 in hyaluronan receptor function of CD44 in T helper type 2-mediated airway inflammation of murine acute asthmatic model. Clinical and Experimental Immunology, 2010,161(2):233-241
[3]	Krolikoski M, Monslow J, Puré E. The CD44-HA axis and inflammation in atherosclerosis: A temporal perspective. Matrix Biology, 2019, 78-79:201-218
[4]	Screaton GR, Bell MV, Jackson DG. et al. Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons. Proceedings of the National Academy of Sciences of the United States of America, 1992,89(24):12160-12164
[5]	Ponta H, Sherman L, Herrlich P A. CD44: From adhesion molecules to signalling regulators. Nature Reviews Molecular Cell Biology, 2003,4(1):33-45
[6]	Naor D, Nedvetzki S, Golan I. et al. CD44 in cancer. Critical Reviews in Clinical Laboratory Sciences, 2002,39(6):527-579
[7]	Brown TA, Bouchard T, John TS. et al. Human keratinocytes express a new CD44 core protein (CD44E) as a heparan-sulfate intrinsic membrane proteoglycan with additional exons. Journal of Cell Biology, 1991,113(1):207-221
[8]	Jiang L, Liu G, Liu H. et al. Molecular weight impact on the mechanical forces between hyaluronan and its receptor. Carbohydrate Polymers, 2018,197:326-336
[9]	Murai T, Hokonohara H, Takagi A. et al. Atomic force microscopy imaging of supramolecular organization of hyaluronan and its receptor CD44. IEEE Transactions on Nanobioscience, 2009,8(4):294-299
[10]	Greenfield B, Wang WC, Marquardt H. et al. Characterization of the heparan sulfate and chondroitin sulfate assembly sites in CD44. Journal of Biological Chemistry, 1999,274(4):2511-2517
[11]	Screaton G, Bell M, Bell J, et al. The identification of a new alternative exon with highly restricted tissue expression in transcripts encoding the mouse Pgp-1 (CD44) homing receptor. Comparison of all 10 variable exons between mouse, human, and rat. Journal of Biological Chemistry, 1993,268(17):12235-12238
[12]	Okamoto, I. Kawano, Y. Murakami, D. et al. Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway. Journal of Cell Biology, 2001,155(5):755-762
[13]	Kalnina Z, Zayakin P, Silina K. et al. Alterations of pre-mRNA splicing in cancer. Genes Chromosomes & Cancer, 2005,42(4):342-357
[14]	Liu D, Sy MS. Phorbol myristate acetate stimulates the dimerization of CD44 involving a cysteine in the transmembrane domain. Journal of Immunology, 1997,159(6):2702-2711
[15]	Neame SJ, Uff CR, Sheikh H. et al. CD44 exhibits a cell type dependent interaction with Triton X-100 insoluble, lipid rich, plasma membrane domains. Journal of Cell Science, 1995,108(9):3127-3135
[16]	Stamenkovic I, Yu Q. Merlin, a "Magic" linker between the extracellular cues and intracellular signaling pathways that regulate cell motility, proliferation, and survival. Current Protein & Peptide Science, 2010,11(6):471-484
[17]	Williams K, Motiani K, Giridhar PV. et al. CD44 integrates signaling in normal stem cell, cancer stem cell and (pre)metastatic niches. Experimental Biology and Medicine, 2013,238(3):324-338
[18]	Legg JW, Lewis CA, Parsons M. et al. A novel PKC-regulated mechanism controls CD44 --ezrin association and directional cell motility. Nature Cell Biology, 2002,4(6):399-407
[19]	Mori T, Kitano K, Terawaki S. et al. Structural basis for CD44 recognition by ERM proteins. Journal of Biological Chemistry, 2008,283(43):29602-29612
[20]	Lesley J, Hyman R, Kincade P. CD44 and its interaction with extracellular matrix. Advances in Immunology, 1993,54:271-335
[21]	Naor D, Sionov R, Ish-Shalom D. CD44: Structure, function and association with the malignant process. Advances in Cancer Research, 1997,71:241-319
[22]	Medzhitov R, Medzhitov R. Origin and physiological roles of inflammation. Nature, 2008,454(7203):428-435
[23]	Barton, MG. A calculated response: Control of inflammation by the innate immune system. Journal of Clinical Investigation, 2008,118(2):413-420
[24]	Nathan C. Neutrophils and immunity: Challenges and opportunities. Nature Reviews Immunology, 2006,6(3):173-182
[25]	Kolaczkowska E, Kubes P. Neutrophil recruitment and function in health and inflammation. Nature Reviews Immunology, 2013,13(3):159-175
[26]	McEver RP. Adhesive interactions of leukocytes, platelets, and the vessel wall during hemostasis and inflammation. Thrombosis and Haemostasis, 2001,86(3):746-756
[27]	Vestweber D and Blanks JE. Mechanisms that regulate the function of selectins and their ligands. Physiological Reviews, 1999,79(1):181-213
[28]	Lee D, Schultz JB, Knauf PA. et al. Mechanical shedding of L-selectin from the neutrophil surface during rolling on sialyl Lewis x under flow. Journal of Biological Chemistry, 2007,282(7):4812-4820
[29]	Yao L, Setiadi H, Xia L. et al. Divergent inducible expression of P-selectin and E-selectin in mice and primates. Blood , 1999,94(11):3820-3828
[30]	Katayama Y, Hidalgo A, Chang JS. et al. CD44 is a physiological E-selectin ligand on neutrophils. Journal of Experimental Medicine, 2005,201(8):1183-1189
[31]	Yago T, Shao B, Miner JJ. et al. E-selectin engages PSGL-1 and CD44 through a common signaling pathway to induce integrin alpha(L)beta(2)-mediated slow leukocyte rolling. Blood, 2010,116(3):485-494
[32]	Nacher M, Blazquez AB, Shao BJ. et al. Physiological contribution of CD44 as a ligand for E-selectin during inflammatory T-cell recruitment. American Journal of Pathology, 2011,178(5):2437-2446
[33]	Jacobs PP, Sackstein R. CD44 and HCELL: Preventing hematogenous metastasis at step 1. FEBS Letters, 2011,585(20):3148-3158
[34]	Ali AJ, Abuelela AF, Merzaban JS. An analysis of trafficking receptors show that CD44 and P-Selectin glycoprotein ligand-1 collectively control the migration of activated human T-cells. Frontiers in Immunology, 2017,8:492
[35]	Hidalgo A, Peired AJ, Wild MK. et al. Complete identification of E-selectin ligands on neutrophils reveals distinct functions of PSGL-1, ESL-1, and CD44. Immunity, 2007,26(4):477-489
[36]	AbuZineh K, Joudeh LI, Al Alwan B, et al. Microfluidics-based super-resolution microscopy enables nanoscopic characterization of blood stem cell rolling. Science Advances, 2018, 4(7): eaat5304
[37]	Day A, Motte C. Hyaluronan cross-linking: A protective mechanism in inflammation? Trends in Immunology, 2006,26(12):637-643
[38]	Jiang D, Liang J, Noble PW. Hyaluronan as an immune regulator in human diseases. Physiological Reviews, 2011,91(1):221-264
[39]	Toole BP, Wight TN, Tammi MI. Hyaluronan-cell interactions in cancer and vascular disease. Journal of Biological Chemistry, 2002,277(7):4593-4596
[40]	Tavianatou AG, Caon I, Franchi M. et al. Hyaluronan: molecular size-dependent signaling and biological functions in inflammation and cancer. FEBS Journal, 2019,286(15):2883-2908
[41]	Ghosh S, Hoselton SA, Wanjara SB. et al. Hyaluronan stimulates ex vivo B lymphocyte chemotaxis and cytokine production in a murine model of fungal allergic asthma. Immunobiology, 2015,220(7):899-909
[42]	Campo GM, Avenoso A, Campo S. et al. Differential effect of molecular size HA in mouse chondrocytes stimulated with PMA. Biochimica et Biophysica Acta, 2009,1790(10):1353-1367
[43]	Campo GM, Avenoso A, Campo S. et al. Small hyaluronan oligosaccharides induce inflammation by engaging both toll-like-4 and CD44 receptors in human chondrocytes. Biochemical Pharmacology, 2010,80(4):480-490
[44]	Wolf KJ, Shukla P, Springer K. et al. A mode of cell adhesion and migration facilitated by CD44 -dependent microtentacles. Proceedings of the National Academy of Sciences of the United States of America, 2020,117(21):11432-11443
[45]	DeGrendele, CH. CD44 and its ligand hyaluronate mediate rolling under physiologic flow: A novel lymphocyte-endothelial cell primary adhesion pathway. Journal of Experimental Medicine, 1996,183(3):1119-1130
[46]	DeGrendele CH. Requirement for CD44 in activated T cell extravasation into an inflammatory site. Science, 1997,278(5338):672-675
[47]	Bonder CS, Clark SR, Norman MU. et al. Use of CD44 by CD4( $+$ ) Th1 and Th2 lymphocytes to roll and adhere. Blood, 2006,107(12):4798-4806
[48]	Pauline Johnson BR. CD44 and its Role in Inflammation and Inflammatory Disease. Inflammation & Allergy Drug Targets, 2009,8(3):208-220
[49]	Hutás G, Bajnok E, Gál I, et al. CD44 -specific antibody treatment and CD44 deficiency exert distinct effects on leukocyte recruitment in experimental arthritis. Blood, 2008,112(13):4999-5006
[50]	Khan AI, Kerfoot SM, Heit B. et al. Role of CD44 and hyaluronan in neutrophil recruitment. Journal of Immunology, 2004,173(12):7594-7601
[51]	Motte CADL, Hascall VC, Drazba J, et al. Mononuclear leukocytes bind to specific hyaluronan structures on colon mucosal smooth muscle cells treated with polyinosinic acid: Polycytidylic acid - inter-alpha-trypsin inhibitor is crucial to structure and function. American Journal of Pathology, 2003,163(1):121-133
[52]	Skelton PT. Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan. Journal of Cell Biology, 1998,140(2):431-446
[53]	Degrendele HC, Kosfiszer M, Estess P. et al. CD44 activation and associated primary adhesion is inducible via T cell receptor stimulation. Journal of Immunology, 1997,159(6):2549-2553
[54]	Maiti A, Maki G, Johnson P. TNF- $alpha$ induction of CD44 -mediated leukocyte adhesion by sulfation. Science, 1998,282(5390):941-943
[55]	Underhill CB, Nguyen HA, Shizari M. et al. CD44 positive macrophages take up hyaluronan during lung development. Developmental Biology, 1993,155(2):324-336
[56]	McDonald B, McAvoy EF, Lam F. et al. Interaction of CD44 and hyaluronan is the dominant mechanism for neutrophil sequestration in inflamed liver sinusoids. Journal of Experimental Medicine, 2008,205(4):915-927
[57]	Kolaczkowska E, Kubes P. Neutrophil recruitment and function in health and inflammation. Nature Reviews Immunology, 2013,13(3):159-175
[58]	Menezes GB, Lee WY, Zhou H. et al. Selective down-regulation of neutrophil mac-1 in endotoxemic hepatic microcirculation via IL-10. Journal of Immunology, 2009,183(11):7557-7568
[59]	Choudhury SR, Babes L, Rahn JJ. et al. Dipeptidase-1 is an adhesion receptor for neutrophil recruitment in lungs and liver. Cell, 2019,178(5):1205-1221
[60]	Zhuo L, Kanamori A, Kannagi R. et al. SHAP potentiates the CD44-mediated leukocyte adhesion to the hyaluronan substratum. Journal of Biological Chemistry, 2006,281(29):20303-20314
[61]	Long M, Lü SQ, Sun GY. Kinetics of receptor-ligand interactions in immune responses. Cellular & Molecular Immunology, 2006,3(2):79-86
[62]	Li N, Lü SQ, Zhang Y. et al. Mechanokinetics of receptor-ligand interactions in cell adhesion. Acta Mechanica Sinica, 2015,31(2):248-258
[63]	Lesley J, English N, Charles C. et al. The role of the CD44 cytoplasmic and transmembrane domains in constitutive and inducible hyaluronan binding. European Journal of Immunology, 2000,30(1):245-253
[64]	AbuSamra DB, Al-Kilani A, Hamdan SM. et al. Quantitative characterization of E-selectin interaction with native CD44 and P-selectin glycoprotein ligand-1 (PSGL-1) using a real time immunoprecipitation-based binding assay. Journal of Biological Chemistry, 2015,290(35):21213-21230
[65]	AbuSamra DB, Aleisa F A, Al-Amoodi A S. et al. Not just a marker: CD34 on human hematopoietic stem/progenitor cells dominates vascular selectin binding along with CD44. Blood Advances, 2017,1(27):2799-2816
[66]	Mizrahy S, Raz SR, Hasgaard M. et al. Hyaluronan-coated nanoparticles: The influence of the molecular weight on CD44 -hyaluronan interactions and on the immune response. Journal of Controlled Release, 2011,156(2):231-238
[67]	Sapudom J, Ullm F, Martin S. et al. Molecular weight specific impact of soluble and immobilized hyaluronan on CD44 expressing melanoma cells in 3D collagen matrices. Acta Biomaterialia, 2017,50:259-270
[68]	Bano F, Banerji S, Howarth M. et al. A single molecule assay to probe monovalent and multivalent bonds between hyaluronan and its key leukocyte receptor CD44 under force. Scientific Reports, 2016,6:34176
[69]	Raman PS, Alves CS, Wirtz D. et al. Single-molecule binding of CD44 to fibrin versus P-selectin predicts their distinct shear-dependent interactions in cancer. Journal of Cell Science, 2011,124(11):1903-1910
[70]	Raman PS, Alves CS, Wirtz D. et al. Distinct kinetic and molecular requirements govern CD44 binding to hyaluronan versus fibrin(ogen). Biophysical Journal, 2012,103(3):415-423
[71]	Lamontagne CA, Grandbois M. PKC-induced stiffening of hyaluronan/CD44 linkage; local force measurements on glioma cells. Experimental Cell Research, 2008,314(2):227-236
[72]	Martin S, Wang HQ, Rathke T. et al. Polymer hydrogel particles as biocompatible AFM probes to study CD44/hyaluronic acid interactions on cells. Polymer, 2016,102:342-349
[73]	Dimitroff CJ, Lee JY, Rafii S. et al. CD44 is a major E-selectin ligand on human hematopoietic progenitor cells. Journal of Cell Biology, 2001,153(6):1277-1286
[74]	Dimitroff CJ, Lee JY, Fuhlbrigge RC. et al. A distinct glycoform of CD44 is an L-selectin ligand on human hematopoietic cells. Proceedings of the National Academy of Sciences of the United States of America, 2000,97(25):13841-13846
[75]	Hanley WD, Napier SL, Burdick MM. et al. Variant isoforms of CD44 are P- and L-selectin ligands on colon carcinoma cells. FASEB Journal, 2006,20(2):337-339
[76]	Napier SL, Healy ZR, Schnaar RL. et al. Selectin ligand expression regulates the initial vascular interactions of colon carcinoma cells - The roles of CD44V and alternative sialofucosylated selectin ligands. Journal of Biological Chemistry, 2007,282(6):3433-3441
[77]	Christophis C, Taubert I, Meseck G R. et al. Shear stress regulates adhesion and rolling of CD44 $+$ leukemic and hematopoietic progenitor cells on hyaluronan. Biophysical Journal, 2011,101(3):585-593
[78]	Hanke M, Hoffmann I, Christophis C, et al. Differences between healthy hematopoietic progenitors and leukemia cells with respect to CD44 mediated rolling versus adherence behavior on hyaluronic acid coated surfaces. Biomaterials, 2014,35(5):1411-1419
[79]	Kim Y, Kumar S. CD44 -mediated adhesion to hyaluronic acid contributes to mechanosensing and invasive motility. Molecular Cancer Research, 2014,12(10):1416-1429
[80]	Marshall BT, Long M, Piper JW. et al. Direct observation of catch bonds involving cell-adhesion molecules. Nature, 2003,423(6936):190-193
[81]	Suzuki T, Suzuki M, Ogino S. et al. Mechanical force effect on the two-state equilibrium of the hyaluronan-binding domain of CD44 in cell rolling. Proceedings of the National Academy of Sciences of the United States of America, 2015,112(22):6991-6996
[82]	Ishii S, Ford R, Thomas P. et al. CD44 participates in the adhesion of human colorectal carcinoma cells to laminin and type IV collagen. Surgical Oncology, 1993,2(4):255-264
[83]	Jalkanen S. Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin. Journal of Cell Biology, 1992,116(3):817-825
[84]	Misra S, Hascall VC, Markwald RR. et al. Interactions between hyaluronan and its receptors (CD44, RHAMM) regulate the activities of inflammation and cancer. Frontiers in Immunology, 2015,6:201
[85]	Johnson P, Maiti A, Brown K. et al. A role for the cell adhesion molecule CD44 and sulfation in leukocyte-endothelial cell adhesion during an inflammatory response? Biochemical Pharmacology, 2000,59(5):455-465
[86]	Teriete P, Banerji S, Noble M. et al. Structure of the regulatory hyaluronan binding domain in the inflammatory leukocyte homing receptor CD44. Molecular Cell, 2004,13(4):483-496
[87]	Takeda M, Ogino S, Umemoto R. et al. Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR. Journal of Biological Chemistry, 2006,281(52):40089-40095
[88]	Banerji S, Wright AJ, Noble M. et al. Structures of the Cd44-hyaluronan complex provide insight into a fundamental carbohydrate-protein interaction. Nature Structural & Molecular Biology, 2007,14(3):234-239
[89]	Ogino S, Nishida N, Umemoto R. et al. Two-state conformations in the hyaluronan-binding domain regulate CD44 adhesiveness under flow condition. Structure, 2010,18(5):649-656
[90]	Vuorio J, Vattulainen I, Martinez-Seara H. Atomistic fingerprint of hyaluronan-CD44 binding. PLOS Computational Biology, 2017,13(7):e1005663
[91]	Somers WS, Tang J, Shaw GD. et al. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1. Cell, 2000,103(3):467-479
[92]	Lü SQ, Zhang Y, Long M. Visualization of allostery in P-selectin lectin domain using MD simulations. PLOS One, 2010,5(12):e15417
[93]	Lü SQ, Chen SB, Mao DB. et al. Contribution of the CR domain to P-selectin lectin domain allostery by regulating the orientation of the EGF domain. PLOS One, 2015,10(2):e0118083
[94]	Lou J, Zhu C. A structure-based sliding-rebinding mechanism for catch bonds. Biophysical Journal, 2007,92(5):1471-1485
[95]	Bourguignon LYW. CD44 isoform-cytoskeleton interaction in oncogenic signaling and tumor progression. Frontiers in Bioscience, 1998,3(4):637-649
[96]	冯世亮, 周吕文, 吕守芹等. 悬浮态上皮细胞粘附的力学化学耦合模型及数值模拟. 力学学报, 2020,52(3):255-264 (Feng Shiliang, Zhou Lüwen, Lü Shouqin, et al. Mechanochemical coupling model and numerical simulation for cell-cell adhesion in suspended epithelial cells. Chinese Journal of Theoretical and Applied Mechanics. 2020,52(3):854-863 (in Chinese))
[97]	Tsukita S. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. Journal of Cell Biology, 1994,126(2):391-401
[98]	Ng T, Parsons M, Hughes WE. et al. Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility. The EMBO Journal, 2001,20(11):27232741
[99]	Morrison H. The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44. Genes & Development, 2001,15(8):968-980
[100]	Bourguignon LYW, Zhu H, Shao L. et al. CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migration. Journal of Biological Chemistry, 2001,276(10):7327-7336
[101]	Bourguignon LYW, Gilad E, Rothman K. et al. Hyaluronan-CD44 interaction with IQGAP1 promotes Cdc42 and ERK signaling, leading to actin binding, Elk-1/Estrogen receptor transcriptional activation, and ovarian cancer progression. Journal of Biological Chemistry, 2005,280(12):11961-11972
[102]	Bourguignon LYW, Zhu HB, Shao LJ. et al. CD44 interaction with Tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. Journal of Biological Chemistry, 2000,275(3):1829-1838
[103]	Bourguignon LYW, Zhu H, Zhou B. et al. Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185HER2 and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth. Journal of Biological Chemistry, 2001,276(52):48679-48692
[104]	Manning BD, Toker A. AKT/PKB signaling: Navigating the network. Cell, 2017,169(3):381-405
[105]	Liu S, Cheng C. Akt signaling is sustained by a CD44 splice isoform-mediated positive feedback loop. Cancer Research, 2017,77(14):3791-3801
[106]	Khaldoyanidi S, Moll J, Karakhanova S. et al. Hyaluronate-enhanced hematopoiesis: Two different receptors trigger the release of interleukin-1 $eta$ and interleukin-6 from bone marrow macrophages. Blood, 1999,94(3):940-949
[107]	Slevin M, Krupinski J, Kumar S. et al. Angiogenic oligosaccharides of hyaluronan induce protein tyrosine kinase activity in endothelial cells and cytoplasmic signal transduction pathway resulting in proliferation. Laboratory Investigation, 1998,78(8):987-1003
[108]	Orian-Rousseau V, Ponta H. Adhesion proteins meet receptors: A common theme? Advances in Cancer Research, 2008,101:63-92
[109]	Krause DS, Etten RAV. Tyrosine kinases as targets for cancer therapy. New England Journal of Medicine, 2005,353(2):172-187
[110]	Hoon DSB, Kitago M, Kim J. et al. Molecular mechanisms of metastasis. Cancer & Metastasis Reviews, 2006,25(2):203-220
[111]	Kissil JL, Johnson KC, Eckman MS. et al. Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization. Journal of Biological Chemistry, 2002,277(12):10394-10399
[112]	Siegelman MH, Stanescu D, Estess P. The CD44 -initiated pathway of T-cell extravasation uses VLA-4 but not LFA-1 for firm adhesion. Journal of Clinical Investigation, 2000,105(5):683-691
[113]	Nandi A, Estess P, Siegelman M. Bimolecular complex between rolling and firm adhesion receptors required for cell arrest: CD44 association with VLA-4 in T cell extravasation. Immunity, 2004,20(4):455-465
[114]	Chopra A, Murray ME, Byfield FJ. et al. Augmentation of integrin-mediated mechanotransduction by hyaluronic acid. Biomaterials, 2014,35(1):71-82
[115]	Fujisaki T, Tanaka Y, Fujii K. et al. CD44 stimulation induces integrin-mediated adhesion of colon cancer cell lines to endothelial cells by up-regulation of integrins and c-Met and activation of integrins. Cancer Research, 1999,59(17):4427-4434
[116]	Wang HS, Ying H, Su CH. et al. CD44 Cross-linking induces integrin-mediated adhesion and transendothelial migration in breast cancer cell line by up-regulation of LFA-1 ( $alpha$ L $eta$ 2) and VLA-4 ( $alpha$ 4 $eta$ 1). Experimental Cell Research, 2005,304(1):116-126
[117]	Murai T, Sato C, Sato M. et al. Membrane cholesterol modulates the hyaluronan-binding ability of CD44 in T lymphocytes and controls rolling under shear flow. Journal of Cell Science, 2013,126(15):3284-3294
[118]	Yang Z, Qin W, Chen Y. et al. Cholesterol inhibits hepatocellular carcinoma invasion and metastasis by promoting CD44 localization in lipid rafts. Cancer Letters, 2018,429:66-77
[119]	Turley E, Noble P, Bourguignon L. Signaling properties of hyaluronan receptors. The Journal of Biological Chemistry, 2002,277(7):4589-4592
[120]	Anastasia, Tavianatou, Ilaria, et al. Hyaluronan: molecular size-dependent signaling and biological functions in inflammation and cancer. FEBS Journal, 2019,286(15):2883-2908
[121]	Petrey A C, de la Motte CA. Hyaluronan, a crucial regulator of inflammation. Frontiers in Immunology, 2014,5(5):101
[122]	Yang C, Cao M, Liu H. et al. The high and low molecular weight forms of hyaluronan have distinct effects on CD44 clustering. Journal of Biological Chemistry, 2012,287(51):43094-43107
[123]	Wu X, Hu J, Li G. et al. Biomechanical stress regulates mammalian tooth replacement via the integrin beta 1-RUNX2-Wnt pathway. The EMBO Journal, 2020,39(3):e102374
[124]	Lorenz L, Axnick J, Buschmann T. et al. Mechanosensing by $eta$ 1 integrin induces angiocrine signals for liver growth and survival. Nature, 2018,562(7725):128-132
[125]	Qi JY, Wu BB, Feng SL. et al. Mechanical regulation of organ asymmetry in leaves. Nature Plants, 2017,3(9):724-733
[126]	Huang G, Xu F, Genin GM. et al. Mechanical microenvironments of living cells: a critical frontier in mechanobiology. Acta Mechanica Sinica, 2019,35(002):265-269
[127]	Zhou Z, Li W, Huang C. et al. Mechanical microenvironment as a key cellular regulator in the liver. Acta Mechanica Sinica, 2019,35(2):289-298
[128]	Tajik A, Zhang Y, Wei F. et al. Transcription upregulation via force-induced direct stretching of chromatin. Nature Materials, 2016,15(12):1287-1296
[129]	Zhu C, Chen W, Lou JZ. et al. Mechanosensing through immunoreceptors. Nature Immunology, 2019,20(10):1269-1278

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BIOMECHANICS AND FUNCTIONAL REGULATIONS OF CD44-LIGAND INTERACTIONS

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BIOMECHANICS AND FUNCTIONAL REGULATIONS OF CD44-LIGAND INTERACTIONS

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