Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Microglia use multiple mechanisms to mediate interactions with vitronectin; non-essential roles for the highly-expressed avb3 and avb5 integrins
Integrin a2b1 is the major receptor for collagens in human tissues, being involved in cell adhesion and the control of collagen and collagenase gene expression. The collagen binding site of a2b1 has been localized to the a2 von Willebrand Factor type A (VWFA) domain (A-domain or I-domain) and the residues responsible for the interaction with collagen have been mapped. We report a study of a2 VWFA domain in which residue E318, which lies outside the collagen binding site, is mutated to tryptophan, showing that this is a gain-of-function mutation. ...
The red cell intercellular adhesion molecule-4 (ICAM-4)
binds to different members of the integrin receptor families.
Tobetterdefine the ICAM-4 integrinreceptor specificity, cell
transfectants individually expressing various integrins were
used to demonstrate thataLb2,aMb2,andaIIbb3(activated)
bind specifically and dose dependently to the recombinant
ICAM-4-Fcprotein.We also showthat cell surface ICAM-4
interacts with the cell surface aVb3
Adhesive properties of endothelial cells are influenced by the thioldisulfide
balance. However, the molecular mechanism of this effect is unclear,
although recent observations indicate that integrin receptors may be direct
targets for redox modulation. The purpose of this study was to examine
whether protein disulfide isomerase (PDI) is directly involved in this pro-cess.
Recently, a new protein containing a disintegrin domain,
alternagin-C (Alt-C), was purified fromBothrops alternatus
venom. Unlike other disintegrins, in Alt-C an ECD amino
acid motif takes the place of the RGD sequence. Most dis-integrins contain an RGD/KGD sequence and are very
potent inhibitors of platelet aggregation, as well as other cell
interactions with the extracellular matrix, including tumor
cell metastasis and angiogenesis. The present study investi-gated the effects of Alt-C on human neutrophil chemotaxis
in vitro and the activation of integrin-mediated pathways....
Being diagnosed with cancer is devastating. But when the cancer cells have to spread
to form secondary colonies, the prognosis for the patient is worse. If meaningful
improvements in survival are to occur, then control of metastasis will be a
foundation. Relatively little is known about the control of the metastatic process at
the molecular level. This volume begins to explore our current knowledge regarding
the underlying molecular and biochemical mechanisms controlling the metastatic
Tumor angiogenesis is a complex process involving many different cell types that must proliferate, migrate, invade, and differentiate in response to signals from the tumor microenvironment. Endothelial cells (ECs) sprout from host vessels in response to VEGF, bFGF, Ang2, and other proangiogenic stimuli. Sprouting is stimulated by VEGF/VEGFR2, Ang2/Tie-2, and integrin/extracellular matrix (ECM) interactions.
Numerous virus–target cell interactions have been described, and it is now clear that different viruses can use similar host-cell receptors for entry. The list of certain and likely host receptors for viral pathogens is long. Among the host membrane components that can serve as receptors for viruses are sialic acids, gangliosides, glycosaminoglycans, integrins and other members of the immunoglobulin superfamily, histocompatibility antigens, and regulators and receptors for complement components.
The vertex of the adenoviral capsid is formed by the penton, a complex of
two proteins, the pentameric penton base and the trimeric fiber protein.
The penton contains all necessary components for viral attachment and
entry into the host cell. After initial attachment via the head domain of the
fiber protein, the penton base interacts with cellular integrins through an
Arg-Gly-Asp (RGD) motif located in a hypervariable surface loop, trigger-ing virus internalization.
The platelet integrin receptoraIIbb3 plays a critical role
in thrombosis and haemostasis by mediating interactions
between platelets and several ligands but primarily fibrin-ogen. It has been shown previously that the YMESRADR
KLAEVGRVYLFL (313–332) sequence of theaIIb
plays an important role in platelet activation, fibrinogen
-mediated outside-in signalling.
The small G protein Rap1 regulates diverse cellular processes such as inte-grin activation, cell adhesion, cell–cell junction formation and cell polarity.
It is crucial to identify Rap1 effectors to better understand the signalling
pathways controlling these processes.
NBR1(named as next toBRCA1) was originally cloned as a
candidate gene for the ovarian cancer antigen CA125, using
expression cloning with the anti-CA125 Ig, OC125.NBR1
has been of interest due to its position close toBRCA1,
although no involvement in breast or ovarian cancer has
been demonstrated. Recently, the antigen CA125 has been
cloned, and identi®ed as a new mucin, MUC16, entirely
dierent from NBR1.