Purification and partial characterization of CD9 antigen of human platelets

@article{Higashihara1990PurificationAP,
  title={Purification and partial characterization of CD9 antigen of human platelets},
  author={M. Higashihara and K. Takahata and Y. Yatomi and K. Nakahara and K. Kurokawa},
  journal={FEBS Letters},
  year={1990},
  volume={264}
}
CD9 antigen (p24) was purified from human platelets and partially characterized. The yield was 75 μg from 10 units of platelet concentrates. p24 (38 000 copies/platelet) has intramolecular disulfide bond(s) and, in SDS‐PAGE, consists of major 24‐kDa molecule and minor 26‐ to 31‐kDa molecules. The N‐terminal sequence of p24, PVKGOTKXIKYLLFGFNFIF, indicates that the protein has not previously been characterized and amino terminus (position 12–20) is hydrophobic. 
CD9, a major platelet cell surface glycoprotein, is a ROCA antigen and is expressed in the nervous system
TLDR
Results provide another example of a cell surface protein expressed by both hematopoietic and neural cells, and suggest a role for CD9 in intercellular signaling in the nervous system. Expand
Differential expression of CD42b and CD9 proteins in platelets and extracellular membrane vesicles during platelet-concentrate storage
TLDR
The results obtained indicate that platelet concentrates contain different populations of membrane vesicles, the molecular composition of which varies during storage. Expand
Monoclonal antibody AG-1 initiates platelet activation by a pathway dependent on glycoprotein IIb-IIIa and extracellular calcium.
TLDR
The results suggest that AG-1 binding to a unique platelet-surface glycoprotein initiates platelet responses through the activation of PIP2-specific phospholipase C, and that this occurs through a signal pathway that is dependent on GpIIb-IIIa and extracellular calcium. Expand
A review of the role of platelet membrane glycoproteins in the platelet-vessel wall interaction.
TLDR
This review indicates how research into platelet membrane glycoprotein (GP) receptors is yielding vital information on the mechanisms of platelet adhesion and aggregation and the role of GP IIb-IIIa complexes which, following platelet activation, bind fibrinogen and other adhesive proteins. Expand
Identification of Tspan9 as a novel platelet tetraspanin and the collagen receptor GPVI as a component of tetraspanin microdomains
TLDR
A role for Tspan9 in regulating platelet function in concert with other platelet tetraspanins and their associated proteins is suggested. Expand
CD9 negatively regulates integrin αIIbβ3 activation and could thus prevent excessive platelet recruitment at sites of vascular injury
TLDR
The results indicated that CD9 does not play a critical role in primary hemostasis and thrombosis, and its ability to regulate integrin aIIbb3 functions remains largely unknown. Expand
Quantitative characterization of Tetraspanin 8 homointeractions in the plasma membrane.
The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional proteinExpand
Structural and biochemical studies of phage P2 DNA-binding proteins and human tetraspanins
TLDR
Biochemical studies of proteins are crucial for a more detailed view of the world around us and can vary, from a complex mammalian system to a more simple viral entity. Expand
Characterization of the Tetraspanin protein Tspan18
TLDR
A role for Tspan18 in calcium signalling on these cell types is suggested, as over-expression of T Span18 in lymphocyte cell lines activated an NFAT/AP-1 reporter, which responds to calcium and MAPK signalling. Expand
Site‐specific functionality and tryptophan mimicry of lipidation in tetraspanin CD9
TLDR
It is determined that wild‐type human tetraspanins CD9 and CD81 exhibit nonstochastic distributions of bound acyl chains, and tryptophan mimicry is identified as a possible biochemical approach to study site‐specific transmembrane‐protein lipidation. Expand
...
1
2
3
...

References

SHOWING 1-10 OF 32 REFERENCES
Mechanisms of the mAb ALB6(CD9) induced human platelet activation: comparison with thrombin.
TLDR
Final biological and metabolic effects of ALB6 appear similar to that of thrombin but three differences bring additional information: the lag phase, the kinetic of ALb6-induced release is identical for all granules whereas the release of dense granules is faster when induced byThrombin. Expand
The platelet protein phosphorylation induced by a monoclonal antibody against human platelets (TP82).
TLDR
It is suggested that polyphosphoinositide breakdown plays an essential role in antibody-induced release of platelet granules. Expand
Possible involvement of two proteins (phosphoprotein and CD9(p24)) in regulation of platelet calcium fluxes
TLDR
Proteins of similar molecular mass appear to be involved in calcium fluxes: one is recognized by the ALB6 antibody while the other can be phosphorylated by the C‐subunit. Expand
Expression of a 26,000-dalton glycoprotein on activated human T cells.
TLDR
The expression of a 26,000-dalton glycoprotein on human T cells following stimulation by either mitogen or alloantigen is described and it is shown that the GP 26-bearing cells are not directly responsible for the cytotoxicity generated in MLR. Expand
The functional cell surface glycoprotein CD9 is distinguished by being the major fatty acid acylated and a major iodinated cell-surface component of the human platelet.
We showed that a 22 kDa protein (which comigrated with the leukocyte differentiation antigen CD9 as determined by immunoblotting with the platelet-activating mAb 50H.19) is a major iodinatedExpand
The biochemical characterization of a cell surface antigen associated with acute lymphoblastic leukemia and lymphocyte precursors.
TLDR
Serologic studies indicate that the cALL-associated antigen is found on the terminal transferase-positive lymphoid cells, and it therefore seems likely that the gp100 molecule is a normal gene products of lymphocyte precursors. Expand
Biochemical characterization of human carcinoma surface antigen associated with protein kinase activity
TLDR
Both glycoproteins undergo an apparent increase of molecular weight of about 500 daltons when run in the non‐reduced form on SDS polyacrylamide gels under standard electrophoretic conditions, suggesting they contain a similar degree of intra‐chain disulphide bonding. Expand
Characteristics of platelet aggregation induced by the monoclonal antibody ALB6 (acute lymphoblastic leukemia antigen p 24)
TLDR
The results suggest that ALB6 interferes with a mechanism common to all aggregation pathways; the possible mechanisms are discussed. Expand
Exposure of platelet fibrinogen receptors by a monoclonal antibody to CD9 antigen.
TLDR
It is demonstrated that the binding of IgG molecules to the CD9 antigen exposes fibrinogen receptors through both secreted ADP and thromboxane and that either one of both can expose the receptors to an extent sufficient to aggregate platelets. Expand
Biochemical characterisation of leukaemia-associated antigen p24 defined by the monoclonal antibody BA-2.
TLDR
Identical molecular weights, when reduced and non-reduced antigens were compared, suggest that it contains no internal disulphide linkages and failure to detect any other band on gradient gel SDS-polyacrylamide gel electrophoresis from 5-15% suggests that is is not strongly associated with any other structure. Expand
...
1
2
3
4
...