Myeloid progenitor surface antigen identified by monoclonal antibody

Bradstock, Kenneth F.; Favaloro, Emmanuel J.; Kabral, Arnold; Kerr, Arna; Hughes, W. G.; Musgrove, Elizabeth A.

doi:10.1111/j.1365-2141.1985.tb04055.x

Cited by 24 publications

(8 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To confirm that botrocetin modulated the binding of vWF to GP Ib-IX complex by a mechanism similar to that of ristocetin, we examined the effect of a series of anti-GP Ib-IX complex and anti-vWF monoclonal antibodies on the botrocetin-dependent binding of vWF to platelets and GP Ib-IX complex coated beads (Figure 6). WM 15 is an irrelevant monoclonal antibody directed against a 165-kDa membrane protein on myeloid precursor cells (Bradstock et al, 1985) and served as a negative control. Two monoclonal antibodies directed against epitopes on the 45-kDa, N-terminal region of GP Iba, HIP 1 and AK 2, strongly inhibited the botrocetin-dependent binding of vWF to platelets and GP Ib-IX complex coated beads.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex

Andrews¹,

Booth²,

Gorman³

et al. 1989

Biochemistry

168

120

View full text Add to dashboard Cite

Interaction of von Willebrand factor (vWF) with its platelet receptor only occurs in vitro in the presence of a modulator such as ristocetin. We have recently confirmed that the human platelet membrane glycoprotein (GP) Ib-IX complex is the receptor involved in the ristocetin-dependent binding of vWF by reconstitution with the purified components [Berndt, M.C., Du, X., & Booth, W.J. (1988) Biochemistry 27, 633-640]. We have now developed a similar solid-phase reconstitution assay using an alternate modulator, botrocetin, for the competitive analysis of functional domains in both vWF and the GP Ib-IX complex. Botrocetin was purified from Bothrops jararaca venom by ammonium sulfate fractionation and subsequent DEAE-cellulose and hydroxylapatite chromatography. The purified protein was a 25-kilodalton (kDa) disulfide-linked dimer with apparent subunit molecular weights of 14,000 and 14,500. Binding studies with immobilized botrocetin demonstrated that botrocetin bound to vWF and to a 52/48-kDa region of vWF that contains the GP Ib binding domain, but not to glycocalicin, a proteolytic fragment of GP Ib that contains the vWF binding site. Binding of 125I-labeled vWF to GP Ib-IX complex coated beads and to platelets was strictly botrocetin-dependent with half-maximal binding at a botrocetin concentration of congruent to 0.27 microM. Botrocetin-dependent binding of vWF was specific, saturable, and comparable to that observed with ristocetin. An anti-vWF monoclonal antibody, 3F8, inhibited ristocetin- but not botrocetin-dependent binding of vWF, suggesting the presence of distinct ristocetin and botrocetin modulator sites on vWF. The botrocetin reconstitution assay was at least an order of magnitude more sensitive than the corresponding ristocetin assay for the competitive analysis of functional domains on both vWF and the GP Ib-IX complex and has confirmed the localization of the vWF-binding domain to the 45-kDa N-terminal region of GP Ib.

show abstract

Section: Resultsmentioning

confidence: 99%

“…2C9 and 3F8 are directed against distinct epitopes on the vWF molecule (Booth et al, 1984b). WM 15 is an irrelevant monoclonal antibody against a 165-kDa protein of myeloid cells and was employed as a control monoclonal antibody (Bradstock et al, 1985).…”

Section: Methodsmentioning

confidence: 99%

Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex

Andrews¹,

Booth²,

Gorman³

et al. 1989

Biochemistry

168

120

View full text Add to dashboard Cite

show abstract

“…TdT was examined using specific rabbit anti-calf TdT antibody [17]. Antibody WM-15, described in detail elsewhere [18,19], reacts with a 165 KD surface membrane antigen expressed on a subset of normal bone marrow myeloid precursor cells, and on 60% of cases of acute myeloid leukaemias and its variants. WM-15 is unreactive with normal and leukaemic lymphoid cells.…”

Section: Anti Bodiesmentioning

confidence: 99%

Coexpression of p165 myeloid surface antigen and terminal deoxynucleotidyl transferase: A comparison of acute myeloid leukaemia and normal bone marrow cells

et al. 1986

Self Cite

View full text Add to dashboard Cite

A double immunofluorescence technique, using antibodies to terminal transferase (TdT) and a 165-kilodalton myeloid differentiation antigen (p165), has been used to investigate the phenomenon of TdT expression in cases of acute myeloid leukaemia (AML). Five cases of AML were shown to have significant (18-90%) numbers of leukaemic cells that concurrently expressed both TdT and p165 myeloid surface antigen. Examination of nonleukaemic bone marrow cells showed that the vast majority of normal TdT+ cells are p165 negative. However, in 5 of the 11 samples analyzed, rare cells staining for both p165 and TdT were found. These results suggest that some cases of TdT+ AML may arise from the clonal expansion of rare "biphenotypic" precursor cells existing in normal bone marrow.

show abstract

“…The generation of granulocytes frotn stem cells in bone marrow involves morphologically identifiable stages of development towards their fully differentiated phenotype. Together with ultrastructural changes, cellular development can be demonstrated using cytochemical (1; 2) and immunochemical markers (3)(4)(5)(6).…”

Section: Introductionmentioning

confidence: 99%

“…Together with ultrastructural changes, cellular development can be demonstrated using cytochemical (1; 2) and immunochemical markers (3)(4)(5)(6).…”

Section: Introductionmentioning

confidence: 99%

Antigen expression during early human granulocyte development studied with immuno‐electron microscopy

et al. 1987

Immunol Cell Biol

View full text Add to dashboard Cite

Summary. Expression of the hapten fucosyl-N-acetyltactosamine was correlated with ultrastructural development in human granulocyie precursors using the monoclonal antibody FMC 10 with immunogoid techniques. The antigen was detectable from ihe myeloblast/early neutrophilic promyelocyte stage onwards and was associated with striking development of ihe rough endoplasmic reticular system. In addition, low levels of labelling were seen on monocytes, eosinophils and some basophll precursors. Coniraciion and alignment of the cisternae of the rough endoplastnic reiiciilum during the promyelocyte stage of neutrophilic differentiation gave the appearance of a plasma cell. However, on closer examination it was apparent that irue plasma cells did not react with this aniibody.

show abstract

Myeloid progenitor surface antigen identified by monoclonal antibody

Cited by 24 publications

References 28 publications

Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex

Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex

Coexpression of p165 myeloid surface antigen and terminal deoxynucleotidyl transferase: A comparison of acute myeloid leukaemia and normal bone marrow cells

Antigen expression during early human granulocyte development studied with immuno‐electron microscopy

Contact Info

Product

Resources

About