Abstract
The murine monoclonal antibody (MoAb) NL07 was generated by immunization with human platelet extracts. NL07 MoAb recognized a molecule expressed by human platelets, monocytes, and endothelial cells, as well as by the myelomonocytic line U937 and by some melanoma cells or lines. Normal endothelial cells and the melanoma cells express the NL07 epitope only while adhering to a substrate. SDS-polyacrylamide gel electrophoresis and two-dimensional gel analysis indicate that the molecule recognized by NL07 MoAb on platelets is a single chain structure featuring a molecular weight of 85 kDa under reducing conditions, with an acidic isoelectric point ranging from 5.2 to 5.5. The specific phenotype distribution and the biochemical structure indicate that NL07 MoAb recognizes the platelet GPIV (CD36) molecule, a surface glycoprotein with a functional role of thrombospondin receptor. The results of competition tests with OKM5 MoAb (specific for the CD36 molecule) confirm the molecular specificity and epitope coincidence. Furthermore, upon binding to the platelets, NL07 MoAb is able to transmit via CD36 an activation signal which is followed by a potent aggregation. On the contrary, there is lack of evidence concerning the ability of the CD36 molecule of transmitting signal(s) on the U937 cells.
| Original language | English |
|---|---|
| Pages (from-to) | 487-500 |
| Number of pages | 14 |
| Journal | Cellular Immunology |
| Volume | 137 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Oct 15 1991 |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
- Immunology
Cite this
Analysis of the human CD36 leucocyte differentiation antigen by means of the monoclonal antibody NL07. / Alessio, M.; Ghigo, D.; Garbarino, G.; Geuna, M.; Malavasi, F.
In: Cellular Immunology, Vol. 137, No. 2, 15.10.1991, p. 487-500.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Analysis of the human CD36 leucocyte differentiation antigen by means of the monoclonal antibody NL07
AU - Alessio, M.
AU - Ghigo, D.
AU - Garbarino, G.
AU - Geuna, M.
AU - Malavasi, F.
PY - 1991/10/15
Y1 - 1991/10/15
N2 - The murine monoclonal antibody (MoAb) NL07 was generated by immunization with human platelet extracts. NL07 MoAb recognized a molecule expressed by human platelets, monocytes, and endothelial cells, as well as by the myelomonocytic line U937 and by some melanoma cells or lines. Normal endothelial cells and the melanoma cells express the NL07 epitope only while adhering to a substrate. SDS-polyacrylamide gel electrophoresis and two-dimensional gel analysis indicate that the molecule recognized by NL07 MoAb on platelets is a single chain structure featuring a molecular weight of 85 kDa under reducing conditions, with an acidic isoelectric point ranging from 5.2 to 5.5. The specific phenotype distribution and the biochemical structure indicate that NL07 MoAb recognizes the platelet GPIV (CD36) molecule, a surface glycoprotein with a functional role of thrombospondin receptor. The results of competition tests with OKM5 MoAb (specific for the CD36 molecule) confirm the molecular specificity and epitope coincidence. Furthermore, upon binding to the platelets, NL07 MoAb is able to transmit via CD36 an activation signal which is followed by a potent aggregation. On the contrary, there is lack of evidence concerning the ability of the CD36 molecule of transmitting signal(s) on the U937 cells.
AB - The murine monoclonal antibody (MoAb) NL07 was generated by immunization with human platelet extracts. NL07 MoAb recognized a molecule expressed by human platelets, monocytes, and endothelial cells, as well as by the myelomonocytic line U937 and by some melanoma cells or lines. Normal endothelial cells and the melanoma cells express the NL07 epitope only while adhering to a substrate. SDS-polyacrylamide gel electrophoresis and two-dimensional gel analysis indicate that the molecule recognized by NL07 MoAb on platelets is a single chain structure featuring a molecular weight of 85 kDa under reducing conditions, with an acidic isoelectric point ranging from 5.2 to 5.5. The specific phenotype distribution and the biochemical structure indicate that NL07 MoAb recognizes the platelet GPIV (CD36) molecule, a surface glycoprotein with a functional role of thrombospondin receptor. The results of competition tests with OKM5 MoAb (specific for the CD36 molecule) confirm the molecular specificity and epitope coincidence. Furthermore, upon binding to the platelets, NL07 MoAb is able to transmit via CD36 an activation signal which is followed by a potent aggregation. On the contrary, there is lack of evidence concerning the ability of the CD36 molecule of transmitting signal(s) on the U937 cells.
UR - http://www.scopus.com/inward/record.url?scp=0025998336&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025998336&partnerID=8YFLogxK
U2 - 10.1016/0008-8749(91)90096-T
DO - 10.1016/0008-8749(91)90096-T
M3 - Article
VL - 137
SP - 487
EP - 500
JO - Cellular Immunology
JF - Cellular Immunology
SN - 0008-8749
IS - 2
ER -