| Literature References | 1. OKUMURA, T. AND JAMIESON, G.A.
Platelet glycocalicin. Orientation of glycoproteins on the human platelet
surface.
J.BIOL.CHEM. 251 5944-5949 (1976).
2. NICHOLSON, A.C., FEBBRAIO, M., HAN, J., SILVERSTEIN, R.L. AND
HAJJAR, D.P.
CD36 in atherosclerosis. The role of a class B macrophage scavenger receptor.
ANN.N.Y.ACAD.SCI. 902 128-131 (2000).
3. SILVERSTEIN, R.L. AND FEBBRAIO, M.
CD36 and atherosclerosis.
CURR.OPIN.LIPIDOL. 11 483-491 (2000).
4. SAVILL, J., HOGG, N., REN, Y. AND HASLETT, C.
Thrombospondin cooperates with CD36 and the vitronectin receptor
in macrophage recognition of neutrophils undergoing apoptosis.
J.CLIN.INVEST. 90 1513-1522 (1989).
5. TANDON, NN., KRALISZ, U. AND JAMIESON, GA.
Identification of glycoprotein IV (CD36) as a primary receptor
for platelet-collagen adhesion.
J.BIOL.CHEM. 264 7576-7583 (1989).
6. MCGREGOR, J.L., CATIMEL, B., PARMENTIER, S., CLEZARDIN, P., DECHAVANNE, M.
AND LEUNG, L.L.
Rapid purification and partial characterization of human platelet
glycoprotein IIIb. Interaction with thrombospondin and its role in platelet
aggregation.
J.BIOL.CHEM. 264 501-506 (1989).
7. BARNWELL, J.W., ASCH, A.S., NACHMAN, R.L., YAMAYA, M., AIKAWA, M. AND
INGRAVALLO, P.
A human 88-kD membrane glycoprotein (CD36) functions in vitro as a receptor
for a cytoadherence ligand on Plasmodium falciparum-infected erythrocytes.
J.CLIN.INVEST. 84 765-772 (1989).
8. BULL, H.A., BRICKELL, P.M. AND DOWD, P.M.
Src-related protein tyrosine kinases are physically associated with the
surface antigen CD36 in human dermal microvascular endothelial cells.
FEBS LETT. 351 41-44 (1994).
9. MIYAOKA, K., KUWASAKO, T., HIRANO, K., NOZAKI, S., YAMASHITA, S.
AND MATSUZAWA, Y.
CD36 deficiency associated with insulin resistance.
LANCET 357 686-687 (2001).
10. VEGA, M.A., SEGUI-REAL, B., GARCIA, J.A., CALES, C., RODRIGUEZ, F.,
VANDERKERCKHOVE, J. AND SANDOVAL, I.V.
Cloning, sequencing, and expression of a cDNA encoding rat LIMP II, a novel
74-kDa lysosomal membrane protein related to the surface adhesion protein
CD36.
J.BIOL.CHEM. 266 16818-16824 (1991).
11. FUJITA, H., EZAKI, J., NOGUCHI, Y., KONO, A., HIMENO, M. AND KATO, K.
Isolation and sequencing of a cDNA clone encoding 85kDa sialoglycoprotein
in rat liver lysosomal membranes.
BIOCHEM.BIOPHYS.RES.COMMUN. 178 444-452 (1991).
12. FUJITA, H., TAKATA, Y., KONO, A., TANAKA, Y., TAKAHASHI, T., HIMENO, M.
AND KATO, K.
Isolation and sequencing of a cDNA clone encoding the 85 kDa human lysosomal
sialoglycoprotein (hLGP85) in human metastatic pancreas islet tumor cells.
BIOCHEM.BIOPHYS.RES.COMMUN. 184 604-611 (1992).
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| Documentation | CD36 is a transmembrane, highly glycosylated, 88kDa glycoprotein [1]
expressed by monocytes, macrophages, platelets, microvascular endothelial
cells and adipose tissue [2]. It is a multifunctional receptor that binds
to oxidised LDL (OxLDL), long chain fatty acids, anionic phospholipids,
apoptotic cells, thrombospondin (TSP), collagen and Plasmodium falciparum-
infected erythrocytes [2].
CD36 has numerous cellular functions. It is a type B scavenger receptor,
playing a major role in the uptake of OxLDL by macrophages [3]. The lipid-
rich macrophages are then differentiated into foam cells and contribute to
the formation of atherosclerotic lesions [3]. In addition, CD36 of macro-
phages, together with TSP and the integrin alphav beta3, can phagocytose
apoptotic neutrophils [4]. Furthermore, the protein is one of the receptors
of collagen in platelet adhesion and aggregation [5,6]. CD36 can also
mediate cytoadherence of Plasmodium falciparum-infected erythrocytes to the
endothelium of post-capillary venules of different organs [7]. Moreover,
cytoplasmic CD36 plays an important role in signal transduction by inter-
acting with Src family tyrosine kinases [8]. Deficiency in CD36 in Asian
and African populations has been associated with insulin resistance [9].
Lysosome membrane protein II (LIMP II) is a 478-residue glycoprotein
expressed in the membrane of lysosomes and secretory granules with lysosomal
properties [10]. The N-terminal segment (residues ~4-26) constitute an
uncleavable signal peptide [10]. LIMP II possesses an additional C-terminal
hydrophobic region that, together with the signal peptide, may anchor the
protein to the membrane [10]. The major portion of the protein resides on
the luminal side and contains 11 potential N-glycosylation sites and 5
cysteine residues. The N- and C-terminal ends of the protein constitute
short cytoplasmic tails.
Comparison of the sequence to that of other lysosomal membrane glycoproteins
reveals no similarity. Glycine-tyrosine residues (the so-called GY motif),
believed to constitute an important signal for delivery of lysosomal
membrane glycoproteins to lysosomes, are not contained in the cytoplasmic
tail [11,12]. The protein thus appears to be a unique LIMP that does not
require tyrosine residues for targeting to lysosomes [11]. Sequence database
searches reveal extensive similarity between LIMP II and the cell surface
protein CD36 involved in cell adhesion [10].
CD36FAMILY is a 6-element fingerprint that provides a signature for the
adhesion molecule CD36 family. The fingerprint was derived from an initial
alignment of 6 sequences: the motifs were drawn from conserved regions
spanning the lumenal domain. Seven iterations on SPTR40_18f were required
to reach convergence, at which point a true set comprising 29 sequences
was identified. Several partial matches were also found, all of which are
proteins related to the CD36 family that fail to make significant matches
with one or more motifs.
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