Evidence for clustered mannose as a new ligand for hyaluronan- binding protein (HABP1) from human fibroblasts.
We have earlier reported that overexpression of the gene encoding human hyaluronan-binding protein (HABP1) is functionally active, as it binds specifically with hyaluronan (HA). In this communication, we confirm the collapse of the filamentous and branched structure of HA by interaction with increasing concentrations of recombinant-HABP1 (rHABP1). HA is the reported ligand of rHABP1. Here, we show the affinity of rHABP1 towards D-mannosylated albumin (DMA) by overlay assay and purification using a DMA affinity column. Our data suggests that DMA is another ligand for HABP1. Furthermore, we have observed that DMA inhibits the binding of HA in a concentration-dependent manner, suggesting its multiligand affinity amongst carbohydrates. rHABP1 shows differential affinity towards HA and DMA which depends on pH and ionic strength. These data suggest that affinity of rHABP1 towards different ligands is regulated by the microenvironment.
Kumar
R
R
Biochemistry Laboratory, School of Environmental Sciences, Jawaharlal Nehru University, New Delhi 110 067, India.
Choudhury
N R
NR
Salunke
D M
DM
Datta
K
K
D000818:Animals; D004800:Enzymes, Immobilized / Q000378:metabolism; D005347:Fibroblasts / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D018960:Hyaluronan Receptors / Q000378:metabolism*; D006820:Hyaluronic Acid / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008358:Mannose / Q000737:chemistry* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012685:Sepharose / Q000737:chemistry; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism
D004800:Enzymes, Immobilized; D018960:Hyaluronan Receptors; D008024:Ligands; D011994:Recombinant Proteins; D012709:Serum Albumin; C023840:mannose-bovine serum albumin conjugate; D006820:Hyaluronic Acid; D012685:Sepharose; D008358:Mannose